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Conserved domains on  [gi|1168757051|ref|WP_080327664|]
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23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI [Enterobacter chuandaensis]

Protein Classification

23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI( domain architecture ID 11487669)

23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI methylates 23S rRNA at the 5-position of cytosine 1962

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
1-396 0e+00

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


:

Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 867.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051   1 MSVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDKDETIDIDFFV 80
Cdd:PRK15128    1 MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDESIDIAFFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051  81 RRLQQAQQWRDWLAKRDGLDSYRLIAGESDGLPGVTIDRFGNFLVLQLLSAGAEYQRAALISALQTLFPECAIYDRSDVA 160
Cdd:PRK15128   81 RRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRQYVADKRVLNCFSYTGGFAVSALM 240
Cdd:PRK15128  161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 241 GGCAQVVSVDTSQEALDVAKQNVELNKLDLSKAEFVRDDVFKLLRKYRDGGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320
Cdd:PRK15128  241 GGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168757051 321 INMLAIQLLNPGGVLLTFSCSGLMTTDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
Cdd:PRK15128  321 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
 
Name Accession Description Interval E-value
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
1-396 0e+00

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


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 867.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051   1 MSVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDKDETIDIDFFV 80
Cdd:PRK15128    1 MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDESIDIAFFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051  81 RRLQQAQQWRDWLAKRDGLDSYRLIAGESDGLPGVTIDRFGNFLVLQLLSAGAEYQRAALISALQTLFPECAIYDRSDVA 160
Cdd:PRK15128   81 RRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRQYVADKRVLNCFSYTGGFAVSALM 240
Cdd:PRK15128  161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 241 GGCAQVVSVDTSQEALDVAKQNVELNKLDLSKAEFVRDDVFKLLRKYRDGGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320
Cdd:PRK15128  241 GGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168757051 321 INMLAIQLLNPGGVLLTFSCSGLMTTDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
Cdd:PRK15128  321 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 4-395 0e+00

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: 564.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051   4 RLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDKDETIDIDFFVRRL 83
Cdd:COG1092     1 KVRLKPGKERRLRRGHPWVFSNEIDRVEGELEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEPIDAAFFANRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051  84 QQAQQWRDWLAKRDGLDSYRLIAGESDGLPGVTIDRFGNFLVLQLLSAGAEYQRAALISALQTLFPECAIYDRSDVAVRK 163
Cdd:COG1092    81 RKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEALVEVLGPEGIYLRSDVRVRQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 164 KEGMELTQGPVTGELPPAlLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRQYVADKRVLNCFSYTGGFAVSALMGGC 243
Cdd:COG1092   161 LEGLPQYEGVLYGEAPEE-VEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSVHAAAGGA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 244 AQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLLRKYRDGGEKFDVIVMDPPKFVENKSQLMGACRGYKDINM 323
Cdd:COG1092   240 KSVTSVDLSATALEWAKENAALNGLD-DRHEFVQADAFDWLRELAREGERFDLIILDPPAFAKSKKDLFDAQRDYKDLNR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168757051 324 LAIQLLNPGGVLLTFSCSGLMTTDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRV 395
Cdd:COG1092   319 LALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLRV 390
RlmI_M_like cd11572
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ...
 77-176 1.70e-36

Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or central domain is typically found between an N-terminal PUA domain and a C-terminal SAM-dependent methyltransferase domain, such as in the Escherichia coli ribosomal RNA large subunit methyltransferase RlmI (YccW). It may be involved in binding to the RNA substrate.


Pssm-ID: 211413 [Multi-domain]  Cd Length: 99  Bit Score: 128.35  E-value: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051  77 DFFVRRLQQAQQWRDWLAkRDGLDSYRLIAGESDGLPGVTIDRFGNFLVLQLLSAGAEYQRAALISALQTLFPECAIYDR 156
Cdd:cd11572     1 AFFKRRIEKALALRKRLL-LDDTNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKELLGPKGIYER 79

                          90       100
                  ....*....|....*....|
gi 1168757051 157 SDVAVRKKEGMELTQGPVTG 176
Cdd:cd11572    80 SDAAVRELEGLPEEVGVLYG 99
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
 185-377 7.95e-28

S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.


