NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1437745528|emb|SUC09570|]
View 

23S rRNA m(2)G2445 methyltransferase [Proteus mirabilis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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)) ...
 1-701 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: 1356.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528   1 MRSLFASTGRGLEELLKTELEHLGAQSCQITQGGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDLDLYLGVQAID 80
Cdd:PRK11783    1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  81 WSEVFTVNHTFAIHFNGTNDVIRNSQYGALKAKDAIVDSFQRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSGDGLH 160
Cdd:PRK11783   81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 161 QRGYRDLTGQAPLKENLAAAIIMRSGWKTD-TPLIDPMCGSGTLLIEAAMMATDCAPALNRVHWGFRHWLGHNEALWKEV 239
Cdd:PRK11783  161 QRGYRQATGEAPLKENLAAAILLRSGWPQEgTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 240 THEAFARFREGKKNTQARFYGFDVDKRVLDMARANARRADVADLITFTQGDAAKLTNPVSTGVKGTIISNPPYGERLESE 319
Cdd:PRK11783  241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 320 PALIALHSQLGRAVKAHFPGWRLSLFSASPELLSCIQLRAEREFKAKNGPLDCVQKNYLLSETPSTINTRLAEDFANRLR 399
Cdd:PRK11783  321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDAEGAQDFANRLR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 400 KNEKKLAKWAKQQQIECYRLYDADLPEYNVAVDRYGEKVVIQEYAPPKTINEHKARQRLFDVISATMEVLALRSDQLILK 479
Cdd:PRK11783  401 KNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVLK 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 480 TRQRQKGKQQYEKMAEKGDFFLVDEFGAKFWVNLTDYLDTGLFLDHRIARQMLGEMSKGKDFLNLFAYTGSASVHAGLGG 559
Cdd:PRK11783  481 TRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALGG 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 560 AKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQADCLQWLSQSNEQFDVIFIDPPTFSNSKRMENTFDVQRDHIELMK 639
Cdd:PRK11783  561 AKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRDHVALIK 640

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745528 640 HLKRLLRKGGTIMFSNNKRGFKMDHEALANIGLTAKEITQKTLSQDFARNRQIHNCWLLNHA 701
Cdd:PRK11783  641 DAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
 
Name Accession Description Interval E-value
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 1-701 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: 1356.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528   1 MRSLFASTGRGLEELLKTELEHLGAQSCQITQGGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDLDLYLGVQAID 80
Cdd:PRK11783    1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  81 WSEVFTVNHTFAIHFNGTNDVIRNSQYGALKAKDAIVDSFQRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSGDGLH 160
Cdd:PRK11783   81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 161 QRGYRDLTGQAPLKENLAAAIIMRSGWKTD-TPLIDPMCGSGTLLIEAAMMATDCAPALNRVHWGFRHWLGHNEALWKEV 239
Cdd:PRK11783  161 QRGYRQATGEAPLKENLAAAILLRSGWPQEgTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 240 THEAFARFREGKKNTQARFYGFDVDKRVLDMARANARRADVADLITFTQGDAAKLTNPVSTGVKGTIISNPPYGERLESE 319
Cdd:PRK11783  241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 320 PALIALHSQLGRAVKAHFPGWRLSLFSASPELLSCIQLRAEREFKAKNGPLDCVQKNYLLSETPSTINTRLAEDFANRLR 399
Cdd:PRK11783  321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDAEGAQDFANRLR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 400 KNEKKLAKWAKQQQIECYRLYDADLPEYNVAVDRYGEKVVIQEYAPPKTINEHKARQRLFDVISATMEVLALRSDQLILK 479
Cdd:PRK11783  401 KNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVLK 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 480 TRQRQKGKQQYEKMAEKGDFFLVDEFGAKFWVNLTDYLDTGLFLDHRIARQMLGEMSKGKDFLNLFAYTGSASVHAGLGG 559
Cdd:PRK11783  481 TRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALGG 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 560 AKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQADCLQWLSQSNEQFDVIFIDPPTFSNSKRMENTFDVQRDHIELMK 639
Cdd:PRK11783  561 AKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRDHVALIK 640

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745528 640 HLKRLLRKGGTIMFSNNKRGFKMDHEALANIGLTAKEITQKTLSQDFARNRQIHNCWLLNHA 701
Cdd:PRK11783  641 DAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 24-372 3.35e-172

