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Conserved domains on  [gi|16128915|ref|NP_415468|]
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fused 23S rRNA m(2)G2445 methyltransferase and 23S rRNA m(7)G2069 methyltransferase [Escherichia coli str. K-12 substr. MG1655]

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

Gene Ontology:  GO:0070043|GO:0003723

Graphical summary

 Zoom to residue level

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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)) ...
1-702 0e+00

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


:

Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 1393.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915    1 MNSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAIN 80
Cdd:PRK11783   1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   81 WTEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLH 160
Cdd:PRK11783  81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  161 LRGYRDRAGIAPIKETLAAAIVMRSGW-QPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEV 239
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  240 KAEAQTRARKGLAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTNPLPKGPYGTVLSNPPYGERLDSE 319
Cdd:PRK11783 241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  320 PALIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKNYHVAEStPDSKPAMVAEDYTNRL 399
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEE-STSSDAEGAQDFANRL 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  400 RKNLKKFEKWARQEGIECYRLYDADLPEYNVAVDRYADWVVVQEYAPPKTIDAHKARQRLFDIIAATISVLGIAPNKLVL 479
Cdd:PRK11783 400 RKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVL 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  480 KTRERQKGKNQYQKLGEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDFLNLFSYTGSATVHAGLG 559
Cdd:PRK11783 480 KTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALG 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  560 GARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWLREANEQFDLIFIDPPTFSNSKRMEDAFDVQRDHLALM 639
Cdd:PRK11783 560 GAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRDHVALI 639
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128915  640 KDLKRLLRAGGTIMFSNNKRGFRMDLDGLAKLGLKAQEITQKTLSQDFARNRQIHNCWLITAA 702
Cdd:PRK11783 640 KDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
 
Name Accession Description Interval E-value
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
1-702 0e+00

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 1393.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915    1 MNSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAIN 80
Cdd:PRK11783   1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   81 WTEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLH 160
Cdd:PRK11783  81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  161 LRGYRDRAGIAPIKETLAAAIVMRSGW-QPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEV 239
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  240 KAEAQTRARKGLAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTNPLPKGPYGTVLSNPPYGERLDSE 319
Cdd:PRK11783 241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  320 PALIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKNYHVAEStPDSKPAMVAEDYTNRL 399
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEE-STSSDAEGAQDFANRL 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  400 RKNLKKFEKWARQEGIECYRLYDADLPEYNVAVDRYADWVVVQEYAPPKTIDAHKARQRLFDIIAATISVLGIAPNKLVL 479
Cdd:PRK11783 400 RKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVL 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  480 KTRERQKGKNQYQKLGEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDFLNLFSYTGSATVHAGLG 559
Cdd:PRK11783 480 KTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALG 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  560 GARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWLREANEQFDLIFIDPPTFSNSKRMEDAFDVQRDHLALM 639
Cdd:PRK11783 560 GAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRDHVALI 639
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128915  640 KDLKRLLRAGGTIMFSNNKRGFRMDLDGLAKLGLKAQEITQKTLSQDFARNRQIHNCWLITAA 702
Cdd:PRK11783 640 KDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
2-372 8.36e-165

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 478.06  E-value: 8.36e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   2 NSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINW 81
Cdd:COG0116   1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  82 TEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLHL 161
Cdd:COG0116  81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 162 RGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRgRWGFSGWAQHDEAIWQEVKA 241
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR-DFAFEKWPDFDAELWQELRE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 242 EAQTRARKGLAeysSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTnplPKGPYGTVLSNPPYGERLDSEPA 321
Cdd:COG0116 240 EAEARIKRDPP---LPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLE---PPAEPGLIITNPPYGERLGEEEE 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 16128915 322 LIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDC 372
Cdd:COG0116 314 LEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLEC 364
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
162-376 1.85e-69

