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Conserved domains on  [gi|515624630|ref|WP_017057230|]
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MULTISPECIES: bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL [Vibrio]

Protein Classification

23S rRNA (guanine(2445)-N(2))/(guanine(2069)-N(7))-methyltransferase( domain architecture ID 11485505)

ribosomal RNA large subunit methyltransferase K/L is a class I SAM-dependent rRNA methyltransferase that methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of the 23S rRNA

EC:  2.1.1.173|2.1.1.264
Gene Ontology:  GO:0070043|GO:0003723

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 1-706 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: 1306.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   1 MNQYLAVTSNGLENLLVEELTQLGITNAKPVQAGVKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDMDLYLSTTAVN 80
Cdd:PRK11783   1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  81 WVNQFHSSKRFVVDFNGTNNEIRNSQYGAMKVKDAVVDCFEKKSLPRPSISKENPDVRIHVRLHRDKAILGVDMVGSGLH 160
Cdd:PRK11783  81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 161 QRGYRPESGRAPLRETLAAAILIRSGW-DATKPFLDPMCGSGTLVIEAAMMAANMAPGVKRQKWCFESLEDFEPELWAEV 239
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 240 KAEANVQGRRGVKKVECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPT-EFTDGVIVSNPPYGERLGTE 318
Cdd:PRK11783 241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLpKGPTGLVISNPPYGERLGEE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 319 PGLIALYTAFGAQLKAEFGGCNASIFSSSDELLSCLRMRADKQFKLNNGALPCHQKNYSISDRPMSERPTGeqeqliAPD 398
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDAEG------AQD 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 399 FANRLKKNIGKIGKWAKKEQLDCYRIYDADLPEYNVAIDVYPGHLVIQEYAAPKDVPEDKAKRRLTDIIRAAIQVTGVEA 478
Cdd:PRK11783 395 FANRLRKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPP 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 479 NNVVLKVRQKQKGRSQYQKMAQDSSNLEVNEYGVKLIVNLHDYLDTGLFLDHKITRRRIGEMAAGKDFLNLFAYTGSASV 558
Cdd:PRK11783 475 NKVVLKTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASV 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 559 HAAVGGARSTTTVDMSNTYLEWAKQNMELNGRVGRQHQFVQADCLQWLVKEQGSYDLIFIDPPTFSNSKRMDQSFDVQRD 638
Cdd:PRK11783 555 HAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRD 634

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624630 639 HIQLMENLKRLLREEGTIVFSNNKRHFKMDLEGLEALGLKAQNISAKTLPLDFSRNKHIHNCWLITHK 706
Cdd:PRK11783 635 HVALIKDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
 
Name Accession Description Interval E-value
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 1-706 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: 1306.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   1 MNQYLAVTSNGLENLLVEELTQLGITNAKPVQAGVKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDMDLYLSTTAVN 80
Cdd:PRK11783   1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  81 WVNQFHSSKRFVVDFNGTNNEIRNSQYGAMKVKDAVVDCFEKKSLPRPSISKENPDVRIHVRLHRDKAILGVDMVGSGLH 160
Cdd:PRK11783  81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 161 QRGYRPESGRAPLRETLAAAILIRSGW-DATKPFLDPMCGSGTLVIEAAMMAANMAPGVKRQKWCFESLEDFEPELWAEV 239
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 240 KAEANVQGRRGVKKVECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPT-EFTDGVIVSNPPYGERLGTE 318
Cdd:PRK11783 241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLpKGPTGLVISNPPYGERLGEE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 319 PGLIALYTAFGAQLKAEFGGCNASIFSSSDELLSCLRMRADKQFKLNNGALPCHQKNYSISDRPMSERPTGeqeqliAPD 398
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDAEG------AQD 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 399 FANRLKKNIGKIGKWAKKEQLDCYRIYDADLPEYNVAIDVYPGHLVIQEYAAPKDVPEDKAKRRLTDIIRAAIQVTGVEA 478
Cdd:PRK11783 395 FANRLRKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPP 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 479 NNVVLKVRQKQKGRSQYQKMAQDSSNLEVNEYGVKLIVNLHDYLDTGLFLDHKITRRRIGEMAAGKDFLNLFAYTGSASV 558
Cdd:PRK11783 475 NKVVLKTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASV 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 559 HAAVGGARSTTTVDMSNTYLEWAKQNMELNGRVGRQHQFVQADCLQWLVKEQGSYDLIFIDPPTFSNSKRMDQSFDVQRD 638
Cdd:PRK11783 555 HAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRD 634

