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Conserved domains on  [gi|1907143695|ref|XP_036018537|]
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tRNA (cytosine(72)-C(5))-methyltransferase NSUN6 isoform X2 [Mus musculus]

Protein Classification

RsmB/NOP family class I SAM-dependent RNA methyltransferase( domain architecture ID 15340246)

RsmB/NOP family class I SAM-dependent RNA methyltransferase similar to tRNA (cytosine(34)-C(5))-methyltransferase, which methylates cytosine at specific positions of intron-containing tRNA(Leu)(CAA) precursors and tRNA(Gly)(GCC) precursors

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0003723
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 54-324 2.15e-67

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


:

Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 217.95  E-value: 2.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  54 GIRMTEPIYLS--PSFDNvlpSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKV 131
Cdd:COG0144   211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 132 NKLKQNASLLGLHSIRAFCFDATKALKldttdgieggppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQP 208
Cdd:COG0144   288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 209 LQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMVGAGltleqlkqLQRFDPSVv 288
Cdd:COG0144   356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG--------YLRLLPHR- 426

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907143695 289 plQNMDtdslgearredmiwlankdciGFFIAKFLK 324
Cdd:COG0144   427 --HGTD---------------------GFFIARLRK 439
PUA_NSun6-like cd21150
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ...
 1-61 9.08e-29

PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this subfamily contain PUA domains that co-occur with SAM-dependent methyltransferase domains and may play roles as cytosine-C(5)-methyltransferases specific for tRNAs or rRNAs. Nsun6 binding to its tRNA substrates requires the presence of a 3'-CCA sequence, which is precisely recognized primarily through interactions with residues from the PUA domain, where the molecular surface of the PUA domain snugly fits onto each nucleotide residue of the CCA end. Human RNA:m5C methyltransferase NSun6 (hNSun6) plays a major role in bone metastasis and could be a valuable therapeutic target for bone metastasis and therapy-resistant tumors.


:

Pssm-ID: 409292 [Multi-domain]  Cd Length: 92  Bit Score: 106.38  E-value: 9.08e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143695   1 MKAGDVISVYSDINGKCKKGA-KEFDGTKVFLGNGISELSRKDIFNGLPDLKGIGIRMTEPI 61
Cdd:cd21150    31 LKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKPSGIAVEMTEPV 92
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 54-324 2.15e-67

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 217.95  E-value: 2.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  54 GIRMTEPIYLS--PSFDNvlpSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKV 131
Cdd:COG0144   211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 132 NKLKQNASLLGLHSIRAFCFDATKALKldttdgieggppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQP 208
Cdd:COG0144   288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 209 LQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMVGAGltleqlkqLQRFDPSVv 288
Cdd:COG0144   356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG--------YLRLLPHR- 426

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907143695 289 plQNMDtdslgearredmiwlankdciGFFIAKFLK 324
Cdd:COG0144   427 --HGTD---------------------GFFIARLRK 439
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
74-324 1.03e-62

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 205.80  E-value: 1.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  74 YIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDA 153
Cdd:PRK14902  231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 154 TKAlkldttdgieggPPFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYS 230
Cdd:PRK14902  311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 231 TCTITLAENEEQVAWALRTFPCLQLQPQEPqiggegmvgaGLTLEQLKQLQRFDPSVVPLQNmDTDslgearredmiwla 310
Cdd:PRK14902  379 TCTIEKEENEEVIEAFLEEHPEFELVPLQH----------EKPDELVYEVKDGYLQILPNDY-GTD-------------- 433

                         250
                  ....*....|....
gi 1907143695 311 nkdciGFFIAKFLK 324
Cdd:PRK14902  434 -----GFFIAKLRK 442
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 86-323 2.89e-53

16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.


Pssm-ID: 426109 [Multi-domain]  Cd Length: 199  Bit Score: 173.76  E-value: 2.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  86 AHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKalkldtTDGI 165
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------PDQW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 166 EGGppflpESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQ 242
Cdd:pfam01189  75 LGG-----VLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 243 VAWALRTFPCLQLQPqepqIGGEGMVGAGLTLEQLKQlqrfdpsVVPLQNmdtdslgearredmiwlaNKDciGFFIAKF 322
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLR-------LLPHTH------------------NGD--GFFIAKL 198


                  .
gi 1907143695 323 L 323
Cdd:pfam01189 199 R 199
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 71-324 5.48e-48

NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 162.25  E-value: 5.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  71 LPSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFC 150
Cdd:TIGR00446  49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 151 FDATKAlkldttdgieggPPFLPEsFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVL 227
Cdd:TIGR00446 129 ADGRKF------------GAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 228 VYSTCTITLAENEEQVAWALRTFPCLQLqpqEPQIGGEGMvGAGLTLEQLKQLQRFDPSvvplqnmdtdslgearredmi 307
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDEFF-GINIGKGEVKGALRVFPQ--------------------- 250

                         250
                  ....*....|....*..
gi 1907143695 308 wlaNKDCIGFFIAKFLK 324
Cdd:TIGR00446 251 ---NYDCEGFFVAKLRK 264
PUA_NSun6-like cd21150
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ...
 1-61 9.08e-29

PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this subfamily contain PUA domains that co-occur with SAM-dependent methyltransferase domains and may play roles as cytosine-C(5)-methyltransferases specific for tRNAs or rRNAs. Nsun6 binding to its tRNA substrates requires the presence of a 3'-CCA sequence, which is precisely recognized primarily through interactions with residues from the PUA domain, where the molecular surface of the PUA domain snugly fits onto each nucleotide residue of the CCA end. Human RNA:m5C methyltransferase NSun6 (hNSun6) plays a major role in bone metastasis and could be a valuable therapeutic target for bone metastasis and therapy-resistant tumors.


Pssm-ID: 409292 [Multi-domain]  Cd Length: 92  Bit Score: 106.38  E-value: 9.08e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143695   1 MKAGDVISVYSDINGKCKKGA-KEFDGTKVFLGNGISELSRKDIFNGLPDLKGIGIRMTEPI 61
Cdd:cd21150    31 LKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKPSGIAVEMTEPV 92
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-230 1.23e-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: 49.35  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  96 KILDMCAAPGGKTTHTAAlmQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKAlkldttdgieggPPFLPES 175
Cdd:cd02440     1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907143695 176 FDRIILDAPCSgmgqrpnmactwtlkevtSYQPLQRKLLHVAVQLLKPGGVLVYS 230
Cdd:cd02440    67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 54-324 2.15e-67

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 217.95  E-value: 2.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  54 GIRMTEPIYLS--PSFDNvlpSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKV 131
Cdd:COG0144   211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 132 NKLKQNASLLGLHSIRAFCFDATKALKldttdgieggppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQP 208
Cdd:COG0144   288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 209 LQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMVGAGltleqlkqLQRFDPSVv 288
Cdd:COG0144   356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG--------YLRLLPHR- 426

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907143695 289 plQNMDtdslgearredmiwlankdciGFFIAKFLK 324
Cdd:COG0144   427 --HGTD---------------------GFFIARLRK 439
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
74-324 1.03e-62

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 205.80  E-value: 1.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  74 YIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDA 153
Cdd:PRK14902  231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 154 TKAlkldttdgieggPPFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYS 230
Cdd:PRK14902  311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 231 TCTITLAENEEQVAWALRTFPCLQLQPQEPqiggegmvgaGLTLEQLKQLQRFDPSVVPLQNmDTDslgearredmiwla 310
Cdd:PRK14902  379 TCTIEKEENEEVIEAFLEEHPEFELVPLQH----------EKPDELVYEVKDGYLQILPNDY-GTD-------------- 433

                         250
                  ....*....|....
gi 1907143695 311 nkdciGFFIAKFLK 324
Cdd:PRK14902  434 -----GFFIAKLRK 442
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 85-262 7.24e-60

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 198.23  E-value: 7.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  85 VAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIrafcfdatKALKLDTTDG 164
Cdd:PRK14901  244 VAPLLDPQPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSASRLKKLQENAQRLGLKSI--------KILAADSRNL 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 165 IEGGPPFLpESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITLAENEE 241
Cdd:PRK14901  316 LELKPQWR-GYFDRILLDAPCSGLGtlhRHPDARWRQTPEKIQELAPLQAELLESLAPLLKPGGTLVYATCTLHPAENEA 394

                         170       180
                  ....*....|....*....|.
gi 1907143695 242 QVAWALRTFPCLQLQPQEPQI 262
Cdd:PRK14901  395 QIEQFLARHPDWKLEPPKQKI 415
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 86-323 2.89e-53

16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.