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: 496.93  E-value: 3.35e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  24 GAQSCQITQGGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDLDLYLGVQAIDWSEVFTVNHTFAIHFNGTNDVIR 103
Cdd:COG0116    23 GAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPWEEYLPPDGTFAVDATSVKSKLF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 104 NSQYGALKAKDAIVDSFQRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSGDGLHQRGYRDLTGQAPLKENLAAAIIM 183
Cdd:COG0116   103 HSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHKRGYREAQGEAPLKETLAAALLL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 184 RSGWKTDTPLIDPMCGSGTLLIEAAMMATDCAPALNRvHWGFRHWLGHNEALWKEVTHEAFARFregKKNTQARFYGFDV 263
Cdd:COG0116   183 LSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR-DFAFEKWPDFDAELWQELREEAEARI---KRDPPLPIFGSDI 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 264 DKRVLDMARANARRADVADLITFTQGDAAKLTNPVSTGVkgtIISNPPYGERLESEPALIALHSQLGRAVKAHFPGWRLS 343
Cdd:COG0116   259 DPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGL---IITNPPYGERLGEEEELEALYRELGDVLKQRFKGWSAY 335

                         330       340
                  ....*....|....*....|....*....
gi 1437745528 344 LFSASPELLSCIQLRAEREFKAKNGPLDC 372
Cdd:COG0116   336 ILTSDPELEKAIGLKASKRRKLYNGGLEC 364
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 162-376 8.18e-61

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: 201.82  E-value: 8.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 162 RGYRDLTGQAPLKENLAAAIIMRSGWKTDTPLIDPMCGSGTLLIEAAMMATDCAPALNRVhwgfrhwlghnealwkevth 241
Cdd:pfam01170   1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDA-------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 242 eafarfregkkNTQARFYGFDVDKRVLDMARANARRADVADLITFTQGDAAKLtnPVSTGVKGTIISNPPYGERLESEPA 321
Cdd:pfam01170  61 -----------RVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADL--PLLEGSVDVIVTNPPYGIRLGSKGA 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745528 322 LIALHSQLGRAVKAHF--PGWRLSLFSASPELLSCIQLRAEREFKAKNGPLDCVQKN 376
Cdd:pfam01170 128 LEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 24-156 4.32e-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: 160.82  E-value: 4.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  24 GAQSCQITQGGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDLDLYLGVQAIDWSEVFTVNHTFAIHFNGTNDVIR 103
Cdd:cd11715    21 GAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWEDYLDPDGTFAVRATRVGSKLF 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1437745528 104 NSQYGALKAKDAIVDSFqRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSG 156
Cdd:cd11715   101 HSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
33-316 1.34e-45

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


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 166.77  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  33 GGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDL-DLYLGVQAIDWSEVfTVNHTFAIHFN--GTNDVirNSQYGA 109
Cdd:NF040721   34 GRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSLeDIYKRVYSIDFSFI-KPEQSFAIRPLrvGEHDF--TSIDIG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 110 LKAKDAIVDSFQRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSGD-GLHQRGYRDLTGQAPLKENLAAAIIMRSGWK 188
Cdd:NF040721  111 RVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGDeGLHKRGYRVYQHPAHLNPTIASSLIYLSGWK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 189 TDTPLIDPMCGSGTLLIEAAMMATDCAPALNRVHWGFRHWLGHnEALWKEvtheafarfregKKNTQARFYGFDVDKRVL 268
Cdd:NF040721  191 DEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKIFGH-ELLEKI------------KKDVELKIYGIEKFRKHL 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1437745528 269 DMARANARRADVADLITFTQGDAAKLTNPV-STGVkgtIISNPPYGERL 316
Cdd:NF040721  258 EGAKKNAENAGVDDTIKFIQGDATKLDKYFdSVDV---IVTNPPYGLRI 303
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 68-153 5.55e-13

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


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 64.60  E-value: 5.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528   68 SDLDLYLGVQA-IDWSEVFTVNHTFAIHFNGTNdviRNSQYGALKAKDAIVDSFQRKIGQRPdVAKQSPDIRLTIHLHKE 146
Cdd:smart00981   1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKD 76


                   ....*..
gi 1437745528  147 KASLSLD 153
Cdd:smart00981  77 KAYLSID 83
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
 538-654 2.57e-06

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 48.56  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 538 GKDFLNLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQAD--CLQWLSQSNEQFDVIFIDP 615
Cdd:TIGR00095  51 GAHFLDLFAGSGALGLEALSRGAASAVFVEQDRKVAQTLKENLSTLKKSGEQATVLNDAvrALLFLAKKQTPFDIIYLDP 130