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624630 639 HIQLMENLKRLLREEGTIVFSNNKRHFKMDLEGLEALGLKAQNISAKTLPLDFSRNKHIHNCWLITHK 706
Cdd:PRK11783 635 HVALIKDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 2-372 1.76e-163

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: 474.97  E-value: 1.76e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   2 NQYLAVTSNGLENLLVEELTQLGITNAKPVQAGVKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDMDLYLSTTAVNW 81
Cdd:COG0116    1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  82 VNQFHSSKRFVVDFNGTNNEIRNSQYGAMKVKDAVVDCFEKKSLPRPSISKENPDVRIHVRLHRDKAILGVDMVGSGLHQ 161
Cdd:COG0116   81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 162 RGYRPESGRAPLRETLAAAILIRSGWDATKPFLDPMCGSGTLVIEAAMMAANMAPGVKRqKWCFESLEDFEPELWAEVKA 241
Cdd:COG0116  161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR-DFAFEKWPDFDAELWQELRE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 242 EANVQGRRgvkKVECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPTEftDGVIVSNPPYGERLGTEPGL 321
Cdd:COG0116  240 EAEARIKR---DPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAE--PGLIITNPPYGERLGEEEEL 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515624630 322 IALYTAFGAQLKAEFGGCNASIFSSSDELLSCLRMRADKQFKLNNGALPCH 372
Cdd:COG0116  315 EALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECR 365
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 162-375 6.29e-56

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: 188.72  E-value: 6.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  162 RGYRPESGRAPLRETLAAAILIRSGWDATKPFLDPMCGSGTLVIEAAMMAANMAPGvkrqkwcfesLEDFEPELwaevka 241
Cdd:pfam01170   1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPG----------KFDARVRA------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  242 eanvqgrrgvkkvecKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPTEFTDgVIVSNPPYGERLGTEPGL 321
Cdd:pfam01170  65 ---------------PLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVD-VIVTNPPYGIRLGSKGAL 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 515624630  322 IALYTAFGAQLKAEF--GGCNASIFSSSDELLSCLRMRADKQFKLNNGALPCHQKN 375
Cdd:pfam01170 129 EALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 4-156 2.19e-47

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: 164.29  E-value: 2.19e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   4 YLAVTSNGLENLLVEELTQLGITNAKPVQAGVKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDMDLYLSTTAVNWVN 83
Cdd:cd11715    1 FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624630  84 QFHSSKRFVVDFNGTNNEIRNSQYGAMKVKDAVVDCFEKKsLPRPSISKENPDVRIHVRLHRDKAILGVDMVG 156
Cdd:cd11715   81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
4-328 4.22e-40

tRNA (guanine(6)-N2)-methyltransferase;


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 151.36  E-value: 4.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   4 YLAVTSNGLENLLVEELTQLGItNAKPVQAG---VKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDM-DLYLSTTAV 79
Cdd:NF040721   3 FYATLSPGLEKISAEEIEELGG-KIKEIREGkgrVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSLeDIYKRVYSI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  80 NW----VNQFHS--SKRfVVDFNGTNNEIrnsqygAMKVKDAVVDCFEKKSLPRPSISKENPDVRIHVRLHRDKAILGVD 153
Cdd:NF040721  82 DFsfikPEQSFAirPLR-VGEHDFTSIDI------GRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGID 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 154 MVG-SGLHQRGYRPESGRAPLRETLAAAILIRSGWDATKPFLDPMCGSGTLVIEAAMMAANMAPGVKRQKWCFESLEDFE 232
Cdd:NF040721 155 TTGdEGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKIFGHE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 233 PELWAEvkaeanvqgrrgvKKVECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPTEFTDgVIVSNPPYG 312
Cdd:NF040721 235 LLEKIK-------------KDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSVD-VIVTNPPYG 300

