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Conserved domains on  [gi|1593795265|ref|NP_001356005|]
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putative methyltransferase NSUN4 isoform b [Mus musculus]

Protein Classification

NOL1/NOP2/SUN domain family protein( domain architecture ID 1003105)

NOL1/NOP2/SUN domain (NSUN) family protein such as mammalian nucleolar protein NOP2 which is required for nucleolar maturation and ribosome biogenesis

Gene Ontology:  GO:0003723|GO:0000027|GO:0008173|GO:0001510

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
nop2p super family cl33194
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 103-274 2.37e-34

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


The actual alignment was detected with superfamily member TIGR00446:

Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 126.43  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 103 YYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSTSRTgrlqKVLHSYVPqdiREG-N 177
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 178 QVRVTSWDGRKWGELeGDTYDRVLVDVPCTTDrHSLHEEENNIFQRSrKKERQMLPMLQVQLLAAGLLATKPGGHVVYST 257
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 1593795265 258 CSLSHLQNEYVVQGAIE 274
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
 
Name Accession Description Interval E-value
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 103-274 2.37e-34

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


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 126.43  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 103 YYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSTSRTgrlqKVLHSYVPqdiREG-N 177
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 178 QVRVTSWDGRKWGELeGDTYDRVLVDVPCTTDrHSLHEEENNIFQRSrKKERQMLPMLQVQLLAAGLLATKPGGHVVYST 257
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 1593795265 258 CSLSHLQNEYVVQGAIE 274
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 83-274 2.82e-34

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: 130.13  E-value: 2.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265  83 SRGDVSRFPPARLGslglmDYYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQ----TGccrNLAANDLSTSRT 158
Cdd:COG0144   216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAElmgnKG---RVVAVDISEHRL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 159 GRLQKVLHsyvpqdiREG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslHEEennifQRSRKKER--QML 232
Cdd:COG0144   288 KRLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEdiAEL 353

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1593795265 233 PMLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIE 274
Cdd:COG0144   354 AALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLA 395
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 114-273 5.14e-27

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: 105.20  E-value: 5.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 114 VLALGLQHGDTVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSTSRTGRLQKVLHsyvpqdiREGNQ-VRVTSWDGRKWGE 191
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGVTnTIILNGDGRQPDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 192 -LEGDTYDRVLVDVPCT----TDRHSlheeenNIFQRSRKKERQMLPMLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNE 266
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147


                  ....*..
gi 1593795265 267 YVVQGAI 273
Cdd:pfam01189 148 AVIEYFL 154
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 94-298 1.99e-22

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


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 97.29  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265  94 RLGSL-----GLMdyYLMDAASLLPVLAL--GLQHGDTVLDLCAAPGGKTLallQTGCCRN----LAANDLSTSRTgrlq 162
Cdd:PRK11933   81 PLGNTaehlsGLF--YIQEASSMLPVAALfaDDNAPQRVLDMAAAPGSKTT---QIAALMNnqgaIVANEYSASRV---- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 163 KVLHSYVPqdiREG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT------TDRHSLH----EEENNIFQrsrkkerqm 231
Cdd:PRK11933  152 KVLHANIS---RCGvSNVALTHFDGRVFGAALPETFDAILLDAPCSgegtvrKDPDALKnwspESNLEIAA--------- 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593795265 232 lpmLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGaielLANQYNIKVQVEDLShfrKLFMD 298
Cdd:PRK11933  220 ---TQRELIESAFHALKPGGTLVYSTCTLNREENQAVCLW----LKETYPDAVEFEPLG---DLFPG 276
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 124-256 4.18e-06

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 45.11  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 124 TVLDLCAAPGGKTLALLQTGCCRNLaANDLSTSRTGRLQKVlhsyvpQDIREGNQVRVTSWDGRKWGELEGDTYDRVLVD 203
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVT-GVDISPVALELARKA------AAALLADNVEVLKGDAEELPPEADESFDVIISD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1593795265 204 VPCttdrhslheeennifqrsrkkerQMLPMLQVQLLAAGLLATKPGGHVVYS 256
Cdd:cd02440    74 PPL-----------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 103-274 2.37e-34

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


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 126.43  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 103 YYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSTSRTgrlqKVLHSYVPqdiREG-N 177
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 178 QVRVTSWDGRKWGELeGDTYDRVLVDVPCTTDrHSLHEEENNIFQRSrKKERQMLPMLQVQLLAAGLLATKPGGHVVYST 257
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 1593795265 258 CSLSHLQNEYVVQGAIE 274
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 83-274 2.82e-34

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: 130.13  E-value: 2.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265  83 SRGDVSRFPPARLGslglmDYYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQ----TGccrNLAANDLSTSRT 158
Cdd:COG0144   216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAElmgnKG---RVVAVDISEHRL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 159 GRLQKVLHsyvpqdiREG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslHEEennifQRSRKKER--QML 232
Cdd:COG0144   288 KRLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEdiAEL 353