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1437745528 616 PTfsNSKRMENTfdvqrdhIELMKHLKRLLRKGGTIMFS 654
Cdd:TIGR00095 131 PF--NRGLLEAL-------LELLGENKWLNPKGLIVVEY 160
 
Name Accession Description Interval E-value
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 1-701 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: 1356.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528   1 MRSLFASTGRGLEELLKTELEHLGAQSCQITQGGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDLDLYLGVQAID 80
Cdd:PRK11783    1 MNSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  81 WSEVFTVNHTFAIHFNGTNDVIRNSQYGALKAKDAIVDSFQRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSGDGLH 160
Cdd:PRK11783   81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 161 QRGYRDLTGQAPLKENLAAAIIMRSGWKTD-TPLIDPMCGSGTLLIEAAMMATDCAPALNRVHWGFRHWLGHNEALWKEV 239
Cdd:PRK11783  161 QRGYRQATGEAPLKENLAAAILLRSGWPQEgTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 240 THEAFARFREGKKNTQARFYGFDVDKRVLDMARANARRADVADLITFTQGDAAKLTNPVSTGVKGTIISNPPYGERLESE 319
Cdd:PRK11783  241 LEEAQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGPTGLVISNPPYGERLGEE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 320 PALIALHSQLGRAVKAHFPGWRLSLFSASPELLSCIQLRAEREFKAKNGPLDCVQKNYLLSETPSTINTRLAEDFANRLR 399
Cdd:PRK11783  321 PALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDAEGAQDFANRLR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 400 KNEKKLAKWAKQQQIECYRLYDADLPEYNVAVDRYGEKVVIQEYAPPKTINEHKARQRLFDVISATMEVLALRSDQLILK 479
Cdd:PRK11783  401 KNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLGIPPNKVVLK 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 480 TRQRQKGKQQYEKMAEKGDFFLVDEFGAKFWVNLTDYLDTGLFLDHRIARQMLGEMSKGKDFLNLFAYTGSASVHAGLGG 559
Cdd:PRK11783  481 TRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALGG 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 560 AKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQADCLQWLSQSNEQFDVIFIDPPTFSNSKRMENTFDVQRDHIELMK 639
Cdd:PRK11783  561 AKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDVQRDHVALIK 640

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745528 640 HLKRLLRKGGTIMFSNNKRGFKMDHEALANIGLTAKEITQKTLSQDFARNRQIHNCWLLNHA 701
Cdd:PRK11783  641 DAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITHA 702
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 24-372 3.35e-172

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: 496.93  E-value: 3.35e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  24 GAQSCQITQGGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDLDLYLGVQAIDWSEVFTVNHTFAIHFNGTNDVIR 103
Cdd:COG0116    23 GAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPWEEYLPPDGTFAVDATSVKSKLF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 104 NSQYGALKAKDAIVDSFQRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSGDGLHQRGYRDLTGQAPLKENLAAAIIM 183
Cdd:COG0116   103 HSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHKRGYREAQGEAPLKETLAAALLL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 184 RSGWKTDTPLIDPMCGSGTLLIEAAMMATDCAPALNRvHWGFRHWLGHNEALWKEVTHEAFARFregKKNTQARFYGFDV 263
Cdd:COG0116   183 LSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR-DFAFEKWPDFDAELWQELREEAEARI---KRDPPLPIFGSDI 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 264 DKRVLDMARANARRADVADLITFTQGDAAKLTNPVSTGVkgtIISNPPYGERLESEPALIALHSQLGRAVKAHFPGWRLS 343
Cdd:COG0116   259 DPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGL---IITNPPYGERLGEEEELEALYRELGDVLKQRFKGWSAY 335

                         330       340
                  ....*....|....*....|....*....
gi 1437745528 344 LFSASPELLSCIQLRAEREFKAKNGPLDC 372
Cdd:COG0116   336 ILTSDPELEKAIGLKASKRRKLYNGGLEC 364
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 391-698 6.40e-122