                        330
                 ....*....|....*.
gi 515624630 313 ERLGTEPGLIALYTAF 328
Cdd:NF040721 301 LRIGKKRIIKKLYNNF 316
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 68-153 1.47e-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: 1.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630    68 DDMDLYLSTTA-VNWVNQFHSSKRFVVDFNGTNNeirNSQYGAMKVKDAVVDCFeKKSLPRPSISKENPDVRIHVRLHRD 146
Cdd:smart00981   1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRGK---NHEFTSLEVKRAIGDKL-LEKTGGRKVDLKNPDVVIRVELRKD 76


                   ....*..
gi 515624630   147 KAILGVD 153
Cdd:smart00981  77 KAYLSID 83
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 130-328 7.56e-08

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: 54.75  E-value: 7.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  130 ISKENPDVRIHVRLHRDKAILGV---DMVGSGLHQR--GYRPESGRAPLRETLAAAILIRSGWDATKPFLDPMCGSGTLV 204
Cdd:TIGR01177 118 VSLRRPDIVVRVVITEDIFYLGRvleERDKEQFIERkpDRRPFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTGGFL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  205 IEAammaanmapgvkrqkwcfesledfepelwaevkaeanvqGRRGVKKveckfYGYDNDERMIKTARDNARRAGVEElI 284
Cdd:TIGR01177 198 IEA---------------------------------------GLMGAKV-----IGCDIDWKMVAGARINLEHYGIED-F 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 515624630  285 EFEVGDAAKLKRPTEFTDGvIVSNPPYGeRLGTEPG--LIALYTAF 328
Cdd:TIGR01177 233 FVKRGDATKLPLSSESVDA-IATDPPYG-RSTTAAGdgLESLYERS 276
 
Name Accession Description Interval E-value
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 1-706 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: 1306.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   1 MNQYLAVTSNGLENLLVEELTQLGITNAKPVQAGVKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDMDLYLSTTAVN 80
Cdd:PRK11783   1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  81 WVNQFHSSKRFVVDFNGTNNEIRNSQYGAMKVKDAVVDCFEKKSLPRPSISKENPDVRIHVRLHRDKAILGVDMVGSGLH 160
Cdd:PRK11783  81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 161 QRGYRPESGRAPLRETLAAAILIRSGW-DATKPFLDPMCGSGTLVIEAAMMAANMAPGVKRQKWCFESLEDFEPELWAEV 239
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 240 KAEANVQGRRGVKKVECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPT-EFTDGVIVSNPPYGERLGTE 318
Cdd:PRK11783 241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLpKGPTGLVISNPPYGERLGEE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 319 PGLIALYTAFGAQLKAEFGGCNASIFSSSDELLSCLRMRADKQFKLNNGALPCHQKNYSISDRPMSERPTGeqeqliAPD 398
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDAEG------AQD 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 399 FANRLKKNIGKIGKWAKKEQLDCYRIYDADLPEYNVAIDVYPGHLVIQEYAAPKDVPEDKAKRRLTDIIRAAIQVTGVEA 478
Cdd:PRK11783 395 FANRLRKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPP 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 479 NNVVLKVRQKQKGRSQYQKMAQDSSNLEVNEYGVKLIVNLHDYLDTGLFLDHKITRRRIGEMAAGKDFLNLFAYTGSASV 558
Cdd:PRK11783 475 NKVVLKTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASV 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 559 HAAVGGARSTTTVDMSNTYLEWAKQNMELNGRVGRQHQFVQADCLQWLVKEQGSYDLIFIDPPTFSNSKRMDQSFDVQRD 638
Cdd:PRK11783 555 HAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRD 634

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624630 639 HIQLMENLKRLLREEGTIVFSNNKRHFKMDLEGLEALGLKAQNISAKTLPLDFSRNKHIHNCWLITHK 706
Cdd:PRK11783 635 HVALIKDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 2-372 1.76e-163

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: 474.97  E-value: 1.76e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   2 NQYLAVTSNGLENLLVEELTQLGITNAKPVQAGVKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDMDLYLSTTAVNW 81
Cdd:COG0116    1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  82 VNQFHSSKRFVVDFNGTNNEIRNSQYGAMKVKDAVVDCFEKKSLPRPSISKENPDVRIHVRLHRDKAILGVDMVGSGLHQ 161
Cdd:COG0116   81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 162 RGYRPESGRAPLRETLAAAILIRSGWDATKPFLDPMCGSGTLVIEAAMMAANMAPGVKRqKWCFESLEDFEPELWAEVKA 241
Cdd:COG0116  161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR-DFAFEKWPDFDAELWQELRE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 242 EANVQGRRgvkKVECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPTEftDGVIVSNPPYGERLGTEPGL 321
Cdd:COG0116  240 EAEARIKR---DPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAE--PGLIITNPPYGERLGEEEEL 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515624630 322 IALYTAFGAQLKAEFGGCNASIFSSSDELLSCLRMRADKQFKLNNGALPCH 372
Cdd:COG0116  315 EALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECR 365
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 389-704 6.47e-121