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 224.93  E-value: 1.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   162 RGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRgrwgfsgwaqhdeaiwqevka 241
Cdd:pfam01170   1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFD--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   242 eaqtrarkglAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLtnPLPKGPYGTVLSNPPYGERLDSEPA 321
Cdd:pfam01170  60 ----------ARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADL--PLLEGSVDVIVTNPPYGIRLGSKGA 127
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128915   322 LIALHSLLGRIMKNQF--GGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKN 376
Cdd:pfam01170 128 LEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
24-156 2.10e-46

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 161.59  E-value: 2.10e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  24 GAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINWTEMFNPGATFAVHFSGLNDTIR 103
Cdd:cd11715  21 GAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWEDYLDPDGTFAVRATRVGSKLF 100
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16128915 104 NSQYGAMKVKDAIVDAFtRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSG 156
Cdd:cd11715 101 HSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
33-316 8.76e-36

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


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 139.04  E-value: 8.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   33 GGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDL-DLYLGVQAINWTEMfNPGATFAVHFSGLNDTIRNSQYGAMK 111
Cdd:NF040721  34 GRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSLeDIYKRVYSIDFSFI-KPEQSFAIRPLRVGEHDFTSIDIGRV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  112 VKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGD-GLHLRGYRDRAGIAPIKETLAAAIVMRSGWQPG 190
Cdd:NF040721 113 AGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGDeGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDE 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  191 TPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEvkaeaqtrarkglAEYSSHFYGSDSDARVIQR 270
Cdd:NF040721 193 ESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKIFGHELLEKIK-------------KDVELKIYGIEKFRKHLEG 259
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 16128915  271 ARTNARLAGIGELITFEVKDVAQLTNPLPKGPYgtVLSNPPYGERL 316
Cdd:NF040721 260 AKKNAENAGVDDTIKFIQGDATKLDKYFDSVDV--IVTNPPYGLRI 303
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
68-153 1.31e-14

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 69.23  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915     68 SDLDLYLGVQA-INWTEMFNPGATFAVHFSGLNdtiRNSQYGAMKVKDAIVDAFtRKNLPRPNVDRDAPDIRVNVWLHKE 146
Cdd:smart00981   1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKL-LEKTGGRKVDLKNPDVVIRVELRKD 76

                   ....*..
gi 16128915    147 TASIALD 153
Cdd:smart00981  77 KAYLSID 83
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
71-351 1.26e-07

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 53.98  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915    71 DLYLGVQAINWTEMFNpgATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRknlprpnVDRDAPDIRVNVWLHKETASI 150
Cdd:TIGR01177  68 DLYDFVAGLEASDLDR--KSFAVRVRDLRGYSVDKARLERKIGAILKKKGFK-------VSLRRPDIVVRVVITEDIFYL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   151 AL---DLSGDGLHLRGYRDRAGIAP--IKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLatdrapGLHRgrwgf 225
Cdd:TIGR01177 139 GRvleERDKEQFIERKPDRRPFFKPgsMDPKLARAMVNLARVTEGDRVLDPFCGTGGFLIEAGLM------GAKV----- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   226 sgwaqhdeaiwqevkaeaqtrarkglaeysshfYGSDSDARVIQRARTNARLAGIgELITFEVKDVAQLtnPLPKGPYGT 305
Cdd:TIGR01177 208 ---------------------------------IGCDIDWKMVAGARINLEHYGI-EDFFVKRGDATKL--PLSSESVDA 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16128915   306 VLSNPPYG-------ERLDS--EPALIALHSLLGRimknqfGGWNLSLFSASPDL 351
Cdd:TIGR01177 252 IATDPPYGrsttaagDGLESlyERSLEEFHEVLKS------EGWIVYAVPTRIDL 300
 
Name Accession Description Interval E-value
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
1-702 0e+00