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1593795265 233 PMLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIE 274
Cdd:COG0144   354 AALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLA 395
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 114-273 5.14e-27

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: 105.20  E-value: 5.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 114 VLALGLQHGDTVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSTSRTGRLQKVLHsyvpqdiREGNQ-VRVTSWDGRKWGE 191
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGVTnTIILNGDGRQPDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 192 -LEGDTYDRVLVDVPCT----TDRHSlheeenNIFQRSRKKERQMLPMLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNE 266
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147


                  ....*..
gi 1593795265 267 YVVQGAI 273
Cdd:pfam01189 148 AVIEYFL 154
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 94-298 1.99e-22

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


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 97.29  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265  94 RLGSL-----GLMdyYLMDAASLLPVLAL--GLQHGDTVLDLCAAPGGKTLallQTGCCRN----LAANDLSTSRTgrlq 162
Cdd:PRK11933   81 PLGNTaehlsGLF--YIQEASSMLPVAALfaDDNAPQRVLDMAAAPGSKTT---QIAALMNnqgaIVANEYSASRV---- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 163 KVLHSYVPqdiREG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT------TDRHSLH----EEENNIFQrsrkkerqm 231
Cdd:PRK11933  152 KVLHANIS---RCGvSNVALTHFDGRVFGAALPETFDAILLDAPCSgegtvrKDPDALKnwspESNLEIAA--------- 219

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593795265 232 lpmLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGaielLANQYNIKVQVEDLShfrKLFMD 298
Cdd:PRK11933  220 ---TQRELIESAFHALKPGGTLVYSTCTLNREENQAVCLW----LKETYPDAVEFEPLG---DLFPG 276
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
103-270 1.29e-21

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 94.86  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 103 YYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKT--LA--LLQTGccrNLAANDLSTSRTgRLqkvlhsyvpqdIREG-- 176
Cdd:PRK14902  232 ITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTthIAelLKNTG---KVVALDIHEHKL-KL-----------IEENak 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 177 ----NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslheeENNIfqRSRKKERQM--LPMLQVQLL--AAGLL 245
Cdd:PRK14902  297 rlglTNIETKALDARKVHEKFAEKFDKILVDAPCSglgVIRR-----KPDI--KYNKTKEDIesLQEIQLEILesVAQYL 369

                         170       180
                  ....*....|....*....|....*
gi 1593795265 246 atKPGGHVVYSTCSLSHLQNEYVVQ 270
Cdd:PRK14902  370 --KKGGILVYSTCTIEKEENEEVIE 392
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 107-270 8.97e-19

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: 86.46  E-value: 8.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 107 DAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQTGCCRNLAANDLSTSrtgRLQKVlhsYVPQDiREGNQVRVTSWDG 186
Cdd:TIGR00563 224 DASAQWVATWLAPQNEETILDACAAPGGKTTHILELAPQAQVVALDIHEH---RLKRV---YENLK-RLGLTIKAETKDG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 187 RK-----WGELEgdTYDRVLVDVPC----TTDRHSlheeenNIFQRSRKKERQMLPMLQVQLLAAGLLATKPGGHVVYST 257
Cdd:TIGR00563 297 DGrgpsqWAENE--QFDRILLDAPCsatgVIRRHP------DIKWLRKPRDIAELAELQSEILDAIWPLLKTGGTLVYAT 368

                         170
                  ....*....|...
gi 1593795265 258 CSLSHLQNEYVVQ 270
Cdd:TIGR00563 369 CSVLPEENSEQIK 381
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
107-259 1.19e-16

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


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 80.23  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 107 DAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQTGCCRNLAANDLSTSRTGRLQKVLhsyvpQDIREGNQVRVTswDG 186
Cdd:PRK10901  230 DAAAQLAATLLAPQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQRLERVRENL-----QRLGLKATVIVG--DA 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 187 RK----WGeleGDTYDRVLVDVPCTTD----RHS---LHEEENNIFQrsrkkerqmLPMLQVQLLAA--GLLatKPGGHV 253
Cdd:PRK10901  303 RDpaqwWD---GQPFDRILLDAPCSATgvirRHPdikWLRRPEDIAA---------LAALQSEILDAlwPLL--KPGGTL 368


                  ....*.
gi 1593795265 254 VYSTCS 259
Cdd:PRK10901  369 LYATCS 374
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 107-287 4.91e-16