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: 366.43  E-value: 6.47e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 389 GEQEQLIAPDFANRLKKNIGKIGKWAKKEQLDCYRIYDAD---LPeyNVAIDVYPGHLVIQEYAAPKDvpedkakRRLTD 465
Cdd:COG1092   66 DPDEPIDAAFFANRLRKALALRRKLAKREGTNAYRLVHGEadgLP--GLIVDRYGDVLVVQEYSAGME-------RRRDE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 466 IIRAAIQVTGVEAnnVVLKV---RQKQKGRSQYQKMA--QDSSNLEVNEYGVKLIVNLHDYLDTGLFLDHKITRRRIGEM 540
Cdd:COG1092  137 ILEALVEVLGPEG--IYLRSdvrVRQLEGLPQYEGVLygEAPEEVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAEL 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 541 AAGKDFLNLFAYTGSASVHAAVGGARSTTTVDMSNTYLEWAKQNMELNGrVGRQHQFVQADCLQWL---VKEQGSYDLIF 617
Cdd:COG1092  215 AKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNG-LDDRHEFVQADAFDWLrelAREGERFDLII 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 618 IDPPTFSNSKRmdQSFDVQRDHIQLMENLKRLLREEGTIVFSNNKRHFKMDL------EGLEALGLKAQNISAKTLPLDF 691
Cdd:COG1092  294 LDPPAFAKSKK--DLFDAQRDYKDLNRLALKLLAPGGILVTSSCSRHFSLDLfleilaRAARDAGRRVRIIERLTQPPDH 371

                        330
                 ....*....|....*...
gi 515624630 692 SRNKHIHN-----CWLIT 704
Cdd:COG1092  372 PVLPAFPEgeylkGLLLR 389
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 162-375 6.29e-56

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: 188.72  E-value: 6.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  162 RGYRPESGRAPLRETLAAAILIRSGWDATKPFLDPMCGSGTLVIEAAMMAANMAPGvkrqkwcfesLEDFEPELwaevka 241
Cdd:pfam01170   1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPG----------KFDARVRA------ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  242 eanvqgrrgvkkvecKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPTEFTDgVIVSNPPYGERLGTEPGL 321
Cdd:pfam01170  65 ---------------PLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVD-VIVTNPPYGIRLGSKGAL 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 515624630  322 IALYTAFGAQLKAEF--GGCNASIFSSSDELLSCLRMRADKQFKLNNGALPCHQKN 375
Cdd:pfam01170 129 EALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 4-156 2.19e-47

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: 164.29  E-value: 2.19e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   4 YLAVTSNGLENLLVEELTQLGITNAKPVQAGVKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDMDLYLSTTAVNWVN 83
Cdd:cd11715    1 FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624630  84 QFHSSKRFVVDFNGTNNEIRNSQYGAMKVKDAVVDCFEKKsLPRPSISKENPDVRIHVRLHRDKAILGVDMVG 156
Cdd:cd11715   81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
4-328 4.22e-40

tRNA (guanine(6)-N2)-methyltransferase;


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 151.36  E-value: 4.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   4 YLAVTSNGLENLLVEELTQLGItNAKPVQAG---VKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDM-DLYLSTTAV 79
Cdd:NF040721   3 FYATLSPGLEKISAEEIEELGG-KIKEIREGkgrVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSLeDIYKRVYSI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  80 NW----VNQFHS--SKRfVVDFNGTNNEIrnsqygAMKVKDAVVDCFEKKSLPRPSISKENPDVRIHVRLHRDKAILGVD 153
Cdd:NF040721  82 DFsfikPEQSFAirPLR-VGEHDFTSIDI------GRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGID 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 154 MVG-SGLHQRGYRPESGRAPLRETLAAAILIRSGWDATKPFLDPMCGSGTLVIEAAMMAANMAPGVKRQKWCFESLEDFE 232
Cdd:NF040721 155 TTGdEGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKIFGHE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 233 PELWAEvkaeanvqgrrgvKKVECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPTEFTDgVIVSNPPYG 312
Cdd:NF040721 235 LLEKIK-------------KDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSVD-VIVTNPPYG 300