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 1393.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915    1 MNSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAIN 80
Cdd:PRK11783   1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   81 WTEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLH 160
Cdd:PRK11783  81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  161 LRGYRDRAGIAPIKETLAAAIVMRSGW-QPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEV 239
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  240 KAEAQTRARKGLAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTNPLPKGPYGTVLSNPPYGERLDSE 319
Cdd:PRK11783 241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  320 PALIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKNYHVAEStPDSKPAMVAEDYTNRL 399
Cdd:PRK11783 321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEE-STSSDAEGAQDFANRL 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  400 RKNLKKFEKWARQEGIECYRLYDADLPEYNVAVDRYADWVVVQEYAPPKTIDAHKARQRLFDIIAATISVLGIAPNKLVL 479
Cdd:PRK11783 400 RKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVL 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  480 KTRERQKGKNQYQKLGEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDFLNLFSYTGSATVHAGLG 559
Cdd:PRK11783 480 KTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALG 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  560 GARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWLREANEQFDLIFIDPPTFSNSKRMEDAFDVQRDHLALM 639
Cdd:PRK11783 560 GAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRDHVALI 639
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128915  640 KDLKRLLRAGGTIMFSNNKRGFRMDLDGLAKLGLKAQEITQKTLSQDFARNRQIHNCWLITAA 702
Cdd:PRK11783 640 KDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
2-372 8.36e-165

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 478.06  E-value: 8.36e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   2 NSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINW 81
Cdd:COG0116   1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  82 TEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLHL 161
Cdd:COG0116  81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 162 RGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRgRWGFSGWAQHDEAIWQEVKA 241
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR-DFAFEKWPDFDAELWQELRE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 242 EAQTRARKGLAeysSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTnplPKGPYGTVLSNPPYGERLDSEPA 321
Cdd:COG0116 240 EAEARIKRDPP---LPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLE---PPAEPGLIITNPPYGERLGEEEE 313
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 16128915 322 LIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDC 372
Cdd:COG0116 314 LEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLEC 364
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
383-700 7.64e-126

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 379.14  E-value: 7.64e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 383 TPDSKPAMVAEDYTNRLRKNLKKFEKWARQEGIECYRLYDAD---LPeyNVAVDRYADWVVVQEYAPPKTIdahkarqRL 459
Cdd:COG1092  64 SRDPDEPIDAAFFANRLRKALALRRKLAKREGTNAYRLVHGEadgLP--GLIVDRYGDVLVVQEYSAGMER-------RR 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 460 FDIIAATISVLGiaPNKLVLKTRER---QKGKNQYQKL--GEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLG 534
Cdd:COG1092 135 DEILEALVEVLG--PEGIYLRSDVRvrqLEGLPQYEGVlyGEAPEEVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVA 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 535 QMSKGKDFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRaHRLIQADCLAWLREA---NEQFDL 611
Cdd:COG1092 213 ELAKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGLDDR-HEFVQADAFDWLRELareGERFDL 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 612 IFIDPPTFSNSKRmeDAFDVQRDHLALMKDLKRLLRAGGTIMFSNNKRGFRMDL------DGLAKLGLKAQEITQKTLSQ 685
Cdd:COG1092 292 IILDPPAFAKSKK--DLFDAQRDYKDLNRLALKLLAPGGILVTSSCSRHFSLDLfleilaRAARDAGRRVRIIERLTQPP 369
                       330       340
                ....*....|....*....|
gi 16128915 686 DFARNRQIHN-----CWLIT 700
Cdd:COG1092 370 DHPVLPAFPEgeylkGLLLR 389
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
162-376 1.85e-69

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 224.93  E-value: 1.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   162 RGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRgrwgfsgwaqhdeaiwqevka 241
Cdd:pfam01170   1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFD--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   242 eaqtrarkglAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLtnPLPKGPYGTVLSNPPYGERLDSEPA 321
Cdd:pfam01170  60 ----------ARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADL--PLLEGSVDVIVTNPPYGIRLGSKGA 127
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128915   322 LIALHSLLGRIMKNQF--GGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKN 376
Cdd:pfam01170 128 LEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
24-156 2.10e-46