Pssm-ID: 426109 [Multi-domain]  Cd Length: 199  Bit Score: 173.76  E-value: 2.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  86 AHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKalkldtTDGI 165
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------PDQW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 166 EGGppflpESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQ 242
Cdd:pfam01189  75 LGG-----VLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 243 VAWALRTFPCLQLQPqepqIGGEGMVGAGLTLEQLKQlqrfdpsVVPLQNmdtdslgearredmiwlaNKDciGFFIAKF 322
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLR-------LLPHTH------------------NGD--GFFIAKL 198


                  .
gi 1907143695 323 L 323
Cdd:pfam01189 199 R 199
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 71-324 5.48e-48

NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 162.25  E-value: 5.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  71 LPSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFC 150
Cdd:TIGR00446  49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 151 FDATKAlkldttdgieggPPFLPEsFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVL 227
Cdd:TIGR00446 129 ADGRKF------------GAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 228 VYSTCTITLAENEEQVAWALRTFPCLQLqpqEPQIGGEGMvGAGLTLEQLKQLQRFDPSvvplqnmdtdslgearredmi 307
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDEFF-GINIGKGEVKGALRVFPQ--------------------- 250

                         250
                  ....*....|....*..
gi 1907143695 308 wlaNKDCIGFFIAKFLK 324
Cdd:TIGR00446 251 ---NYDCEGFFVAKLRK 264
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 89-274 2.42e-46

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 162.92  E-value: 2.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  89 LDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKalkldttdgiegg 168
Cdd:PRK14904  246 LNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYPQKLEKIRSHASALGITIIETIEGDARS------------- 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 169 ppFLPE-SFDRIILDAPCSG---MGQRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQVA 244
Cdd:PRK14904  313 --FSPEeQPDAILLDAPCTGtgvLGRRAELRWKLTPEKLAELVGLQAELLDHAASLLKPGGVLVYATCSIEPEENELQIE 390

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907143695 245 WALRTFPCLQLQPQ-----EPQIGGEGMVGAGLTL 274
Cdd:PRK14904  391 AFLQRHPEFSAEPSpgslpEPFHEVAHPKGAILTL 425
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 77-264 5.99e-40

16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. The reading frame was originally interpreted as two reading frames, fmu and fmv. The recombinant protein from E. coli was shown to methylate only C967 of small subunit (16S) ribosomal RNA and to produce only m5C at that position. The seed alignment is built from bacterial sequences only. Eukaryotic homologs include Nop2, a protein required for processing pre-rRNA, that is likely also a rRNA methyltransferase, although the fine specificity may differ. Cutoff scores are set to avoid treating archaeal and eukaroytic homologs automatically as functionally equivalent, although they may have very similar roles. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273141 [Multi-domain]  Cd Length: 426  Bit Score: 145.40  E-value: 5.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  77 LQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQdKGEVIALDKILTKVNKLKQNASLLGLhsirafcfdatkA 156
Cdd:TIGR00563 222 VQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELAP-QAQVVALDIHEHRLKRVYENLKRLGL------------T 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 157 LKLDTTDGIEGGPPFLPES--FDRIILDAPCSGMG---QRPNMacTWTLKEVTSYQ--PLQRKLLHVAVQLLKPGGVLVY 229
Cdd:TIGR00563 289 IKAETKDGDGRGPSQWAENeqFDRILLDAPCSATGvirRHPDI--KWLRKPRDIAElaELQSEILDAIWPLLKTGGTLVY 366

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907143695 230 STCTITLAENEEQVAWALRTFPCLQL----QPQEPQIGG 264
Cdd:TIGR00563 367 ATCSVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
86-258 2.36e-37

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 138.40  E-value: 2.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  86 AHVLDPQPGEKILDMCAAPGGKTTHTAALmQDKGEVIALDKILTKVNKLKQNASLLGLHSiRAFCFDATkalklDTTDGI 165
Cdd:PRK10901  237 ATLLAPQNGERVLDACAAPGGKTAHILEL-APQAQVVALDIDAQRLERVRENLQRLGLKA-TVIVGDAR-----DPAQWW 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 166 EGGPpflpesFDRIILDAPCSGMG-----------QRPNmactwtlkEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTI 234
Cdd:PRK10901  310 DGQP------FDRILLDAPCSATGvirrhpdikwlRRPE--------DIAALAALQSEILDALWPLLKPGGTLLYATCSI 375

                         170       180
                  ....*....|....*....|....
gi 1907143695 235 TLAENEEQVAWALRTFPCLQLQPQ 258
Cdd:PRK10901  376 LPEENEQQIKAFLARHPDAELLDT 399
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 80-251 6.81e-31

rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 121.55  E-value: 6.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  80 LPstVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATkalkl 159
Cdd:PRK11933  102 LP--VAALFADDNAPQRVLDMAAAPGSKTTQIAALMNNQGAIVANEYSASRVKVLHANISRCGVSNVALTHFDGR----- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 160 dttdgIEGGppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITL 236
Cdd:PRK11933  175 -----VFGA--ALPETFDAILLDAPCSGEGtvrKDPDALKNWSPESNLEIAATQRELIESAFHALKPGGTLVYSTCTLNR 247