                        330
                 ....*....|....*.
gi 515624630 313 ERLGTEPGLIALYTAF 328
Cdd:NF040721 301 LRIGKKRIIKKLYNNF 316
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
 408-657 1.68e-24

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: 104.19  E-value: 1.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  408 GKIGKWAKKEQLDCyriydadlpeynvaiDVYPGHLVIQEYAAPKDVPEDKAKRRLTDIIRAAIQVTGvEANNVVLKVRQ 487
Cdd:pfam10672   6 GRGRCWPGLEQLTC---------------DWLQGQLLVNLFKEVDPAFLQALKRGLEQLTTAPAWAAK-QGRHLVLQHRY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  488 KQKGRSQYQkMAQDSSNLEVNEYGVKLIVNLHDYLDTGLFLDHKITRRRIGEMAAGKDFLNLFAYTGSASVHAAVGGARS 567
Cdd:pfam10672  70 ADGAPSEVL-SGELLETPVVVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  568 TTTVDMSNTYLEWAKQNMELNGRVGRQHQFVQADCLQ-W-LVKEQGSYDLIFIDPPTFSNSkrmdqSFDVQRDHIQLMEN 645
Cdd:pfam10672 149 VVNVDMARGSLNKGRDNHRLNGHDLGRVSFLGHDIFKsWgKIKKLGPYDLVIIDPPSFQKG-----SFALTKDYKKILRR 223

                         250
                  ....*....|..
gi 515624630  646 LKRLLREEGTIV 657
Cdd:pfam10672 224 LPELLVEGGTVL 235
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
388-627 1.69e-19

23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 91.44  E-value: 1.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 388 TGEQEQLIAPDFANRLKKNIGKIGKW-AKKEQLDCYRIYDAD---LPeyNVAIDVYPGHLVIQEYAApkdvpedKAKRRL 463
Cdd:PRK15128  67 TFDPDESIDIAFFTRRLQQAQKWRDWlAQKDGLDSYRLIAGEsdgLP--GITIDRFGNFLVLQLLSA-------GAEYQR 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 464 TDIIrAAIQVTGVEA---NNVVLKVRQKQkGRSQYQKM---AQDSSNLEVNEYGVKLIVNLHDYLDTGLFLDHKITRRRI 537
Cdd:PRK15128 138 AALI-SALQTLYPECaiyDRSDVAVRKKE-GMELTQGPvtgELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLAT 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 538 GEMAAGKDFLNLFAYTGSASVHAAVGGARSTTTVDMSNTYLEWAKQNMELNGRVGRQHQFVQADCLQWL--VKEQG-SYD 614
Cdd:PRK15128 216 RRYVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLrtYRDRGeKFD 295

                        250
                 ....*....|...
gi 515624630 615 LIFIDPPTFSNSK 627
Cdd:PRK15128 296 VIVMDPPKFVENK 308
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 68-153 1.47e-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: 1.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630    68 DDMDLYLSTTA-VNWVNQFHSSKRFVVDFNGTNNeirNSQYGAMKVKDAVVDCFeKKSLPRPSISKENPDVRIHVRLHRD 146
Cdd:smart00981   1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRGK---NHEFTSLEVKRAIGDKL-LEKTGGRKVDLKNPDVVIRVELRKD 76


                   ....*..
gi 515624630   147 KAILGVD 153
Cdd:smart00981  77 KAYLSID 83
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
 5-148 4.79e-14

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: 69.82  E-value: 4.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   5 LAVTSNGLENLLVEELTQLGITNAKPV------QAGVKFKA-TNEQIYRCCLWSRLASRFVRVLseFTC-MDDMDLYLST 76
Cdd:cd11688    2 FATTGKGLEEILAAELYELLEVRGFDAeiqvvpHGRVHFKTdTDEAVYQLVMWSRLISRIMPPL--GECkADLEDLYETA 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515624630  77 TAVNWVNQFHSSKRFVVDFNGTNNEIRNSQYGAMKVKDAVVDCFEkkslprPSISKENPDVRIHVRLHRDKA 148
Cdd:cd11688   80 LEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFN------PEVDLDNPDIVVNVEVHKEIA 145
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 173-328 6.40e-11

