|
Name |
Accession |
Description |
Interval |
E-value |
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
38-404 |
0e+00 |
|
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: 514.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 38 YRLVAKTFQGLEDVLAEELAHIGATGVEKQNRAVLFNGDKAMMYRANYQLRTAISILKPIASFTANDEDALYKEISRINW 117
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 118 ANYMTTEETFSVAAVTFSKVFNHSKFVSLKVKDAIVDQFRRRKGKRPDVDTQDPDLKIHIHITETHCDLLLDSSGDPLFK 197
Cdd:COG0116 81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 198 RGYRVKTTKAPINEVLAAGMIKLSGWNMDCDFYDPMCGSGTILIEAAMTAHGIAPGTYREkFGFESWKDFDSDLFGEISE 277
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNRD-FAFEKWPDFDAELWQELRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 278 ESFG--TPDFKHKILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLKPKTENGFMITNPPYGERL-QPDDLKIFYQ 354
Cdd:COG0116 240 EAEAriKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYGERLgEEEELEALYR 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1082600545 355 KIGDKLKIDFTGFTSWIIGSNADVMKFLGLKPEKKIKLFNGPLECTFRKY 404
Cdd:COG0116 320 ELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
37-408 |
7.72e-123 |
|
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: 371.83 E-value: 7.72e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 37 QYRLVAKTFQGLEDVLAEELAHIGATGVEKQNRAVLFNGDKAMMYRANYQLRTAISILKPIASFTANDEDALYKEISRIN 116
Cdd:PRK11783 1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 117 WANYMTTEETFSVAAVTFSKVFNHSKFVSLKVKDAIVDQFRRRKGKRPDVDTQDPDLKIHIHITETHCDLLLDSSGDPLF 196
Cdd:PRK11783 81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 197 KRGYRVKTTKAPINEVLAAGMIKLSGW-NMDCDFYDPMCGSGTILIEAAMTAHGIAPGTYREKFGFESWKDFDSDLFGEI 275
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 276 SEE-----SFGTPDFKHKILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLK---PKTENGFMITNPPYGERL-QP 346
Cdd:PRK11783 241 LEEaqeraRAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKnplPKGPTGLVISNPPYGERLgEE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082600545 347 DDLKIFYQKIGDKLKIDFTGFTSWIIGSNADVMKFLGLKPEKKIKLFNGPLECTFRKYSVYE 408
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAE 382
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
40-192 |
1.65e-55 |
|
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: 180.47 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 40 LVAKTFQGLEDVLAEELAHIGATGVEKQNRAVLFNGDKAMMYRANYQLRTAISILKPIASFTANDEDALYKEISRINWAN 119
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082600545 120 YMTTEETFSVAAVTFSKVFNHSKFVSLKVKDAIVDQFrRRKGKRPDVDTQDPDLKIHIHITETHCDLLLDSSG 192
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
47-344 |
7.18e-43 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 154.06 E-value: 7.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 47 GLEDVLAEELAHIGATGVEKQ--NRAVLFNGDKAMMYRANYQLRTAISILKPIASFTANDE-DALYKEISRINWAnYMTT 123
Cdd:NF040721 10 GLEKISAEEIEELGGKIKEIRegKGRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSlEDIYKRVYSIDFS-FIKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 124 EETFSVAAVtfsKVFNHSkFVSLKVK----DAIVDQFRRRKGKRPDVDTQDPDLKIHIHITETHCDLLLDSSGD-PLFKR 198
Cdd:NF040721 89 EQSFAIRPL---RVGEHD-FTSIDIGrvagEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGDeGLHKR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 199 GYRVKTTKAPINEVLAAGMIKLSGWNMDCDFYDPMCGSGTILIEAAMTAHGIAPGTYREKFGFEswKDFDSDLFGEISEe 278
Cdd:NF040721 165 GYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFK--KIFGHELLEKIKK- 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082600545 279 sfgtpDFKHKILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLKPKTEN-GFMITNPPYGERL 344
Cdd:NF040721 242 -----DVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSvDVIVTNPPYGLRI 303
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
198-403 |
7.95e-37 |
|
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: 132.48 E-value: 7.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 198 RGYRVKTTKAPINEVLAAGMIKLSGWNMDCDFYDPMCGSGTILIEAAMTAHGIAPGTYREKfgfeswkdfdsdlfgeise 277
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDAR------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 278 esfgtpdFKHKILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLK-PKTENGFMITNPPYGERL-QPDDLKIFYQK 355
Cdd:pfam01170 62 -------VRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPlLEGSVDVIVTNPPYGIRLgSKGALEALYPE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1082600545 356 IGDKLKIDFTGfTSW---IIGSNADVMKFLGLKPEKKIKLFNGPLECTFRK 403
Cdd:pfam01170 135 FLREAKRVLRG-GGWlvlLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
104-186 |
3.94e-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: 64.60 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 104 DEDALYKEISR-INWANYMTTEETFsvaAVTFSKVFNHSKFVSLKVKDAIVDQFRRRKGKRPdVDTQDPDLKIHIHITET 182
Cdd:smart00981 1 DLEDLYETALElIRWEKIFKEGKTF---AVRAKRRGKNHEFTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKD 76
|
....