                         170
                  ....*....|....*
gi 1907143695 237 AENEEQVAWALRTFP 251
Cdd:PRK11933  248 EENQAVCLWLKETYP 262
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
 74-249 1.12e-30

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 120.36  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  74 YIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDA 153
Cdd:PRK14903  218 LATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEKHAKRLKLSSIEIKIADA 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 154 TKALKldttdgieggppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYS 230
Cdd:PRK14903  298 ERLTE------------YVQDTFDRILVDAPCTSLGtarNHPEVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYS 365

                         170       180
                  ....*....|....*....|
gi 1907143695 231 TCTITLAENEEQV-AWALRT 249
Cdd:PRK14903  366 TCTVTKEENTEVVkRFVYEQ 385
PUA_NSun6-like cd21150
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ...
 1-61 9.08e-29

PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this subfamily contain PUA domains that co-occur with SAM-dependent methyltransferase domains and may play roles as cytosine-C(5)-methyltransferases specific for tRNAs or rRNAs. Nsun6 binding to its tRNA substrates requires the presence of a 3'-CCA sequence, which is precisely recognized primarily through interactions with residues from the PUA domain, where the molecular surface of the PUA domain snugly fits onto each nucleotide residue of the CCA end. Human RNA:m5C methyltransferase NSun6 (hNSun6) plays a major role in bone metastasis and could be a valuable therapeutic target for bone metastasis and therapy-resistant tumors.


Pssm-ID: 409292 [Multi-domain]  Cd Length: 92  Bit Score: 106.38  E-value: 9.08e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143695   1 MKAGDVISVYSDINGKCKKGA-KEFDGTKVFLGNGISELSRKDIFNGLPDLKGIGIRMTEPI 61
Cdd:cd21150    31 LKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKPSGIAVEMTEPV 92
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-230 1.23e-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: 49.35  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  96 KILDMCAAPGGKTTHTAAlmQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKAlkldttdgieggPPFLPES 175
Cdd:cd02440     1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907143695 176 FDRIILDAPCSgmgqrpnmactwtlkevtSYQPLQRKLLHVAVQLLKPGGVLVYS 230
Cdd:cd02440    67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 67-228 1.70e-07

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: 49.99  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  67 FDNVLPSYIFLQNLpstvvAHVLDPQPGEKILDMCAAPGgktTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHsI 146
Cdd:COG2226     1 FDRVAARYDGREAL-----LAALGLRPGARVLDLGCGTG---RLALALAERGARVTGVDISPEMLELARERAAEAGLN-V 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 147 RAFCFDATKalkldttdgieggPPFLPESFDRIIldapcsgmgqrpnmaCTWTLKEVTSyqplQRKLLHVAVQLLKPGGV 226
Cdd:COG2226    72 EFVVGDAED-------------LPFPDGSFDLVI---------------SSFVLHHLPD----PERALAEIARVLKPGGR 119


                  ..
gi 1907143695 227 LV 228
Cdd:COG2226   120 LV 121
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 93-229 2.82e-05

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 45.24  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  93 PGEKILDMCAAPGGKTTHTAALmqDKGEVIALDKILTKVNKLKQNASLLGL-HSIRAFCFDATKAlkldttdgieggPPF 171
Cdd:COG2520   180 PGERVLDMFAGVGPFSIPIAKR--SGAKVVAIDINPDAVEYLKENIRLNKVeDRVTPILGDAREV------------APE 245

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907143695 172 LPESFDRIILDAPCSGmgqrpnmactwtlkevtsyqplqRKLLHVAVQLLKPGGVLVY 229
Cdd:COG2520   246 LEGKADRIIMNLPHSA-----------------------DEFLDAALRALKPGGVIHY 280
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 92-231 1.13e-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: 42.24  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  92 QPGEKILD-MCaapGGKTT-HTAALMqdKGEVIALDkILTK-VNKLKQNASLLGLHSIRAFCFDATKalkldttdgiegg 168
Cdd:COG1041    25 KEGDTVLDpFC---GTGTIlIEAGLL--GRRVIGSD-IDPKmVEGARENLEHYGYEDADVIRGDARD------------- 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907143695 169 PPFLPESFDRIILDAPcsgMGQRPnmacTWTLKEVTSyqpLQRKLLHVAVQLLKPGGVLVYST 231
Cdd:COG1041    86 LPLADESVDAIVTDPP---YGRSS----KISGEELLE---LYEKALEEAARVLKPGGRVVIVT 138
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 135-248 1.71e-04