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: 369.13  E-value: 6.40e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 391 AEDFANRLRKNEKKLAKWAKQQQIECYRLYDAD---LPeyNVAVDRYGEKVVIQEYAPPKTInehkarqRLFDVISATME 467
Cdd:COG1092    73 AAFFANRLRKALALRRKLAKREGTNAYRLVHGEadgLP--GLIVDRYGDVLVVQEYSAGMER-------RRDEILEALVE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 468 VLALRSdqLILKT--RQRQ-KGKQQYEKMA--EKGDFFLVDEFGAKFWVNLTDYLDTGLFLDHRIARQMLGEMSKGKDFL 542
Cdd:COG1092   144 VLGPEG--IYLRSdvRVRQlEGLPQYEGVLygEAPEEVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVL 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 543 NLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQANGLSGRqHRLMQADCLQWL---SQSNEQFDVIFIDPPTFS 619
Cdd:COG1092   222 NLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGLDDR-HEFVQADAFDWLrelAREGERFDLIILDPPAFA 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 620 NSKRmeNTFDVQRDHIELMKHLKRLLRKGGTIMFSNNKRGFKMD------HEALANIGLTAKEITQKTLSQDFARNRQIH 693
Cdd:COG1092   301 KSKK--DLFDAQRDYKDLNRLALKLLAPGGILVTSSCSRHFSLDlfleilARAARDAGRRVRIIERLTQPPDHPVLPAFP 378

                         330
                  ....*....|
gi 1437745528 694 N-----CWLL 698
Cdd:COG1092   379 EgeylkGLLL 388
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 162-376 8.18e-61

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: 201.82  E-value: 8.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 162 RGYRDLTGQAPLKENLAAAIIMRSGWKTDTPLIDPMCGSGTLLIEAAMMATDCAPALNRVhwgfrhwlghnealwkevth 241
Cdd:pfam01170   1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDA-------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 242 eafarfregkkNTQARFYGFDVDKRVLDMARANARRADVADLITFTQGDAAKLtnPVSTGVKGTIISNPPYGERLESEPA 321
Cdd:pfam01170  61 -----------RVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADL--PLLEGSVDVIVTNPPYGIRLGSKGA 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1437745528 322 LIALHSQLGRAVKAHF--PGWRLSLFSASPELLSCIQLRAEREFKAKNGPLDCVQKN 376
Cdd:pfam01170 128 LEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 24-156 4.32e-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: 160.82  E-value: 4.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  24 GAQSCQITQGGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDLDLYLGVQAIDWSEVFTVNHTFAIHFNGTNDVIR 103
Cdd:cd11715    21 GAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWEDYLDPDGTFAVRATRVGSKLF 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1437745528 104 NSQYGALKAKDAIVDSFqRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSG 156
Cdd:cd11715   101 HSQFAALRVKDAIVDRF-REKGKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
33-316 1.34e-45

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


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 166.77  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  33 GGVYFRADDKTMYQSLLWSRLASRIMLPLNEFNVYSDL-DLYLGVQAIDWSEVfTVNHTFAIHFN--GTNDVirNSQYGA 109
Cdd:NF040721   34 GRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSLeDIYKRVYSIDFSFI-KPEQSFAIRPLrvGEHDF--TSIDIG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 110 LKAKDAIVDSFQRKIGQRPDVAKQSPDIRLTIHLHKEKASLSLDLSGD-GLHQRGYRDLTGQAPLKENLAAAIIMRSGWK 188
Cdd:NF040721  111 RVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGDeGLHKRGYRVYQHPAHLNPTIASSLIYLSGWK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 189 TDTPLIDPMCGSGTLLIEAAMMATDCAPALNRVHWGFRHWLGHnEALWKEvtheafarfregKKNTQARFYGFDVDKRVL 268
Cdd:NF040721  191 DEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKIFGH-ELLEKI------------KKDVELKIYGIEKFRKHL 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1437745528 269 DMARANARRADVADLITFTQGDAAKLTNPV-STGVkgtIISNPPYGERL 316
Cdd:NF040721  258 EGAKKNAENAGVDDTIKFIQGDATKLDKYFdSVDV---IVTNPPYGLRI 303
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
 502-652 5.35e-21

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: 93.79  E-value: 5.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 502 VDEFGAKFWVNLTDYLDTGLFLDHRIARQMLGEMSKGKDFLNLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQ 581
Cdd:pfam10672  88 VVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARGSLNKGRDNHR 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437745528 582 ANGLSGRQHRLMQADCLQ-W--LSQSNeQFDVIFIDPPTFSnskrmENTFDVQRDHIELMKHLKRLLRKGGTIM 652
Cdd:pfam10672 168 LNGHDLGRVSFLGHDIFKsWgkIKKLG-PYDLVIIDPPSFQ-----KGSFALTKDYKKILRRLPELLVEGGTVL 235
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
 4-151 8.16e-21