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: 61.50  E-value: 6.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 173 LRETLAAAILIRSGWDATKPFLDPMCGSGTLVIeaammaanmapgvkrqkwcfesledfepelwaevkaEANVQGRRGvk 252
Cdd:COG1041   10 LDPRLARALVNLAGAKEGDTVLDPFCGTGTILI------------------------------------EAGLLGRRV-- 51

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515624630 253 kveckfYGYDNDERMIKTARDNARRAGVEElIEFEVGDAAKLKRPTEFTDgVIVSNPPYGERLGTEP-GLIALYTAF 328
Cdd:COG1041   52 ------IGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADESVD-AIVTDPPYGRSSKISGeELLELYEKA 120
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 31-153 2.66e-09

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: 56.29  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630   31 VQAGVKFKATNEQIYRCCLWSRLASRFVRVLSEFTCMDDMDLYLSttAVNWVNQFHSSKRFVVDFNGTNneiRNSQYGAM 110
Cdd:pfam02926  27 VLKGENPEEDRELLKEALEKAPGIERFPVAETCEADLEDILELAK--EIIKDKFKKEGETFAVRVKRRG---KNHEFTSL 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 515624630  111 KVKDAVVDCFEKKSLPRpsISKENPDVRIHVRLHRDKAILGVD 153
Cdd:pfam02926 102 EINREVGKAIVEKTGLK--VDLENPDIVVHVEIIKDKAYISID 142
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 130-328 7.56e-08

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: 54.75  E-value: 7.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  130 ISKENPDVRIHVRLHRDKAILGV---DMVGSGLHQR--GYRPESGRAPLRETLAAAILIRSGWDATKPFLDPMCGSGTLV 204
Cdd:TIGR01177 118 VSLRRPDIVVRVVITEDIFYLGRvleERDKEQFIERkpDRRPFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTGGFL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  205 IEAammaanmapgvkrqkwcfesledfepelwaevkaeanvqGRRGVKKveckfYGYDNDERMIKTARDNARRAGVEElI 284
Cdd:TIGR01177 198 IEA---------------------------------------GLMGAKV-----IGCDIDWKMVAGARINLEHYGIED-F 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 515624630  285 EFEVGDAAKLKRPTEFTDGvIVSNPPYGeRLGTEPG--LIALYTAF 328
Cdd:TIGR01177 233 FVKRGDATKLPLSSESVDA-IATDPPYG-RSTTAAGdgLESLYERS 276
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
543-664 6.77e-07

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 49.93  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  543 GKDFLNLFAYTGSASVHAAVGGARSTTTVDMSNTYLEWAKQNMELNGRVGrqHQFVQADCLQWLVKEQ--GSYDLIFIDP 620
Cdd:pfam03602  42 GARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQLLGLPG--AVLVMDALLALLRLAGkgPVFDIVFLDP 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 515624630  621 PTFSNskrmdqsfDVQRDhIQLMENlKRLLREEGTIVFSNNKRH 664
Cdd:pfam03602 120 PYAKG--------LIEEV-LDLLAE-KGWLKPNALIYVETEKRG 153
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 545-659 3.77e-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: 46.27  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 545 DFLNLFAYTGSASVHAAVGGARSTTTVDMSNTYLEWAKQNMELNGRVGRQhqFVQADCLQWLVKEQGSYDLIFIDPPTFS 624
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVE--VLKGDAEELPPEADESFDVIISDPPLHH 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515624630 625 nskrmdqsfdVQRDHIQLMENLKRLLREEGTIVFS 659
Cdd:cd02440   79 ----------LVEDLARFLEEARRLLKPGGVLVLT 103
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
249-312 7.59e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.21  E-value: 7.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515624630 249 RGVKKVeckfYGYDNDERMIKTARDNARRAGVEelIEFEVGDAAKLKRPTEFTdgVIVSNPPYG 312
Cdd:COG2263   66 LGAKKV----VGVDIDPEALEIARENAERLGVR--VDFIRADVTRIPLGGSVD--TVVMNPPFG 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 252-308 9.09e-06