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 161.59  E-value: 2.10e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  24 GAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINWTEMFNPGATFAVHFSGLNDTIR 103
Cdd:cd11715  21 GAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWEDYLDPDGTFAVRATRVGSKLF 100
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16128915 104 NSQYGAMKVKDAIVDAFtRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSG 156
Cdd:cd11715 101 HSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
4-151 4.75e-43

THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212583  Cd Length: 148  Bit Score: 152.26  E-value: 4.75e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   4 LFASTARGLEELLKTELENLGAV-----ECQVV-QGGVHFKGDT-RLVYQSLMWSRLASRIMLPLGECKVySDLDLYLGV 76
Cdd:cd11688   1 VFATTGKGLEEILAAELYELLEVrgfdaEIQVVpHGRVHFKTDTdEAVYQLVMWSRLISRIMPPLGECKA-DLEDLYETA 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128915  77 QAINWTEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTrknlprPNVDRDAPDIRVNVWLHKETASIA 151
Cdd:cd11688  80 LEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFN------PEVDLDNPDIVVNVEVHKEIASIA 148
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
33-316 8.76e-36

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


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 139.04  E-value: 8.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   33 GGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDL-DLYLGVQAINWTEMfNPGATFAVHFSGLNDTIRNSQYGAMK 111
Cdd:NF040721  34 GRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSLeDIYKRVYSIDFSFI-KPEQSFAIRPLRVGEHDFTSIDIGRV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  112 VKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGD-GLHLRGYRDRAGIAPIKETLAAAIVMRSGWQPG 190
Cdd:NF040721 113 AGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGDeGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDE 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  191 TPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEvkaeaqtrarkglAEYSSHFYGSDSDARVIQR 270
Cdd:NF040721 193 ESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKIFGHELLEKIK-------------KDVELKIYGIEKFRKHLEG 259
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 16128915  271 ARTNARLAGIGELITFEVKDVAQLTNPLPKGPYgtVLSNPPYGERL 316
Cdd:NF040721 260 AKKNAENAGVDDTIKFIQGDATKLDKYFDSVDV--IVTNPPYGLRI 303
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
24-154 4.08e-21

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 90.19  E-value: 4.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915    24 GAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRImlPLGECKVYSDLDLYLGVQAINWTEMFNPGATFAVHFSGLNDtir 103
Cdd:pfam02926  20 GRGRILVVLKGENPEEDRELLKEALEKAPGIERF--PVAETCEADLEDILELAKEIIKDKFKKEGETFAVRVKRRGK--- 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16128915   104 NSQYGAMKVKDAIVDAFTRKNLPRpnVDRDAPDIRVNVWLHKETASIALDL 154
Cdd:pfam02926  95 NHEFTSLEINREVGKAIVEKTGLK--VDLENPDIVVHVEIIKDKAYISIDR 143
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
395-623 7.54e-19

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


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 89.13  E-value: 7.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  395 YTNRLRKnLKKFEKW-ARQEGIECYRLYDAD---LPeyNVAVDRYADWVVVQeyappkTIDAHKARQRlfdiiAATISVL 470
Cdd:PRK15128  79 FTRRLQQ-AQKWRDWlAQKDGLDSYRLIAGEsdgLP--GITIDRFGNFLVLQ------LLSAGAEYQR-----AALISAL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  471 GIAPNKLVLKTRE----RQKGK---NQYQKLGE-KGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDF 542
Cdd:PRK15128 145 QTLYPECAIYDRSdvavRKKEGmelTQGPVTGElPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRV 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  543 LNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWL---REANEQFDLIFIDPPTF 619
Cdd:PRK15128 225 LNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLrtyRDRGEKFDVIVMDPPKF 304

                 ....
gi 16128915  620 SNSK 623
Cdd:PRK15128 305 VENK 308
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
477-653 3.36e-18

S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.