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: 89.47  E-value: 8.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528   4 LFASTGRGLEELLKTELEHLGA-----QSCQI-TQGGVYFRAD-DKTMYQSLLWSRLASRIMLPLNEFNVySDLDLYLGV 76
Cdd:cd11688     1 VFATTGKGLEEILAAELYELLEvrgfdAEIQVvPHGRVHFKTDtDEAVYQLVMWSRLISRIMPPLGECKA-DLEDLYETA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745528  77 QAIDWSEVFTVNHTFAIHFNGTNDVIRNSQYGALKAKDAIVDSFQRKigqrpdVAKQSPDIRLTIHLHKEKASLS 151
Cdd:cd11688    80 LEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFNPE------VDLDNPDIVVNVEVHKEIASIA 148
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
394-622 2.27e-16

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


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 81.81  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 394 FANRLRKNEKKLAKWAKQQQIECYRLYDAD---LPeyNVAVDRYGEKVVIQ------EYAPPKTINehkARQRLFDVISa 464
Cdd:PRK15128   79 FTRRLQQAQKWRDWLAQKDGLDSYRLIAGEsdgLP--GITIDRFGNFLVLQllsagaEYQRAALIS---ALQTLYPECA- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 465 tmevLALRSDQLIlktrqRQKGKQQYEKMAEKGD----FFLVDEFGAKFWVNLTDYLDTGLFLDHRIARQMLGEMSKGKD 540
Cdd:PRK15128  153 ----IYDRSDVAV-----RKKEGMELTQGPVTGElppaLLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKR 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 541 FLNLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQADCLQWLSQ---SNEQFDVIFIDPPT 617
Cdd:PRK15128  224 VLNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTyrdRGEKFDVIVMDPPK 303


                  ....*
gi 1437745528 618 FSNSK 622
Cdd:PRK15128  304 FVENK 308
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 28-154 1.98e-13

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: 67.85  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528  28 CQITQGGVYFRADDKTMYQSLLWSRLASRImlPLNEFNVYSDLDLYLGVQAIDWSEVFTVNHTFAIHFNGTNDvirNSQY 107
Cdd:pfam02926  24 ILVVLKGENPEEDRELLKEALEKAPGIERF--PVAETCEADLEDILELAKEIIKDKFKKEGETFAVRVKRRGK---NHEF 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1437745528 108 GALKAKDAIVDSFQRKIGQRPDVAKqsPDIRLTIHLHKEKASLSLDL 154
Cdd:pfam02926  99 TSLEINREVGKAIVEKTGLKVDLEN--PDIVVHVEIIKDKAYISIDR 143
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 68-153 5.55e-13

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


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 64.60  E-value: 5.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528   68 SDLDLYLGVQA-IDWSEVFTVNHTFAIHFNGTNdviRNSQYGALKAKDAIVDSFQRKIGQRPdVAKQSPDIRLTIHLHKE 146
Cdd:smart00981   1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKD 76


                   ....*..
gi 1437745528  147 KASLSLD 153
Cdd:smart00981  77 KAYLSID 83
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 177-333 2.60e-12

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


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 65.74  E-value: 2.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 177 LAAAIIMRSGWKTDTPLIDPMCGSGTLLIEAAMMAtdcapalnrvhwgfrhwlghnealwkevtheafarfregkkntqA 256
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLG--------------------------------------------R 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 257 RFYGFDVDKRVLDMARANARRADVADlITFTQGDAAKLtnPVSTGVKGTIISNPPYG-------ERLES--EPALIALHS 327
Cdd:COG1041    50 RVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDL--PLADESVDAIVTDPPYGrsskisgEELLElyEKALEEAAR 126


                  ....*....
gi 1437745528 328 QL---GRAV 333
Cdd:COG1041   127 VLkpgGRVV 135
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
531-616 9.74e-09

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 55.32  E-value: 9.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 531 MLGEMSKGKDFLNLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQADCLQWLSQSNEQFDV 610
Cdd:pfam03602  35 WLAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDALLALLRLAGKGPVFDI 114


                  ....*.
gi 1437745528 611 IFIDPP 616
Cdd:pfam03602 115 VFLDPP 120
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 531-616 6.22e-08

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: 53.16  E-value: 6.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 531 MLGEMSKGKDFLNLFAYTGSasvhagLG------GAKSTTTVDMSRTYLEWAEKNFQANGLSGRqHRLMQADCLQWLSQ- 603
Cdd:COG0742    35 ILGPDIEGARVLDLFAGSGA------LGlealsrGAASVVFVEKDRKAAAVIRKNLEKLGLEDR-ARVIRGDALRFLKRl 107