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 9.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515624630  252 KKVECKFYGYDNDERMIKTARDNARRAGVEelIEFEVGDAAKLKRPTEFTDGVIVSN 308
Cdd:pfam13649  17 RRGGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGSFDLVVSSG 71
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 255-311 1.51e-05

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 47.45  E-value: 1.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515624630 255 ECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDA-AKLKRPTEFtDgVIVSNPPY 311
Cdd:COG2890  136 DARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLfEPLPGDGRF-D-LIVSNPPY 191
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 542-657 6.73e-05

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: 44.30  E-value: 6.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 542 AGKDFLNLFAYTGsasvhaAVG------GARSTTTVDMSNTYLEWAKQNME---LNGRVgrqhQFVQADCLQWLVKEQG- 611
Cdd:COG0742   41 EGARVLDLFAGSG------ALGlealsrGAASVVFVEKDRKAAAVIRKNLEklgLEDRA----RVIRGDALRFLKRLAGe 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515624630 612 SYDLIFIDPPtfsnskrmdqsFDVQrDHIQLMENL--KRLLREEGTIV 657
Cdd:COG0742  111 PFDLVFLDPP-----------YAKG-LLEKALELLaeNGLLAPGGLIV 146
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 256-311 1.41e-04

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 44.00  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 515624630  256 CKFYGYDNDERMIKTARDNARRAGVEElIEFEVGDAAklkrpTEFTDG---VIVSNPPY 311
Cdd:TIGR03534 111 ARVTAVDISPEALAVARKNARRLGLEN-VEFLQGDWF-----EPLPSGkfdLIVSNPPY 163
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
248-308 2.36e-04

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 43.62  E-value: 2.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624630 248 RRGVKKVeckfYGYDNDERMIKTARDNARRAGVEELIEFEVGDaakLKRPTEFtDgVIVSN 308
Cdd:COG2264  168 KLGAKRV----LAVDIDPVAVEAARENAELNGVEDRIEVVLGD---LLEDGPY-D-LVVAN 219
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 257-308 3.02e-04

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.60  E-value: 3.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515624630 257 KFYGYDNDERMIKTARDNARRAGVEElIEFEVGDAAKLK-RPTEFTDGVIVSN 308
Cdd:COG0500   51 RVIGIDLSPEAIALARARAAKAGLGN-VEFLVADLAELDpLPAESFDLVVAFG 102
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 256-308 3.77e-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: 41.13  E-value: 3.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515624630 256 CKFYGYDNDERMIKTARDNARRAGVEelIEFEVGDAAKLKRPTEFTDGVIVSN 308
Cdd:COG2226   45 ARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGSFDLVISSF 95
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
596-701 4.37e-04

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 42.60  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 596 QFVQADCLQWLVK-EQGSYDLIFIDPP-----TFSNSKRMDQSFDVQRDHI----QLMENLKRLLREEGTIVFSNNKRHF 665
Cdd:COG0863    1 RLICGDCLEVLKElPDESVDLIVTDPPynlgkKYGLGRREIGNELSFEEYLeflrEWLAECYRVLKPGGSLYVNIGDRYI 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515624630 666 KMDLEGLEALGLKAQN--ISAKTLPLDFSRNKHIHNCW 701
Cdd:COG0863   81 SRLIAALRDAGFKLRNeiIWRKPNGVPGPSKRRFRNSH 118
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 569-660 5.62e-04

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: 41.32  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 569 TTVDMSNTYLEWAKQNME---LNGRVgrqhQFVQADCLQWLVK-EQGSYDLIFIDpptfsnskrmdqsfdVQRDH-IQLM 643
Cdd:COG4122   45 TTIEIDPERAAIARENFAragLADRI----RLILGDALEVLPRlADGPFDLVFID---------------ADKSNyPDYL 105