Pssm-ID: 287624 [Multi-domain]  Cd Length: 286  Bit Score: 85.70  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   477 LVLKTRERQKGKNQYQkLGEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDFLNLFSYTGSATVHA 556
Cdd:pfam10672  63 LVLQHRYADGAPSEVL-SGELLETPVVVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   557 GLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCL-AW--LREANeQFDLIFIDPPTFSNSkrmedAFDVQR 633
Cdd:pfam10672 142 IAGGASQVVNVDMARGSLNKGRDNHRLNGHDLGRVSFLGHDIFkSWgkIKKLG-PYDLVIIDPPSFQKG-----SFALTK 215
                         170       180
                  ....*....|....*....|
gi 16128915   634 DHLALMKDLKRLLRAGGTIM 653
Cdd:pfam10672 216 DYKKILRRLPELLVEGGTVL 235
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
68-153 1.31e-14

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 69.23  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915     68 SDLDLYLGVQA-INWTEMFNPGATFAVHFSGLNdtiRNSQYGAMKVKDAIVDAFtRKNLPRPNVDRDAPDIRVNVWLHKE 146
Cdd:smart00981   1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKL-LEKTGGRKVDLKNPDVVIRVELRKD 76

                   ....*..
gi 16128915    147 TASIALD 153
Cdd:smart00981  77 KAYLSID 83
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
177-313 1.03e-13

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 69.59  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 177 LAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLatdrapglhrGRwgfsgwaqhdeaiwqevkaeaqtrarkglaeyss 256
Cdd:COG1041  14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLL----------GR---------------------------------- 49
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128915 257 HFYGSDSDARVIQRARTNARLAGIgELITFEVKDVAQLtnPLPKGPYGTVLSNPPYG 313
Cdd:COG1041  50 RVIGSDIDPKMVEGARENLEHYGY-EDADVIRGDARDL--PLADESVDAIVTDPPYG 103
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
532-617 1.03e-09

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 58.17  E-value: 1.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 532 MLGQMSKGKDFLNLFSYTGSatvhagLG------GARSTTTVDMSRTYLEWAERNLRLNGLTGRAhRLIQADCLAWL-RE 604
Cdd:COG0742  35 ILGPDIEGARVLDLFAGSGA------LGlealsrGAASVVFVEKDRKAAAVIRKNLEKLGLEDRA-RVIRGDALRFLkRL 107
                        90
                ....*....|...
gi 16128915 605 ANEQFDLIFIDPP 617
Cdd:COG0742 108 AGEPFDLVFLDPP 120
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
519-656 5.98e-09

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


Pssm-ID: 443298  Cd Length: 173  Bit Score: 55.96  E-value: 5.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 519 DTGLFLdhriarRMLGQMSKGKDFLNLFSYTGSATVH--AGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAhRLIQA 596
Cdd:COG4122   3 EQGRLL------YLLARLLGAKRILEIGTGTGYSTLWlaRALPDDGRLTTIEIDPERAAIARENFARAGLADRI-RLILG 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128915 597 DCLAWLRE-ANEQFDLIFIDpptfSNSKRMEDAFDvqrdhlalmkDLKRLLRAGGTIMFSN 656
Cdd:COG4122  76 DALEVLPRlADGPFDLVFID----ADKSNYPDYLE----------LALPLLRPGGLIVADN 122
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
532-617 8.78e-08

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 52.63  E-value: 8.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   532 MLGQMSKGKDFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLtgRAHRLIQADCLAWLR--EANEQF 609
Cdd:pfam03602  35 WLAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQLLGL--PGAVLVMDALLALLRlaGKGPVF 112

                  ....*...
gi 16128915   610 DLIFIDPP 617
Cdd:pfam03602 113 DIVFLDPP 120
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
71-351 1.26e-07