                          90
                  ....*....|...
gi 1437745528 604 SNEQFDVIFIDPP 616
Cdd:COG0742   108 AGEPFDLVFLDPP 120
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 255-325 1.10e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 54.00  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 255 QARFYGFDVDKRVLDMARANARRADVADLITFTQGDaakLTNPVSTgvKGT---IISNPPY----------GERLESEPA 321
Cdd:COG2890   136 DARVTAVDISPDALAVARRNAERLGLEDRVRFLQGD---LFEPLPG--DGRfdlIVSNPPYipedeiallpPEVRDHEPR 210


                  ....
gi 1437745528 322 LiAL 325
Cdd:COG2890   211 L-AL 213
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 564-655 3.62e-07

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: 50.57  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 564 TTVDMSRTYLEWAEKNFQANGLSGRQhRLMQADCLQWLSQ-SNEQFDVIFIDpptfSNSKRMENTFDvqrdhielmkHLK 642
Cdd:COG4122    45 TTIEIDPERAAIARENFARAGLADRI-RLILGDALEVLPRlADGPFDLVFID----ADKSNYPDYLE----------LAL 109

                          90
                  ....*....|...
gi 1437745528 643 RLLRKGGTIMFSN 655
Cdd:COG4122   110 PLLRPGGLIVADN 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 540-654 4.14e-07

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: 48.97  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 540 DFLNLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRlmQADCLQWLSQSNEQFDVIFIDPPTFS 619
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVL--KGDAEELPPEADESFDVIISDPPLHH 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1437745528 620 nskrmentfdVQRDHIELMKHLKRLLRKGGTIMFS 654
Cdd:cd02440    79 ----------LVEDLARFLEEARRLLKPGGVLVLT 103
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
 538-654 2.57e-06

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 48.56  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 538 GKDFLNLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQAD--CLQWLSQSNEQFDVIFIDP 615
Cdd:TIGR00095  51 GAHFLDLFAGSGALGLEALSRGAASAVFVEQDRKVAQTLKENLSTLKKSGEQATVLNDAvrALLFLAKKQTPFDIIYLDP 130

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1437745528 616 PTfsNSKRMENTfdvqrdhIELMKHLKRLLRKGGTIMFS 654
Cdd:TIGR00095 131 PF--NRGLLEAL-------LELLGENKWLNPKGLIVVEY 160
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 251-312 5.40e-06

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: 48.22  E-value: 5.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745528 251 KKNTQARFYGFDVDKRVLDMARANARRADVADLITFTQGDaakLTNPVSTGVKGT---IISNPPY 312
Cdd:COG4123    57 QRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGD---LKEFAAELPPGSfdlVVSNPPY 118
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
 542-616 1.01e-05

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


Pssm-ID: 236793  Cd Length: 199  Bit Score: 47.02  E-value: 1.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437745528 542 LNLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQAngLSGRQHRLMQADCLQWLSQSNEQFDVIFIDPP 616
Cdd:PRK10909   58 LDCFAGSGALGLEALSRYAAGATLLEMDRAVAQQLIKNLAT--LKAGNARVVNTNALSFLAQPGTPHNVVFVDPP 130
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 524-654 1.42e-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: 45.01  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 524 DHRIARQMLGEMSKGKDFLNLFAYTGSASVH-AGLGgaKSTTTVDMSRTYLEWAEKNFQANGLsgrqhRLMQADcLQWLS 602
Cdd:COG2227    11 DRRLAALLARLLPAGGRVLDVGCGTGRLALAlARRG--ADVTGVDISPEALEIARERAAELNV-----DFVQGD-LEDLP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1437745528 603 QSNEQFDVIFidpptfsnskrMENTFDVQRDHIELMKHLKRLLRKGGTIMFS 654
Cdd:COG2227    83 LEDGSFDLVI-----------CSEVLEHLPDPAALLRELARLLKPGGLLLLS 123
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 548-649 2.60e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 43.32  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 548 TGSASVH-AGLGGAKsTTTVDMSRTYLEWAEKNFQANGLsgrQHRLMQADCLQwLSQSNEQFDVIF-------IDPPtfs 619
Cdd:pfam13649   8 TGRLTLAlARRGGAR-VTGVDLSPEMLERARERAAEAGL---NVEFVQGDAED-LPFPDGSFDLVVssgvlhhLPDP--- 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1437745528 620 nskrmentfdvqrDHIELMKHLKRLLRKGG 649
Cdd:pfam13649  80 -------------DLEAALREIARVLKPGG 96
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 251-312 3.26e-05