gi 1082600545 183 HCDL 186
Cdd:smart00981 77 KAYL 80
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
288-340 |
3.13e-05 |
|
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]
Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 45.42 E-value: 3.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1082600545 288 KILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLKPKTENGFMITNPPY 340
Cdd:TIGR00536 140 EVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKIDIIVSNPPY 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
38-404 |
0e+00 |
|
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: 514.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 38 YRLVAKTFQGLEDVLAEELAHIGATGVEKQNRAVLFNGDKAMMYRANYQLRTAISILKPIASFTANDEDALYKEISRINW 117
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 118 ANYMTTEETFSVAAVTFSKVFNHSKFVSLKVKDAIVDQFRRRKGKRPDVDTQDPDLKIHIHITETHCDLLLDSSGDPLFK 197
Cdd:COG0116 81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 198 RGYRVKTTKAPINEVLAAGMIKLSGWNMDCDFYDPMCGSGTILIEAAMTAHGIAPGTYREkFGFESWKDFDSDLFGEISE 277
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNRD-FAFEKWPDFDAELWQELRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 278 ESFG--TPDFKHKILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLKPKTENGFMITNPPYGERL-QPDDLKIFYQ 354
Cdd:COG0116 240 EAEAriKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYGERLgEEEELEALYR 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1082600545 355 KIGDKLKIDFTGFTSWIIGSNADVMKFLGLKPEKKIKLFNGPLECTFRKY 404
Cdd:COG0116 320 ELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
37-408 |
7.72e-123 |
|
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: 371.83 E-value: 7.72e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 37 QYRLVAKTFQGLEDVLAEELAHIGATGVEKQNRAVLFNGDKAMMYRANYQLRTAISILKPIASFTANDEDALYKEISRIN 116
Cdd:PRK11783 1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 117 WANYMTTEETFSVAAVTFSKVFNHSKFVSLKVKDAIVDQFRRRKGKRPDVDTQDPDLKIHIHITETHCDLLLDSSGDPLF 196
Cdd:PRK11783 81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 197 KRGYRVKTTKAPINEVLAAGMIKLSGW-NMDCDFYDPMCGSGTILIEAAMTAHGIAPGTYREKFGFESWKDFDSDLFGEI 275
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 276 SEE-----SFGTPDFKHKILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLK---PKTENGFMITNPPYGERL-QP 346
Cdd:PRK11783 241 LEEaqeraRAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKnplPKGPTGLVISNPPYGERLgEE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082600545 347 DDLKIFYQKIGDKLKIDFTGFTSWIIGSNADVMKFLGLKPEKKIKLFNGPLECTFRKYSVYE 408
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAE 382
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
40-192 |
1.65e-55 |
|
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: 180.47 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 40 LVAKTFQGLEDVLAEELAHIGATGVEKQNRAVLFNGDKAMMYRANYQLRTAISILKPIASFTANDEDALYKEISRINWAN 119
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082600545 120 YMTTEETFSVAAVTFSKVFNHSKFVSLKVKDAIVDQFrRRKGKRPDVDTQDPDLKIHIHITETHCDLLLDSSG 192
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
47-344 |
7.18e-43 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 154.06 E-value: 7.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 47 GLEDVLAEELAHIGATGVEKQ--NRAVLFNGDKAMMYRANYQLRTAISILKPIASFTANDE-DALYKEISRINWAnYMTT 123
Cdd:NF040721 10 GLEKISAEEIEELGGKIKEIRegKGRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSlEDIYKRVYSIDFS-FIKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 124 EETFSVAAVtfsKVFNHSkFVSLKVK----DAIVDQFRRRKGKRPDVDTQDPDLKIHIHITETHCDLLLDSSGD-PLFKR 198
Cdd:NF040721 89 EQSFAIRPL---RVGEHD-FTSIDIGrvagEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGDeGLHKR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 199 GYRVKTTKAPINEVLAAGMIKLSGWNMDCDFYDPMCGSGTILIEAAMTAHGIAPGTYREKFGFEswKDFDSDLFGEISEe 278
Cdd:NF040721 165 GYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFK--KIFGHELLEKIKK- 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082600545 279 sfgtpDFKHKILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLKPKTEN-GFMITNPPYGERL 344
Cdd:NF040721 242 -----DVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSvDVIVTNPPYGLRI 303
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
198-403 |
7.95e-37 |
|
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: 132.48 E-value: 7.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 198 RGYRVKTTKAPINEVLAAGMIKLSGWNMDCDFYDPMCGSGTILIEAAMTAHGIAPGTYREKfgfeswkdfdsdlfgeise 277
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDAR------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 278 esfgtpdFKHKILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLK-PKTENGFMITNPPYGERL-QPDDLKIFYQK 355
Cdd:pfam01170 62 -------VRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPlLEGSVDVIVTNPPYGIRLgSKGALEALYPE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1082600545 356 IGDKLKIDFTGfTSW---IIGSNADVMKFLGLKPEKKIKLFNGPLECTFRK 403
Cdd:pfam01170 135 FLREAKRVLRG-GGWlvlLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
104-186 |
3.94e-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: 64.60 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 104 DEDALYKEISR-INWANYMTTEETFsvaAVTFSKVFNHSKFVSLKVKDAIVDQFRRRKGKRPdVDTQDPDLKIHIHITET 182
Cdd:smart00981 1 DLEDLYETALElIRWEKIFKEGKTF---AVRAKRRGKNHEFTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKD 76
|
....