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 78.43  E-value: 4.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 107 DAASLLPVLALGLQHGDTVLDLCAAPGGKT--LALLqtgccrnlaAND----LSTSRT-GRLQKV--------LHSyvpq 171
Cdd:PRK14901  238 DRSAQLVAPLLDPQPGEVILDACAAPGGKTthIAEL---------MGDqgeiWAVDRSaSRLKKLqenaqrlgLKS---- 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 172 diregnqVRVTSWDGRKWGELEGD---TYDRVLVDVPC----TTDRHSlheeenNIFQRSRKKERQMLPMLQVQLLAAGL 244
Cdd:PRK14901  305 -------IKILAADSRNLLELKPQwrgYFDRILLDAPCsglgTLHRHP------DARWRQTPEKIQELAPLQAELLESLA 371

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1593795265 245 LATKPGGHVVYSTCSLSHLQNEYVVQgaiELLANQYNIKVQVE 287
Cdd:PRK14901  372 PLLKPGGTLVYATCTLHPAENEAQIE---QFLARHPDWKLEPP 411
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
 107-270 3.21e-15

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 76.06  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 107 DAASLLPVLaLGLQHGDTVLDLCAAPGGKTLALLQTGCCR-NLAANDLSTSRTGRLQKvlhsyvpQDIREG-NQVRVTSW 184
Cdd:PRK14903  224 ESSQIVPLL-MELEPGLRVLDTCAAPGGKTTAIAELMKDQgKILAVDISREKIQLVEK-------HAKRLKlSSIEIKIA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 185 DGRKWGELEGDTYDRVLVDVPCTtdrhSLHEEENN--IFQRSRKKERQMLPMLQVQLLAAGLLATKPGGHVVYSTCSLSH 262
Cdd:PRK14903  296 DAERLTEYVQDTFDRILVDAPCT----SLGTARNHpeVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYSTCTVTK 371


                  ....*...
gi 1593795265 263 LQNEYVVQ 270
Cdd:PRK14903  372 EENTEVVK 379
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 77-266 4.07e-12

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 66.62  E-value: 4.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265  77 LRCFTFSRgDVSRFPPA-RLGSLGLMDyylmdAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQ----TGccrNLAAN 151
Cdd:PRK14904  211 LPNFFLSK-DFSLFEPFlKLGLVSVQN-----PTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAElmqnRG---QITAV 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 152 DLSTSRTGRLQKvLHSYVPQDI---REGNQVRVTSwdgrkwgeleGDTYDRVLVDVPCT-----TDRHSLHeeenniFQR 223
Cdd:PRK14904  282 DRYPQKLEKIRS-HASALGITIietIEGDARSFSP----------EEQPDAILLDAPCTgtgvlGRRAELR------WKL 344

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1593795265 224 SRKKERQmLPMLQVQLL--AAGLLatKPGGHVVYSTCSLSHLQNE 266
Cdd:PRK14904  345 TPEKLAE-LVGLQAELLdhAASLL--KPGGVLVYATCSIEPEENE 386
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 124-256 4.18e-06

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 45.11  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 124 TVLDLCAAPGGKTLALLQTGCCRNLaANDLSTSRTGRLQKVlhsyvpQDIREGNQVRVTSWDGRKWGELEGDTYDRVLVD 203
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVT-GVDISPVALELARKA------AAALLADNVEVLKGDAEELPPEADESFDVIISD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1593795265 204 VPCttdrhslheeennifqrsrkkerQMLPMLQVQLLAAGLLATKPGGHVVYS 256
Cdd:cd02440    74 PPL-----------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
PRK14967 PRK14967
putative methyltransferase; Provisional
 110-212 1.54e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 110 SLLPVLAL---GLQHGDTVLDLCAAPGGKTLALLQTGCCRnLAANDLS--TSRTGRLQKVLHSyVPQDIREGNQVRVtsw 184
Cdd:PRK14967   22 TQLLADALaaeGLGPGRRVLDLCTGSGALAVAAAAAGAGS-VTAVDISrrAVRSARLNALLAG-VDVDVRRGDWARA--- 96

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1593795265 185 dgrkwgeLEGDTYDRVLVD---VPCTTDRHS 212
Cdd:PRK14967   97 -------VEFRPFDVVVSNppyVPAPPDAPP 120
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 119-254 2.69e-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: 38.34  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795265 119 LQHGDTVLDLCAAPGGKTLALLQTGCCRNLAAnDLSTSRTGRLQKVLHSYVPQ-DIREGNQVrvtswdgRKWGELEGDTY 197
Cdd:pfam01728  19 LKPGKTVLDLGAAPGGWSQVALQRGAGKVVGV-DLGPMQLWKPRNDPGVTFIQgDIRDPETL-------DLLEELLGRKV 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593795265 198 DRVLVDV-PCTTDRHSLHEEennifqrsrkkerqmlpmLQVQL----LAAGLLATKPGGHVV 254
Cdd:pfam01728  91 DLVLSDGsPFISGNKVLDHL------------------RSLDLvkaaLEVALELLRKGGNFV 134
 
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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