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: 45.18  E-value: 3.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437745528 251 KKNTQARFYGFDVDKRVLDMARANARRADVADlITFTQGDAaklTNPVSTGVKGTIISNPPY 312
Cdd:COG2813    69 KRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDG---LSGVPDGSFDLILSNPPF 126
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
256-313 4.36e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.89  E-value: 4.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1437745528 256 ARFYGFDVDKRVLDMARANARRADVAdlITFTQGDAAKLTNPVStgvKGTIISNPPYG 313
Cdd:COG2263    69 KKVVGVDIDPEALEIARENAERLGVR--VDFIRADVTRIPLGGS---VDTVVMNPPFG 121
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
547-653 1.83e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.13  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 547 YTGSASVHAGlggAKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQADCLQWLSQ-SNEQFDVIFIDPPTFSNSKRME 625
Cdd:COG2521   145 YTAIEALKRG---AREVITVEKDPNVLELAELNPWSRELANERIKIILGDASEVIKTfPDESFDAIIHDPPRFSLAGELY 221

                          90       100
                  ....*....|....*....|....*...
gi 1437745528 626 NtfdvqrdhIELMKHLKRLLRKGGtIMF 653
Cdd:COG2521   222 S--------LEFYRELYRVLKPGG-RLF 240
PRK14967 PRK14967
putative methyltransferase; Provisional
 538-616 3.54e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 42.73  E-value: 3.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745528 538 GKDFLNLFAYTGSASVHAGLGGAKSTTTVDMSRTYLEWAEKNFQANGLSGRQHRLMQADCLQWlsqsnEQFDVIFIDPP 616
Cdd:PRK14967   37 GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEF-----RPFDVVVSNPP 110
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
591-651 4.81e-04

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 42.22  E-value: 4.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437745528 591 RLMQADCLQWLSQ-SNEQFDVIFIDPP-----TFSNSKRMENTFDVQRDHIE----LMKHLKRLLRKGGTI 651
Cdd:COG0863     1 RLICGDCLEVLKElPDESVDLIVTDPPynlgkKYGLGRREIGNELSFEEYLEflreWLAECYRVLKPGGSL 71
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 255-325 4.93e-04

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.46  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 255 QARFYGFDVDKRVLDMARANARRAdVADLITFTQGDaakLTNPVSTGVKGTIISNPPY----------GERLESEPALiA 324
Cdd:PRK09328  132 DAEVTAVDISPEALAVARRNAKHG-LGARVEFLQGD---WFEPLPGGRFDLIVSNPPYipeadihllqPEVRDHEPHL-A 206


                  .
gi 1437745528 325 L 325
Cdd:PRK09328  207 L 207
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 548-653 1.37e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.91  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 548 TGSASVH-AGLGGAKsTTTVDMSRTYLEWAEKNFQANGLSGRqHRLMQADCLQWlsQSNEQFDVIFIdpptfsnskrMEN 626
Cdd:COG2230    62 WGGLALYlARRYGVR-VTGVTLSPEQLEYARERAAEAGLADR-VEVRLADYRDL--PADGQFDAIVS----------IGM 127

                          90       100
                  ....*....|....*....|....*...
gi 1437745528 627 TFDVQRDHI-ELMKHLKRLLRKGGTIMF 653
Cdd:COG2230   128 FEHVGPENYpAYFAKVARLLKPGGRLLL 155
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 528-673 1.43e-03

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: 39.59  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 528 ARQMLGEMS--KGKDFLNLFAYTGSASVHAGLGGAKsTTTVDMSRTYLEWAEKNFQANGLSGRqhrLMQADcLQWLSQSN 605
Cdd:COG2226    11 REALLAALGlrPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVE---FVVGD-AEDLPFPD 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437745528 606 EQFDVIFidpptfsnskrMENTFDVQRDHIELMKHLKRLLRKGGTIMFSNNKRGFKMD-HEALANIGLT 673
Cdd:COG2226    86 GSFDLVI-----------SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAElEELLAEAGFE 143
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 576-653 2.50e-03

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: 40.13  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 576 AEKNFQANGLSGRQHrLMQADCLQWLSQ-SNEQFDVIFIDPPTFSNSKRMENTfDVQR---------DHIELMKHLKRLL 645
Cdd:COG4123    77 ARRNVALNGLEDRIT-VIHGDLKEFAAElPPGSFDLVVSNPPYFKAGSGRKSP-DEARaiarhedalTLEDLIRAAARLL 154