gi 1082600545 183 HCDL 186
Cdd:smart00981 77 KAYL 80
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
209-341 |
1.48e-12 |
|
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 65.36 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 209 INEVLAAGMIKLSGWNMDCDFYDPMCGSGTILIEAAMtaHGIapgtyrekfgfeswkdfdsdlfgeiseesfgtpdfkhK 288
Cdd:COG1041 10 LDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGL--LGR-------------------------------------R 50
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1082600545 289 ILGSDISPLAIKIAEENIaKAFLTKKISVAPKNFFDLKPKTEN-GFMITNPPYG 341
Cdd:COG1041 51 VIGSDIDPKMVEGARENL-EHYGYEDADVIRGDARDLPLADESvDAIVTDPPYG 103
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
73-190 |
2.26e-08 |
|
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: 52.83 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 73 FNGDKAMMYRANYQLRTAISIlkPIASFTANDEDALYKEISRINWANYMTTEETFsvaAVTFSKVFNHSKFVSLKVKDAI 152
Cdd:pfam02926 33 PEEDRELLKEALEKAPGIERF--PVAETCEADLEDILELAKEIIKDKFKKEGETF---AVRVKRRGKNHEFTSLEINREV 107
|
90 100 110
....*....|....*....|....*....|....*...
gi 1082600545 153 VDQFRRRKGKRpdVDTQDPDLKIHIHITETHCDLLLDS 190
Cdd:pfam02926 108 GKAIVEKTGLK--VDLENPDIVVHVEIIKDKAYISIDR 143
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
288-340 |
3.13e-05 |
|
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]
Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 45.42 E-value: 3.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1082600545 288 KILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLKPKTENGFMITNPPY 340
Cdd:TIGR00536 140 EVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKIDIIVSNPPY 192
|
|
| THUMP |
cd11688 |
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ... |
40-179 |
1.06e-04 |
|
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: 42.09 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 40 LVAKTFQGLEDVLAEELAHIGATGVEKQNRAVLFNGDKAMM---YRANYQL----RTAISILKPIASFTANDEDaLYKEI 112
Cdd:cd11688 1 VFATTGKGLEEILAAELYELLEVRGFDAEIQVVPHGRVHFKtdtDEAVYQLvmwsRLISRIMPPLGECKADLED-LYETA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082600545 113 SRINWANYMTTEETFSVAAVTFSKVFNHSKFVSLKVKDAIVDQFrrrkgkRPDVDTQDPDLKIHIHI 179
Cdd:cd11688 80 LEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAF------NPEVDLDNPDIVVNVEV 140
|
|
| HsdM |
COG0286 |
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms]; |
230-364 |
3.69e-04 |
|
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
Pssm-ID: 440055 [Multi-domain] Cd Length: 243 Bit Score: 41.71 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082600545 230 YDPMCGSGTILIEAAmtahgiapgtyreKFGFESWKDFDSDLfgeiseesfgtpdfkhKILGSDISPLAIKIA------- 302
Cdd:COG0286 48 YDPACGSGGFLVEAA-------------EYLKEHGGDERKKL----------------SLYGQEINPTTYRLAkmnlllh 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082600545 303 ---EENIAKA-FLTKKISvaPKNFFDlkpktengFMITNPPYG-----ERLQPDDLKIFYQKIGDKLKIDF 364
Cdd:COG0286 99 gigDPNIELGdTLSNDGD--ELEKFD--------VVLANPPFGgkwkkEELKDDLLGRFGYGLPPKSNADL 159
|
|
| PRK01544 |
PRK01544 |
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ... |
288-340 |
1.94e-03 |
|
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed
Pssm-ID: 234958 [Multi-domain] Cd Length: 506 Bit Score: 40.23 E-value: 1.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1082600545 288 KILGSDISPLAIKIAEENIAKAFLTKKISVAPKNFFDLKPKTENGFMITNPPY 340
Cdd:PRK01544 164 NVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFENIEKQKFDFIVSNPPY 216
|
|
| |