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 53.98  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915    71 DLYLGVQAINWTEMFNpgATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRknlprpnVDRDAPDIRVNVWLHKETASI 150
Cdd:TIGR01177  68 DLYDFVAGLEASDLDR--KSFAVRVRDLRGYSVDKARLERKIGAILKKKGFK-------VSLRRPDIVVRVVITEDIFYL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   151 AL---DLSGDGLHLRGYRDRAGIAP--IKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLatdrapGLHRgrwgf 225
Cdd:TIGR01177 139 GRvleERDKEQFIERKPDRRPFFKPgsMDPKLARAMVNLARVTEGDRVLDPFCGTGGFLIEAGLM------GAKV----- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   226 sgwaqhdeaiwqevkaeaqtrarkglaeysshfYGSDSDARVIQRARTNARLAGIgELITFEVKDVAQLtnPLPKGPYGT 305
Cdd:TIGR01177 208 ---------------------------------IGCDIDWKMVAGARINLEHYGI-EDFFVKRGDATKL--PLSSESVDA 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16128915   306 VLSNPPYG-------ERLDS--EPALIALHSLLGRimknqfGGWNLSLFSASPDL 351
Cdd:TIGR01177 252 IATDPPYGrsttaagDGLESlyERSLEEFHEVLKS------EGWIVYAVPTRIDL 300
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
541-655 1.19e-06

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 47.42  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 541 DFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNlRLNGLTGRAhRLIQADCLAWLREANEQFDLIFIDPPTFS 620
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKA-AAALLADNV-EVLKGDAEELPPEADESFDVIISDPPLHH 78
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16128915 621 NSKRMEDAFDVqrdhlalmkdLKRLLRAGGTIMFS 655
Cdd:cd02440  79 LVEDLARFLEE----------ARRLLKPGGVLVLT 103
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
592-652 1.06e-05

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 47.22  E-value: 1.06e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128915 592 RLIQADCLAWLRE-ANEQFDLIFIDPP-----TFSNSKRMEDAFDVQRDHLALMKD----LKRLLRAGGTI 652
Cdd:COG0863   1 RLICGDCLEVLKElPDESVDLIVTDPPynlgkKYGLGRREIGNELSFEEYLEFLREwlaeCYRVLKPGGSL 71
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
525-655 2.68e-05

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 44.24  E-value: 2.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 525 DHRIARRMLGQMSKGKDFLNLFSYTGSATVHAGLGGARsTTTVDMSRTYLEWAERNLRLNGLtgrahRLIQADCLAwLRE 604
Cdd:COG2227  11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAELNV-----DFVQGDLED-LPL 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 16128915 605 ANEQFDLIFidpptfsnskrmedAFDVQ---RDHLALMKDLKRLLRAGGTIMFS 655
Cdd:COG2227  84 EDGSFDLVI--------------CSEVLehlPDPAALLRELARLLKPGGLLLLS 123
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
557-654 4.88e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 45.67  E-value: 4.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 557 GLG---------GARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWLRE-ANEQFDLIFIDPPTFSNSKRME 626
Cdd:COG2521 142 GLGytaiealkrGAREVITVEKDPNVLELAELNPWSRELANERIKIILGDASEVIKTfPDESFDAIIHDPPRFSLAGELY 221
                        90       100
                ....*....|....*....|....*...
gi 16128915 627 DafdvqrdhLALMKDLKRLLRAGGtIMF 654
Cdd:COG2521 222 S--------LEFYRELYRVLKPGG-RLF 240
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
549-650 4.88e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.55  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   549 TGSATVH-AGLGGARsTTTVDMSRTYLEWAERNLRLNGLTgraHRLIQADCLAwLREANEQFDLIFidpptfsnskrmed 627
Cdd:pfam13649   8 TGRLTLAlARRGGAR-VTGVDLSPEMLERARERAAEAGLN---VEFVQGDAED-LPFPDGSFDLVV-------------- 68
                          90       100
                  ....*....|....*....|....*...
gi 16128915   628 AFDV-----QRDHLALMKDLKRLLRAGG 650
Cdd:pfam13649  69 SSGVlhhlpDPDLEAALREIARVLKPGG 96
PRK14967 PRK14967
putative methyltransferase; Provisional
519-683 9.20e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 44.27  E-value: 9.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  519 DTGLFLDhRIARRMLGQmskGKDFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADC 598
Cdd:PRK14967  21 DTQLLAD-ALAAEGLGP---GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915  599 LAWLReaneqFDLIFIDPP------TFSNSKRMEDAFDVQRDHLALM----KDLKRLLRAGGTIMFSNNK-RGFRMDLDG 667
Cdd:PRK14967  97 VEFRP-----FDVVVSNPPyvpappDAPPSRGPARAWDAGPDGRAVLdrlcDAAPALLAPGGSLLLVQSElSGVERTLTR 171
                        170
                 ....*....|....*.
gi 16128915  668 LAKLGLKAQEITQKTL 683
Cdd:PRK14967 172 LSEAGLDAEVVASQWI 187
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
549-654 1.16e-04