                  ....*...
gi 1437745528 646 RKGGTIMF 653
Cdd:COG4123   155 KPGGRFAL 162
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 549-669 2.96e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 39.51  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 549 GSASVHAGLGGAKsTTTVDMSRTYLEWAEKNFQANGLSgrQHRLMQADCLQWLSQSNEQFDVIF-------IDPptfsnS 621
Cdd:COG0500    39 RNLLALAARFGGR-VIGIDLSPEAIALARARAAKAGLG--NVEFLVADLAELDPLPAESFDLVVafgvlhhLPP-----E 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1437745528 622 KRMEntfdvqrdhieLMKHLKRLLRKGGTIMFSNNKRGFKMDHEALAN 669
Cdd:COG0500   111 EREA-----------LLRELARALKPGGVLLLSASDAAAALSLARLLL 147
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 511-673 2.96e-03

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: 39.26  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 511 VNLTDYLDTGLFLDhriarQMLGemskgkdflnlfayTGSASVHAGLGGAKSTTT------------VDMSRTYLEWAEK 578
Cdd:pfam01170  21 VNLAGWKPGDPLLD-----PMCG--------------SGTILIEAALMGANIAPGkfdarvraplygSDIDRRMVQGARL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 579 NFQANGLSGRQHrLMQADCLQwLSQSNEQFDVIFIDPPTfsnSKRMENTFDVQRDHIELMKHLKRLLRKGG--TIMFSNN 656
Cdd:pfam01170  82 NAENAGVGDLIE-FVQADAAD-LPLLEGSVDVIVTNPPY---GIRLGSKGALEALYPEFLREAKRVLRGGGwlVLLTAEN 156

                         170       180
                  ....*....|....*....|....*
gi 1437745528 657 K--------RGFKMDHEALANIGLT 673
Cdd:pfam01170 157 KdfekaareRAWRKKKEFNVHIGGT 181
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 523-693 5.28e-03

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: 38.39  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 523 LDHRIARQM--LGEMSKGKDFLNLFAYTGSASVHAGLGGAKSTTtVDMSRTYLEWAEKNFQANGLsgRQHRLMQADCLQw 600
Cdd:COG1041    10 LDPRLARALvnLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIG-SDIDPKMVEGARENLEHYGY--EDADVIRGDARD- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 601 LSQSNEQFDVIFIDPP--TFSNSKRmentfdvqRDHIELMK----HLKRLLRKGGTIMFSNNKRGFKMDHEAlaniGLTA 674
Cdd:COG1041    86 LPLADESVDAIVTDPPygRSSKISG--------EELLELYEkaleEAARVLKPGGRVVIVTPRDIDELLEEA----GFKV 153

                         170
                  ....*....|....*....
gi 1437745528 675 KEITQKTLSQDFArnRQIH 693
Cdd:COG1041   154 LERHEQRVHKSLT--RYIL 170
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 548-653 6.77e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 36.49  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437745528 548 TGSASVHAGLGGAKsTTTVDMSRTYLEWAEKNFQANGLSgrqhrLMQADCLQwLSQSNEQFDVIFidpptfsnskrMENT 627
Cdd:pfam08241   7 TGLLTELLARLGAR-VTGVDISPEMLELAREKAPREGLT-----FVVGDAED-LPFPDNSFDLVL-----------SSEV 68

                          90       100
                  ....*....|....*....|....*.
gi 1437745528 628 FDVQRDHIELMKHLKRLLRKGGTIMF 653
Cdd:pfam08241  69 LHHVEDPERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 256-331 7.13e-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: 36.64  E-value: 7.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745528 256 ARFYGFDVDKRVLDMARANARRAdVADLITFTQGDAAKLTNPVSTGVKGtIISNPPYGERLESEPALIALHSQLGR 331
Cdd:cd02440    22 ARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEELPPEADESFDV-IISDPPLHHLVEDLARFLEEARRLLK 95
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 591-653 9.06e-03

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 39.08  E-value: 9.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437745528 591 RLMQADCLQWLSQSNEQFDVIFIDPP---TFSNSKRMENTFdvqrdhielMKHLKRLLRKGGTIMF 653
Cdd:COG4262   346 TVVNADAFQFLRETDEKYDVIIVDLPdpsNFSLGKLYSVEF---------YRLVRRHLAPGGVLVV 402
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH