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Conserved domains on  [gi|2217345401|ref|XP_047304640|]
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tRNA (cytosine(34)-C(5))-methyltransferase, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

RsmB/NOP family class I SAM-dependent RNA methyltransferase( domain architecture ID 1000767)

RsmB/NOP family class I SAM-dependent RNA methyltransferase similar to Homo sapiens mitochondrial tRNA (cytosine(34)-C(5))-methyltransferase, which mediates methylation of cytosine to 5-methylcytosine (m5C) at position 34 of mt-tRNA(Met), and to 5-methylcytosine rRNA methyltransferase NSUN4 involved in mitochondrial ribosome small subunit (SSU) maturation by methylation of mitochondrial 12S rRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RsmB super family cl33775
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
118-248 1.73e-23

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


The actual alignment was detected with superfamily member COG0144:

Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 98.54  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 118 AASLLPVLALELRDGEKVLDLCAAPGGKSIALLQCACP-GYLHCNEYDSLRLRWLRQTLesfipQPL-INVIKVSELDGR 195
Cdd:COG0144   236 EASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNkGRVVAVDISEHRLKRLRENL-----ARLgLSNVEVVVADAR 310
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217345401 196 KMGDAQPEMFDKVLVDAPCSN--------DRSWLFSSDSQKAscrisqrrnLPLLQIELLR 248
Cdd:COG0144   311 ELLEWLPGKFDRVLLDAPCSGtgtlrrhpDIKWRRTPEDIAE---------LAALQRELLD 362
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
118-248 1.73e-23

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: 98.54  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 118 AASLLPVLALELRDGEKVLDLCAAPGGKSIALLQCACP-GYLHCNEYDSLRLRWLRQTLesfipQPL-INVIKVSELDGR 195
Cdd:COG0144   236 EASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNkGRVVAVDISEHRLKRLRENL-----ARLgLSNVEVVVADAR 310
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217345401 196 KMGDAQPEMFDKVLVDAPCSN--------DRSWLFSSDSQKAscrisqrrnLPLLQIELLR 248
Cdd:COG0144   311 ELLEWLPGKFDRVLLDAPCSGtgtlrrhpDIKWRRTPEDIAE---------LAALQRELLD 362
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
98-216 1.54e-18

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


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 82.51  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401  98 GRIPseRHQIGNlkkYYLLNAASLLPVLALELRDGEKVLDLCAAPGGKSIALLQ-CACPGYLHCNEYDSLRLrwlrQTLE 176
Cdd:TIGR00446  43 GSTP--EYLFGY---YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlMKNKGCIVANEISKSRT----KALI 113
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217345401 177 SFIPQPLINVIKVSELDGRKMGDAQPEmFDKVLVDAPCSN 216
Cdd:TIGR00446 114 SNINRMGVLNTIVINADGRKFGAYLLK-FDAILLDAPCSG 152
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
119-215 1.75e-15

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 75.60  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 119 ASLLPVLALELRDGEKVLDLCAAPGGKSIallqcacpgylHCNEY-------DSL-----RLRWLRQTLESfipqpL-IN 185
Cdd:PRK14902  238 SSMLVAPALDPKGGDTVLDACAAPGGKTT-----------HIAELlkntgkvVALdihehKLKLIEENAKR-----LgLT 301
                          90       100       110
                  ....*....|....*....|....*....|
gi 2217345401 186 VIKVSELDGRKMGDAQPEMFDKVLVDAPCS 215
Cdd:PRK14902  302 NIETKALDARKVHEKFAEKFDKILVDAPCS 331
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
124-215 1.09e-14

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: 70.53  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 124 VLALELRDGEKVLDLCAAPGGKSIALLQ-CACPGYLHCNEYDSLRLRWLRQTLESFipqPLINVIkVSELDGRKMGD-AQ 201
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIHRL---GVTNTI-ILNGDGRQPDQwLG 76
                          90
                  ....*....|....
gi 2217345401 202 PEMFDKVLVDAPCS 215
Cdd:pfam01189  77 GVLFDRILLDAPCS 90
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
118-248 1.73e-23

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: 98.54  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 118 AASLLPVLALELRDGEKVLDLCAAPGGKSIALLQCACP-GYLHCNEYDSLRLRWLRQTLesfipQPL-INVIKVSELDGR 195
Cdd:COG0144   236 EASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNkGRVVAVDISEHRLKRLRENL-----ARLgLSNVEVVVADAR 310
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217345401 196 KMGDAQPEMFDKVLVDAPCSN--------DRSWLFSSDSQKAscrisqrrnLPLLQIELLR 248
Cdd:COG0144   311 ELLEWLPGKFDRVLLDAPCSGtgtlrrhpDIKWRRTPEDIAE---------LAALQRELLD 362
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
98-216 1.54e-18

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


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 82.51  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401  98 GRIPseRHQIGNlkkYYLLNAASLLPVLALELRDGEKVLDLCAAPGGKSIALLQ-CACPGYLHCNEYDSLRLrwlrQTLE 176
Cdd:TIGR00446  43 GSTP--EYLFGY---YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlMKNKGCIVANEISKSRT----KALI 113
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217345401 177 SFIPQPLINVIKVSELDGRKMGDAQPEmFDKVLVDAPCSN 216
Cdd:TIGR00446 114 SNINRMGVLNTIVINADGRKFGAYLLK-FDAILLDAPCSG 152
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
119-215 1.75e-15