Pssm-ID: 287624 [Multi-domain]  Cd Length: 286  Bit Score: 111.12  E-value: 7.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 185 IEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRQYVADKRVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVE 264
Cdd:pfam10672  88 VVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARGSLNKGRDNHR 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 265 LNKLDLSKAEFVRDDVFKLLRKYRDGGEkFDVIVMDPPKFVENKSQLMgacRGYKDINMLAIQLLNPGGVLLTFSCSGLM 344
Cdd:pfam10672 168 LNGHDLGRVSFLGHDIFKSWGKIKKLGP-YDLVIIDPPSFQKGSFALT---KDYKKILRRLPELLVEGGTVLACVNSPAV 243

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1168757051 345 TTDLFQKIIADAAidagRDVQFIEQFRQAADHP 377
Cdd:pfam10672 244 GPDFLIEEMAEEA----PSLHFVERLDNPPEFP 272
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
4-67 1.24e-10

Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 57.27  E-value: 1.24e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168757051    4 RLVLAKGREKSLLRRHpWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWT 67
Cdd:smart00359   2 KVVVDDGAEKAILNGA-SLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKG 64
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 222-336 4.96e-07

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 50.81  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 222 KRVLNCFSYTGGFAVS-ALMGGCAQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLLRkyrdgGEKFDVIVMD 300
Cdd:TIGR00536 116 LHILDLGTGSGCIALAlAYEFPNAEVIAVDISPDALAVAEENAEKNQLE-HRVEFIQSNLFEPLA-----GQKIDIIVSN 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1168757051 301 PP-------------KFVENKSQLMGACRGYKD---INMLAIQLLNPGGVLL 336
Cdd:TIGR00536 190 PPyideedladlpnvVRFEPLLALVGGDDGLNIlrqIIELAPDYLKPNGFLV 241
 
Name Accession Description Interval E-value
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
1-396 0e+00

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


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 867.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051   1 MSVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDKDETIDIDFFV 80
Cdd:PRK15128    1 MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDESIDIAFFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051  81 RRLQQAQQWRDWLAKRDGLDSYRLIAGESDGLPGVTIDRFGNFLVLQLLSAGAEYQRAALISALQTLFPECAIYDRSDVA 160
Cdd:PRK15128   81 RRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRQYVADKRVLNCFSYTGGFAVSALM 240
Cdd:PRK15128  161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 241 GGCAQVVSVDTSQEALDVAKQNVELNKLDLSKAEFVRDDVFKLLRKYRDGGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320
Cdd:PRK15128  241 GGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168757051 321 INMLAIQLLNPGGVLLTFSCSGLMTTDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
Cdd:PRK15128  321 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 4-395 0e+00

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: 564.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051   4 RLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDKDETIDIDFFVRRL 83
Cdd:COG1092     1 KVRLKPGKERRLRRGHPWVFSNEIDRVEGELEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEPIDAAFFANRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051  84 QQAQQWRDWLAKRDGLDSYRLIAGESDGLPGVTIDRFGNFLVLQLLSAGAEYQRAALISALQTLFPECAIYDRSDVAVRK 163
Cdd:COG1092    81 RKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEALVEVLGPEGIYLRSDVRVRQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 164 KEGMELTQGPVTGELPPAlLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRQYVADKRVLNCFSYTGGFAVSALMGGC 243
Cdd:COG1092   161 LEGLPQYEGVLYGEAPEE-VEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSVHAAAGGA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 244 AQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLLRKYRDGGEKFDVIVMDPPKFVENKSQLMGACRGYKDINM 323
Cdd:COG1092   240 KSVTSVDLSATALEWAKENAALNGLD-DRHEFVQADAFDWLRELAREGERFDLIILDPPAFAKSKKDLFDAQRDYKDLNR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168757051 324 LAIQLLNPGGVLLTFSCSGLMTTDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRV 395
Cdd:COG1092   319 LALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLRV 390
RlmI_M_like cd11572
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ...
 77-176 1.70e-36

Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or central domain is typically found between an N-terminal PUA domain and a C-terminal SAM-dependent methyltransferase domain, such as in the Escherichia coli ribosomal RNA large subunit methyltransferase RlmI (YccW). It may be involved in binding to the RNA substrate.


Pssm-ID: 211413 [Multi-domain]  Cd Length: 99  Bit Score: 128.35  E-value: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051  77 DFFVRRLQQAQQWRDWLAkRDGLDSYRLIAGESDGLPGVTIDRFGNFLVLQLLSAGAEYQRAALISALQTLFPECAIYDR 156
Cdd:cd11572     1 AFFKRRIEKALALRKRLL-LDDTNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKELLGPKGIYER 79

                          90       100
                  ....*....|....*....|
gi 1168757051 157 SDVAVRKKEGMELTQGPVTG 176
Cdd:cd11572    80 SDAAVRELEGLPEEVGVLYG 99
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 60-340 1.91e-32