                         90
                 ....*....|....*..
gi 515624630 644 ENLKRLLREEGTIVFSN 660
Cdd:COG4122  106 ELALPLLRPGGLIVADN 122
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 255-308 6.27e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.86  E-value: 6.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515624630  255 ECKFYGYDNDERMIKTARDNARRAGVEElIEFEVGDAAKLkrPTEFTDG---VIVSN 308
Cdd:pfam13847  28 NAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEEL--PELLEDDkfdVVISN 81
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 255-311 6.64e-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: 42.05  E-value: 6.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 255 ECKFYGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRptEFTDG---VIVSNPPY 311
Cdd:COG4123   61 GARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAA--ELPPGsfdLVVSNPPY 118
arsM PRK11873
arsenite methyltransferase;
257-308 6.64e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 42.24  E-value: 6.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515624630 257 KFYGYDNDERMIKTARDNARRAGVEElIEFEVGDAAKLKRPTEFTDgVIVSN 308
Cdd:PRK11873 104 KVIGVDMTPEMLAKARANARKAGYTN-VEFRLGEIEALPVADNSVD-VIISN 153
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 553-654 1.01e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 38.70  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  553 TGSASVHAAVGGARSTTTVDMSNTYLEWAKQNMELNG-RVgrqhQFVQADCLQWLVKEqGSYDLIFidpptfsnskrmdq 631
Cdd:pfam13649   8 TGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGlNV----EFVQGDAEDLPFPD-GSFDLVV-------------- 68

                          90       100
                  ....*....|....*....|....*...
gi 515624630  632 SFDV-----QRDHIQLMENLKRLLREEG 654
Cdd:pfam13649  69 SSGVlhhlpDPDLEAALREIARVLKPGG 96
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 262-291 1.41e-03

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 40.17  E-value: 1.41e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 515624630 262 DNDERMIKTARDNARRAGVEELIEFEVGDA 291
Cdd:COG4122   48 EIDPERAAIARENFARAGLADRIRLILGDA 77
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 259-306 1.75e-03

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 40.53  E-value: 1.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 515624630 259 YGYDNDERMIKTARDNARRAGVEELIEFEVGDAAKLKRPTEFtDGVIV 306
Cdd:COG2519  120 YSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIDEGDV-DAVFL 166
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 256-311 2.30e-03

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: 38.18  E-value: 2.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515624630 256 CKFYGYDNDERMIKTARDNARRAGvEELIEFEVGDAAKL--KRPTEFTdgVIVSNPPY 311
Cdd:cd02440   22 ARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELppEADESFD--VIISDPPL 76
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
 547-621 2.33e-03

16S rRNA m(2)G966-methyltransferase; Provisional


Pssm-ID: 236793  Cd Length: 199  Bit Score: 39.70  E-value: 2.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624630 547 LNLFAYTGSASVHAAVGGARSTTTVDMSNTYLEWAKQNMEL----NGRVgrqhqfVQADCLQWLVKEQGSYDLIFIDPP 621
Cdd:PRK10909  58 LDCFAGSGALGLEALSRYAAGATLLEMDRAVAQQLIKNLATlkagNARV------VNTNALSFLAQPGTPHNVVFVDPP 130
PRK14967 PRK14967
putative methyltransferase; Provisional
 543-621 3.96e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 3.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624630 543 GKDFLNLFAYTGSASVHAAVGGARSTTTVDMSNTYLEWAKQNMELNGRVGRQHQFVQADCLQWlvkeqGSYDLIFIDPP 621
Cdd:PRK14967  37 GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEF-----RPFDVVVSNPP 110
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 255-311 4.22e-03

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 39.02  E-value: 4.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515624630 255 ECKFYGYDNDERMIKTARDNARRAGVEElIEFEVGDAAKLKRPTEFTdgVIVSNPPY 311
Cdd:COG2813   73 EARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSGVPDGSFD--LILSNPPF 126
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
239-318 8.66e-03

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 38.63  E-value: 8.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630 239 VKAEANVQGRRGVKKVECKFYGYDNDERMIKTARDNARRAGVEElIEFEVGDA--AKLKRPTEFTdgVIVSNPPYGERLG 316
Cdd:COG0286   59 VEAAEYLKEHGGDERKKLSLYGQEINPTTYRLAKMNLLLHGIGD-PNIELGDTlsNDGDELEKFD--VVLANPPFGGKWK 135


                 ..
gi 515624630 317 TE 318
Cdd:COG0286  136 KE 137
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 250-308 8.91e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 38.79  E-value: 8.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624630  250 GVKKVeckfYGYDNDERMIKTARDNARRAGVEELIEFEV-GDAAKLKRPteftdgVIVSN 308
Cdd:pfam06325 183 GAKKV----VGVDIDPVAVRAAKENAELNGVEARLEVYLpGDLPKEKAD------VVVAN 232
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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