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Conserved domains on  [gi|489113500|ref|WP_003023353|]
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MULTISPECIES: 16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ [Citrobacter]

Protein Classification

16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ( domain architecture ID 10013632)

16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ specifically methylates the guanosine in position 1516 of 16S rRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10742 PRK10742
16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ;
1-249 0e+00

16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ;


:

Pssm-ID: 236749  Cd Length: 250  Bit Score: 510.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500   1 MKICLVDETGAGDGALSVLAARWGLEHDEDNLMALVMTTAHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAK 80
Cdd:PRK10742   1 MKICLIDETGAGDGALSVLAARWGLEHDEDNLMALVLTPEHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500  81 AVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADPEIGPWLQERLQLIHASSLTALTD 160
Cdd:PRK10742  81 AVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADAEIGGWLQERLQLIHASSLTALTD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500 161 ITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARQLATKRVVVKRPDYAPPLADVATPNAVVTKGH 240
Cdd:PRK10742 161 ITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARLLATKRVVVKRPDYAPPLAGVATPNAVVTKGH 240

                 ....*....
gi 489113500 241 RFDIYAGTA 249
Cdd:PRK10742 241 RFDIYAGTP 249
 
Name Accession Description Interval E-value
PRK10742 PRK10742
16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ;
1-249 0e+00

16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ;


Pssm-ID: 236749  Cd Length: 250  Bit Score: 510.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500   1 MKICLVDETGAGDGALSVLAARWGLEHDEDNLMALVMTTAHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAK 80
Cdd:PRK10742   1 MKICLIDETGAGDGALSVLAARWGLEHDEDNLMALVLTPEHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500  81 AVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADPEIGPWLQERLQLIHASSLTALTD 160
Cdd:PRK10742  81 AVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADAEIGGWLQERLQLIHASSLTALTD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500 161 ITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARQLATKRVVVKRPDYAPPLADVATPNAVVTKGH 240
Cdd:PRK10742 161 ITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARLLATKRVVVKRPDYAPPLAGVATPNAVVTKGH 240

                 ....*....
gi 489113500 241 RFDIYAGTA 249
Cdd:PRK10742 241 RFDIYAGTP 249
SAM_MT pfam04445
Putative SAM-dependent methyltransferase; This is a family of putative SAM-dependent ...
19-245 9.26e-151

Putative SAM-dependent methyltransferase; This is a family of putative SAM-dependent methyltransferases.


Pssm-ID: 427952  Cd Length: 230  Bit Score: 419.32  E-value: 9.26e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500   19 LAARWGLEHDEDNLMALVMTTAHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAKAVGIKGDYLPDVVDATAG 98
Cdd:pfam04445   2 LAQRWGLPHDPNSGFALVLTEERLELRKLDEPKLGAVYVDFVSGAAAHRRKFGGGRGQAIAKAVGIKGGYLPTVLDATAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500   99 LGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADPEIGPWLQERLQLIHASSLTALTDITPRPQVVYLDPMFPHKQ 178
Cdd:pfam04445  82 LGRDAFVLASLGCKVTLIERHPVVAALLEDGLQRAYQDPEIGPWIAARMQLLHGSSIEALAALQQYPDVVYLDPMYPHRK 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489113500  179 KSALVKKEMRVFQSLVGPDLDADGLLEPARQLATKRVVVKRPDYAPPLADVATPNAVVTKGHRFDIY 245
Cdd:pfam04445 162 KSALVKKEMRVFQQLVGADLDADALLEPALALAKKRVVVKRPDYAPFLAGKKPSASIETKNHRFDIY 228
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
91-176 2.70e-04

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: 39.34  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500  91 DVVDATAGLGRDAFVLAS-VGCRVRMLERNPVVAALLDDGLARGyadpeigpwLQERLQLIHASSLTALTDITPRPQVVY 169
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAAL---------LADNVEVLKGDAEELPPEADESFDVII 71

                 ....*..
gi 489113500 170 LDPMFPH 176
Cdd:cd02440   72 SDPPLHH 78
 
Name Accession Description Interval E-value
PRK10742 PRK10742
16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ;
1-249 0e+00

16S rRNA (guanine(1516)-N(2))-methyltransferase RsmJ;


Pssm-ID: 236749  Cd Length: 250  Bit Score: 510.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500   1 MKICLVDETGAGDGALSVLAARWGLEHDEDNLMALVMTTAHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAK 80
Cdd:PRK10742   1 MKICLIDETGAGDGALSVLAARWGLEHDEDNLMALVLTPEHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500  81 AVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADPEIGPWLQERLQLIHASSLTALTD 160
Cdd:PRK10742  81 AVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADAEIGGWLQERLQLIHASSLTALTD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500 161 ITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARQLATKRVVVKRPDYAPPLADVATPNAVVTKGH 240
Cdd:PRK10742 161 ITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLEPARLLATKRVVVKRPDYAPPLAGVATPNAVVTKGH 240

                 ....*....
gi 489113500 241 RFDIYAGTA 249
Cdd:PRK10742 241 RFDIYAGTP 249
SAM_MT pfam04445
Putative SAM-dependent methyltransferase; This is a family of putative SAM-dependent ...
19-245 9.26e-151

Putative SAM-dependent methyltransferase; This is a family of putative SAM-dependent methyltransferases.


Pssm-ID: 427952  Cd Length: 230  Bit Score: 419.32  E-value: 9.26e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500   19 LAARWGLEHDEDNLMALVMTTAHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAKAVGIKGDYLPDVVDATAG 98
Cdd:pfam04445   2 LAQRWGLPHDPNSGFALVLTEERLELRKLDEPKLGAVYVDFVSGAAAHRRKFGGGRGQAIAKAVGIKGGYLPTVLDATAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500   99 LGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADPEIGPWLQERLQLIHASSLTALTDITPRPQVVYLDPMFPHKQ 178
Cdd:pfam04445  82 LGRDAFVLASLGCKVTLIERHPVVAALLEDGLQRAYQDPEIGPWIAARMQLLHGSSIEALAALQQYPDVVYLDPMYPHRK 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489113500  179 KSALVKKEMRVFQSLVGPDLDADGLLEPARQLATKRVVVKRPDYAPPLADVATPNAVVTKGHRFDIY 245
Cdd:pfam04445 162 KSALVKKEMRVFQQLVGADLDADALLEPALALAKKRVVVKRPDYAPFLAGKKPSASIETKNHRFDIY 228
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
91-176 2.70e-04

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: 39.34  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113500  91 DVVDATAGLGRDAFVLAS-VGCRVRMLERNPVVAALLDDGLARGyadpeigpwLQERLQLIHASSLTALTDITPRPQVVY 169
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAAL---------LADNVEVLKGDAEELPPEADESFDVII 71

                 ....*..
gi 489113500 170 LDPMFPH 176
Cdd:cd02440   72 SDPPLHH 78
 
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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