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 75.60  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 119 ASLLPVLALELRDGEKVLDLCAAPGGKSIallqcacpgylHCNEY-------DSL-----RLRWLRQTLESfipqpL-IN 185
Cdd:PRK14902  238 SSMLVAPALDPKGGDTVLDACAAPGGKTT-----------HIAELlkntgkvVALdihehKLKLIEENAKR-----LgLT 301
                          90       100       110
                  ....*....|....*....|....*....|
gi 2217345401 186 VIKVSELDGRKMGDAQPEMFDKVLVDAPCS 215
Cdd:PRK14902  302 NIETKALDARKVHEKFAEKFDKILVDAPCS 331
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
124-215 1.09e-14

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: 70.53  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 124 VLALELRDGEKVLDLCAAPGGKSIALLQ-CACPGYLHCNEYDSLRLRWLRQTLESFipqPLINVIkVSELDGRKMGD-AQ 201
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIHRL---GVTNTI-ILNGDGRQPDQwLG 76
                          90
                  ....*....|....
gi 2217345401 202 PEMFDKVLVDAPCS 215
Cdd:pfam01189  77 GVLFDRILLDAPCS 90
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
113-215 1.73e-12

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


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 66.86  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 113 YYLLNAASLLPVLAL--ELRDGEKVLDLCAAPGGKS--IALL---QcacpGYLHCNEYDSLRLRWLRQTLE----Sfipq 181
Cdd:PRK11933   93 FYIQEASSMLPVAALfaDDNAPQRVLDMAAAPGSKTtqIAALmnnQ----GAIVANEYSASRVKVLHANISrcgvS---- 164
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217345401 182 pliNVIkVSELDGRKMGDAQPEMFDKVLVDAPCS 215
Cdd:PRK11933  165 ---NVA-LTHFDGRVFGAALPETFDAILLDAPCS 194
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
117-215 4.79e-12

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: 65.27  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 117 NAASLLPVLALELRDGEKVLDLCAAPGGKSIALLQCACPGYLHCNEYDSLRLRWLRQTLESfipqpLINVIKVSELDGRK 196
Cdd:TIGR00563 224 DASAQWVATWLAPQNEETILDACAAPGGKTTHILELAPQAQVVALDIHEHRLKRVYENLKR-----LGLTIKAETKDGDG 298
                          90       100
                  ....*....|....*....|..
gi 2217345401 197 MGDAQP---EMFDKVLVDAPCS 215
Cdd:TIGR00563 299 RGPSQWaenEQFDRILLDAPCS 320
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
118-215 7.39e-12

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


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 64.83  E-value: 7.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 118 AASLLpvlalELRDGEKVLDLCAAPGGKSIALLQCACPGYLHCNEYDSLRLRWLRQTLESFIPQPLINVikvseldgrkm 197
Cdd:PRK10901  236 AATLL-----APQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQRLERVRENLQRLGLKATVIV----------- 299
                          90       100
                  ....*....|....*....|....*
gi 2217345401 198 GDA-------QPEMFDKVLVDAPCS 215
Cdd:PRK10901  300 GDArdpaqwwDGQPFDRILLDAPCS 324
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
127-215 8.24e-10

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 58.79  E-value: 8.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 127 LELRDGEKVLDLCAAPGGKS--IALLQ------CACPGYLHcneydslRLRWLRQTLESFipqpLINVIKVSELDGRKMG 198
Cdd:PRK14901  248 LDPQPGEVILDACAAPGGKTthIAELMgdqgeiWAVDRSAS-------RLKKLQENAQRL----GLKSIKILAADSRNLL 316
                          90       100
                  ....*....|....*....|
gi 2217345401 199 DAQPE---MFDKVLVDAPCS 215
Cdd:PRK14901  317 ELKPQwrgYFDRILLDAPCS 336
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
118-266 1.97e-09

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 57.58  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 118 AASLLPVLaLELRDGEKVLDLCAAPGGKSIALLQ-CACPGYLHCNEYDSLRLrwlrQTLESFIPQPLINVIKVSELDGRK 196
Cdd:PRK14903  225 SSQIVPLL-MELEPGLRVLDTCAAPGGKTTAIAElMKDQGKILAVDISREKI----QLVEKHAKRLKLSSIEIKIADAER 299
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217345401 197 MGDAQPEMFDKVLVDAPCSNdrswlfssdsqkascrISQRRNLPllqiELLR--ERERFKELAYTAMKAKSQ 266
Cdd:PRK14903  300 LTEYVQDTFDRILVDAPCTS----------------LGTARNHP----EVLRrvNKEDFKKLSEIQLRIVSQ 351
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
117-215 4.54e-09

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 56.61  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345401 117 NAASLLPVLALELRDGEKVLDLCAAPGGKSIALLQcacpgyLHCNE--------YDS--LRLRWLRQTLEsfipqplINV 186
Cdd:PRK14904  236 NPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAE------LMQNRgqitavdrYPQklEKIRSHASALG-------ITI 302
                          90       100
                  ....*....|....*....|....*....
gi 2217345401 187 IKVSELDGRKMgdAQPEMFDKVLVDAPCS 215
Cdd:PRK14904  303 IETIEGDARSF--SPEEQPDAILLDAPCT 329
 
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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