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 129.15  E-value: 1.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051  60 QIRARVWTFDKDETIDidfFVRRLQQ-AQQWRDWlAKRDGLDSYRLIagESDgLP--GVTIDRFGNFLVLQllsagaEY- 135
Cdd:PRK11783  379 TIAEESTSSDAEGAQD---FANRLRKnLKKLKKW-AKQEGIECYRLY--DAD-LPeyNVAVDRYGDWVVVQ------EYa 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 136 -----------QR-----AALISALQTlfpecaiyDRSDVA--VRKK-EGME----LTQgpvTGELppalLPIEEHGMKL 192
Cdd:PRK11783  446 apktideekarQRlfdalAATPEVLGI--------PPNKVVlkTRERqKGKNqyqkLAE---KGEF----LEVTEYGAKL 510

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 193 LVDIQGGHKTGYYLDQRDSRLATRQYVADKRVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDLSK 272
Cdd:PRK11783  511 LVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGTASVHAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQ 590

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 273 AEFVRDDVFKLLRKYRdggEKFDVIVMDPPKFVENKS------------QLMGacrgykdinmLAIQLLNPGGVLLtFSC 340
Cdd:PRK11783  591 HRLIQADCLAWLKEAR---EQFDLIFIDPPTFSNSKRmedsfdvqrdhvALIK----------DAKRLLRPGGTLY-FSN 656
PUA_RlmI cd21153
PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related proteins; The ...
 3-72 7.07e-32

PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related 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 N-terminal to SAM-dependent methyltransferase domains and include Escherichia coli RlmI (rRNA large subunit methyltransferase gene I, also called YccW) and Thermus thermophilus methyltransferase RlmO, which are 5-methylcytosine methyltransferases (m5C MTases) that play a role in modifying 23S rRNA. This subfamily also includes Pyrococcus horikoshii PH1915 that may play a role as a 5-methyluridine MTase, and/or perform similar roles.


Pssm-ID: 409295 [Multi-domain]  Cd Length: 70  Bit Score: 115.37  E-value: 7.07e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051   3 VRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDKDE 72
Cdd:cd21153     1 PRIVLKKGKEKSLRRGHPWIFSGAIDRIEGKPEPGDLVDVYDHKGKFLGTGLYNPHSQIRVRVLSFDKEE 70
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
 185-377 7.95e-28

S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.


Pssm-ID: 287624 [Multi-domain]  Cd Length: 286  Bit Score: 111.12  E-value: 7.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 185 IEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRQYVADKRVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVE 264
Cdd:pfam10672  88 VVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARGSLNKGRDNHR 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 265 LNKLDLSKAEFVRDDVFKLLRKYRDGGEkFDVIVMDPPKFVENKSQLMgacRGYKDINMLAIQLLNPGGVLLTFSCSGLM 344
Cdd:pfam10672 168 LNGHDLGRVSFLGHDIFKSWGKIKKLGP-YDLVIIDPPSFQKGSFALT---KDYKKILRRLPELLVEGGTVLACVNSPAV 243

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1168757051 345 TTDLFQKIIADAAidagRDVQFIEQFRQAADHP 377
Cdd:pfam10672 244 GPDFLIEEMAEEA----PSLHFVERLDNPPEFP 272
PUA_3 pfam17785
PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent ...
 5-68 3.08e-22

PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent methyltransferases.


Pssm-ID: 436043 [Multi-domain]  Cd Length: 64  Bit Score: 89.07  E-value: 3.08e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168757051   5 LVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTF 68
Cdd:pfam17785   1 VTLKKKAEKRLKRGHPWIYSNEIERVEGDLEEGDLVRVVDSDGRFLGTGYYNPQSKIAVRVLSR 64
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 217-302 2.58e-13

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 67.80  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 217 QYVADKRVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVElnKLDLS-KAEFVRDDVFKLLRKYRdgGEKFD 295
Cdd:COG0742    38 PDIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAAAVIRKNLE--KLGLEdRARVIRGDALRFLKRLA--GEPFD 113


                  ....*..
gi 1168757051 296 VIVMDPP 302
Cdd:COG0742   114 LVFLDPP 120
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 220-302 4.01e-11

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 64.04  E-value: 4.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 220 ADKRVLNCFSYTGGFAVsALMGGCAQVVSVDTSQEALDVAKQNVELNklDLSKAEFVRDDVFKLLRKyRDGGEKFDVIVM 299
Cdd:COG2265   233 GGERVLDLYCGVGTFAL-PLARRAKKVIGVEIVPEAVEDARENARLN--GLKNVEFVAGDLEEVLPE-LLWGGRPDVVVL 308


                  ...
gi 1168757051 300 DPP 302
Cdd:COG2265   309 DPP 311
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
216-302 6.45e-11