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: 42.86  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 135 KQNASLLGL----HSIRAFCFDATKALKLDttdgieggppflPESFDRIILDAPcsgmgqrpnmacTWT-----LKEVts 205
Cdd:COG1092   256 KENAALNGLddrhEFVQADAFDWLRELARE------------GERFDLIILDPP------------AFAkskkdLFDA-- 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907143695 206 yqplQR---KLLHVAVQLLKPGGVLVYSTCT--ITLAENEEQVAWALR 248
Cdd:COG1092   310 ----QRdykDLNRLALKLLAPGGILVTSSCSrhFSLDLFLEILARAAR 353
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 93-231 6.20e-04

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: 39.23  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  93 PGEKILDMCAAPGgkttHTAALMQDKG-EVIALDKILTKVNKLKQNASLLGlhsIRAFCFDATKAlkldttdgieggpPF 171
Cdd:COG2227    24 AGGRVLDVGCGTG----RLALALARRGaDVTGVDISPEALEIARERAAELN---VDFVQGDLEDL-------------PL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 172 LPESFDRIIldapCSgmgqrpnmactwtlkEVTSYQPLQRKLLHVAVQLLKPGGVLVYST 231
Cdd:COG2227    84 EDGSFDLVI----CS---------------EVLEHLPDPAALLRELARLLKPGGLLLLST 124
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 93-228 1.42e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 39.11  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  93 PGEKILDMCAAPGGKTthTAALMQDKGEVIALDKILTKVNKLKQNAsllGLHSIRAfcfDATkalKLDTTDGIEggpPFL 172
Cdd:pfam01728  21 PGKTVLDLGAAPGGWS--QVALQRGAGKVVGVDLGPMQLWKPRNDP---GVTFIQG---DIR---DPETLDLLE---ELL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907143695 173 PESFDRIILDApcsgmgqRPNMACTWTLKEVTSYQpLQRKLLHVAVQLLKPGGVLV 228
Cdd:pfam01728  87 GRKVDLVLSDG-------SPFISGNKVLDHLRSLD-LVKAALEVALELLRKGGNFV 134
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 68-230 3.13e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.36  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  68 DNVLPSYIFLqnlpstvVAHVLDPQPGEKILDMCAAPGgktTHTAALMQ-DKGEVIALDKILTKVNKLKQNASLLGLHSI 146
Cdd:COG0500     8 DELLPGLAAL-------LALLERLPKGGRVLDLGCGTG---RNLLALAArFGGRVIGIDLSPEAIALARARAAKAGLGNV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 147 RAFCFDATKALKLDttdgieggppflPESFDRIILdapcsgmgqrpNMACTWTLKEVtsyqplQRKLLHVAVQLLKPGGV 226
Cdd:COG0500    78 EFLVADLAELDPLP------------AESFDLVVA-----------FGVLHHLPPEE------REALLRELARALKPGGV 128


                  ....
gi 1907143695 227 LVYS 230
Cdd:COG0500   129 LLLS 132
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 93-232 3.23e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.40  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  93 PGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRafcFDATKALKLDTTdgieggppFL 172
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVE---FEQGDIEELPEL--------LE 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695 173 PESFDRIILDapcsgmgqrpnmactwtlkEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTC 232
Cdd:pfam13847  72 DDKFDVVISN-------------------CVLNHIPDPDKVLQEILRVLKPGGRLIISDP 112
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 97-225 5.56e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 35.62  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143695  97 ILDMCAAPGgktTHTAALMQDKG-EVIALDKILTKVNKLKQNASLLGLHsIRAFCFDATKalkldttdgieggPPFLPES 175
Cdd:pfam13649   1 VLDLGCGTG---RLTLALARRGGaRVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAED-------------LPFPDGS 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907143695 176 FDRIIldapcsgmgqrpnmaCTWTLKEVTsyQPLQRKLLHVAVQLLKPGG 225
Cdd:pfam13649  64 FDLVV---------------SSGVLHHLP--DPDLEAALREIARVLKPGG 96
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
92-125 7.71e-03

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 37.02  E-value: 7.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907143695  92 QPGEKILDMCAAPGGKTTHTAALMQDKGEVIALD 125
Cdd:PRK11188   50 KPGMTVVDLGAAPGGWSQYAVTQIGDKGRVIACD 83
 
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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