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.99  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 549 TGSATVH-AGLGGARsTTTVDMSRTYLEWAERNLRLNGLTGRAhRLIQADCLAWlrEANEQFDLIFidpptfsnskrMED 627
Cdd:COG2230  62 WGGLALYlARRYGVR-VTGVTLSPEQLEYARERAAEAGLADRV-EVRLADYRDL--PADGQFDAIV-----------SIG 126
                        90       100
                ....*....|....*....|....*....
gi 16128915 628 AFD-VQRDHL-ALMKDLKRLLRAGGTIMF 654
Cdd:COG2230 127 MFEhVGPENYpAYFAKVARLLKPGGRLLL 155
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
562-654 3.28e-04

Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 43.70  E-value: 3.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 562 RSTTTVDMSRTYLEWAERNLRLNGLTGRAH-----RLIQADCLAWLREANEQFDLIFIDPP---TFSNSKRMEDAFdvqr 633
Cdd:COG4262 311 ESVTLVDLDPEVTDLAKTNPFLRELNGGALndprvTVVNADAFQFLRETDEKYDVIIVDLPdpsNFSLGKLYSVEF---- 386
                        90       100
                ....*....|....*....|.
gi 16128915 634 dhlalMKDLKRLLRAGGTIMF 654
Cdd:COG4262 387 -----YRLVRRHLAPGGVLVV 402
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
547-654 4.28e-04

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 40.37  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   547 SYTGSATVHAGL----GGARSTTTVDMSRTYLEwAERNLRLNGLTGRAhRLIQADCLAWLRE-ANEQFDLIFID-PPTFS 620
Cdd:pfam13578   5 TYSGVSTLWLAAalrdNGLGRLTAVDPDPGAEE-AGALLRKAGLDDRV-RLIVGDSREALPSlADGPIDLLFIDgDHTYE 82
                          90       100       110
                  ....*....|....*....|....*....|....
gi 16128915   621 nskrmedafDVQRDhlalMKDLKRLLRAGGTIMF 654
Cdd:pfam13578  83 ---------AVLND----LELWLPRLAPGGVILF 103
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
577-654 4.34e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 42.44  E-value: 4.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 577 AERNLRLNGLTGRAHrLIQADCLAWLRE-ANEQFDLIFIDPPTFSNSK------------RMEDAFdvqrDHLALMKDLK 643
Cdd:COG4123  77 ARRNVALNGLEDRIT-VIHGDLKEFAAElPPGSFDLVVSNPPYFKAGSgrkspdearaiaRHEDAL----TLEDLIRAAA 151
                        90
                ....*....|.
gi 16128915 644 RLLRAGGTIMF 654
Cdd:COG4123 152 RLLKPGGRFAL 162
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
526-617 5.39e-04

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 42.86  E-value: 5.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 526 HRIARRMLGQMskgKDFLNLfsyTGSATV---HAGLGG--------ARSTTTVDMSRTYLEWAERNLRLNGLTGraHRLI 594
Cdd:COG2265 215 PEQAEALYAAA---LEWLDL---TGGERVldlYCGVGTfalplarrAKKVIGVEIVPEAVEDARENARLNGLKN--VEFV 286
                        90       100
                ....*....|....*....|....*
gi 16128915 595 QADCLAWLRE--ANEQFDLIFIDPP 617
Cdd:COG2265 287 AGDLEEVLPEllWGGRPDVVVLDPP 311
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
524-694 5.56e-04

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 41.47  E-value: 5.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 524 LDHRIARRM--LGQMSKGKDFLNLFSYTGSATVHAGLGGARSTTtVDMSRTYLEWAERNLRLNGLTGraHRLIQADCLAw 601
Cdd:COG1041  10 LDPRLARALvnLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIG-SDIDPKMVEGARENLEHYGYED--ADVIRGDARD- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 602 LREANEQFDLIFIDPP--TFSNSKRmedafdvqRDHLALMKD----LKRLLRAGGTIMFSNNKRGFRMdldgLAKLGLKA 675
Cdd:COG1041  86 LPLADESVDAIVTDPPygRSSKISG--------EELLELYEKaleeAARVLKPGGRVVIVTPRDIDEL----LEEAGFKV 153
                       170
                ....*....|....*....
gi 16128915 676 QEITQKTLSQDFArnRQIH 694
Cdd:COG1041 154 LERHEQRVHKSLT--RYIL 170
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
257-312 7.69e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 41.67  E-value: 7.69e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16128915 257 HFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTNPLPKGPYGTVLSNPPY 312
Cdd:COG4123  63 RITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVSNPPY 118
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
529-674 9.26e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 39.98  E-value: 9.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915 529 ARRMLGQMS--KGKDFLNLFSYTGSATVHAGLGGARsTTTVDMSRTYLEWAERNLRLNGLTGRahrLIQADCLAwLREAN 606
Cdd:COG2226  11 REALLAALGlrPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVE---FVVGDAED-LPFPD 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128915 607 EQFDLIFidpptfsnskrMEDAFDVQRDHLALMKDLKRLLRAGGTIMFSNNKRGFRMDLDG-LAKLGLK 674
Cdd:COG2226  86 GSFDLVI-----------SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEElLAEAGFE 143
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
256-313 1.09e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 40.66  E-value: 1.09e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16128915 256 SHFYGSDSDARVIQRARTNARlaGIGELITFEVKDVAQLTnplPKGPYGTVLSNPPYG 313
Cdd:COG2263  69 KKVVGVDIDPEALEIARENAE--RLGVRVDFIRADVTRIP---LGGSVDTVVMNPPFG 121
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
543-617 1.36e-03

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


Pssm-ID: 236793  Cd Length: 199  Bit Score: 40.47  E-value: 1.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128915  543 LNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLngLTGRAHRLIQADCLAWLREANEQFDLIFIDPP 617
Cdd:PRK10909  58 LDCFAGSGALGLEALSRYAAGATLLEMDRAVAQQLIKNLAT--LKAGNARVVNTNALSFLAQPGTPHNVVFVDPP 130
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
549-654 2.01e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 38.03  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128915   549 TGSATVHAGLGGARsTTTVDMSRTYLEWAERNLRLNGLTgrahrLIQADCLAwLREANEQFDLIFidpptfsnskrMEDA 628
Cdd:pfam08241   7 TGLLTELLARLGAR-VTGVDISPEMLELAREKAPREGLT-----FVVGDAED-LPFPDNSFDLVL-----------SSEV 68
                          90       100
                  ....*....|....*....|....*.
gi 16128915   629 FDVQRDHLALMKDLKRLLRAGGTIMF 654
Cdd:pfam08241  69 LHHVEDPERALREIARVLKPGGILII 94
 
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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