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 60.72  E-value: 6.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 216 RQYVADKRVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELnkLDLSKAEFVRDDVFKLLRKYRdGGEKFD 295
Cdd:pfam03602  37 APYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQL--LGLPGAVLVMDALLALLRLAG-KGPVFD 113


                  ....*..
gi 1168757051 296 VIVMDPP 302
Cdd:pfam03602 114 IVFLDPP 120
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
4-67 1.24e-10

Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 57.27  E-value: 1.24e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168757051    4 RLVLAKGREKSLLRRHpWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWT 67
Cdd:smart00359   2 KVVVDDGAEKAILNGA-SLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKG 64
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 187-368 1.71e-10

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: 61.80  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 187 EHGMKLLVDIQgghKTgYYldqrDSRLAT-RQYVADK-----RVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAK 260
Cdd:COG2520   149 ENGCRFKLDVA---KV-YF----SPRLATeRLRIAELvkpgeRVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLK 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 261 QNVELNKLDlSKAEFVRDDVFKLLRKYRdggEKFDVIVMDPPKFVENksqlmgacrgYKDInmlAIQLLNPGGVL----L 336
Cdd:COG2520   221 ENIRLNKVE-DRVTPILGDAREVAPELE---GKADRIIMNLPHSADE----------FLDA---ALRALKPGGVIhyyeI 283

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1168757051 337 TFSCSGLmttDLFQKIIADAAIDAGRDVQFIE 368
Cdd:COG2520   284 VPEEDPF---ERAEERIEEAAEEAGYEVEILE 312
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 223-337 2.72e-10

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: 57.05  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 223 RVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDlsKAEFVRDDVFKLLrkyRDGGEKFDVIVMDPP 302
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLAD--NVEVLKGDAEELP---PEADESFDVIISDPP 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1168757051 303 kfvenksqLMGACRGYKDINMLAIQLLNPGGVLLT 337
Cdd:cd02440    76 --------LHHLVEDLARFLEEARRLLKPGGVLVL 102
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 4-68 3.45e-10

PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, and a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was also found in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in regulating the expression of other genes. It has been shown that the PUA domain acts as an RNA binding domain in at least some of the proteins involved in RNA metabolism.


Pssm-ID: 409289 [Multi-domain]  Cd Length: 73  Bit Score: 55.77  E-value: 3.45e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168757051   4 RLVLAKGREKSLLRRhPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQ--------IRARVWTF 68
Cdd:cd07953     2 VVVVDKGAEKAVLNG-ADLMAPGVVSADGDFKRGDLVRIVSEGGRPLAIGVAEMSSDemkeelkgIAVRVLHF 73
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
222-304 4.95e-09

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 56.84  E-value: 4.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 222 KRVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDLSKAEFVRDDVFKLLRKYRDggEKFDVIVMDP 301
Cdd:COG2521   134 DRVLDTCTGLGYTAIEALKRGAREVITVEKDPNVLELAELNPWSRELANERIKIILGDASEVIKTFPD--ESFDAIIHDP 211


                  ...
gi 1168757051 302 PKF 304
Cdd:COG2521   212 PRF 214
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
219-302 1.12e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 54.52  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 219 VADKRVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDlskAEFVRDDVFKLlrkyrDGGEKFDVIV 298
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLGVR---VDFIRADVTRI-----PLGGSVDTVV 115


                  ....
gi 1168757051 299 MDPP 302
Cdd:COG2263   116 MNPP 119
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 220-343 1.40e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 53.57  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 220 ADKRVLNCFSYTG--GFAVSALMGGCAQVVSVDTSQEALDVAKQNVElnKLDLSKAEFVRDDVFKLLRKYRDggEKFDVI 297
Cdd:pfam13847   3 KGMRVLDLGCGTGhlSFELAEELGPNAEVVGIDISEEAIEKARENAQ--KLGFDNVEFEQGDIEELPELLED--DKFDVV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1168757051 298 VMDppkfveNKSQLMGACRgykDINMLAIQLLNPGGVLLTFSCSGL 343
Cdd:pfam13847  79 ISN------CVLNHIPDPD---KVLQEILRVLKPGGRLIISDPDSL 115
PRK14968 PRK14968
putative methyltransferase; Provisional
 219-302 4.14e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 52.98  E-value: 4.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 219 VADKRVLNCFSYTGGFAVSALMGGCaQVVSVDTSQEALDVAKQNVELNKLDLSKAEFVRDDVFKLLRkyrdgGEKFDVIV 298
Cdd:PRK14968   22 KKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLFEPFR-----GDKFDVIL 95


                  ....
gi 1168757051 299 MDPP 302
Cdd:PRK14968   96 FNPP 99
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 244-336 6.19e-08

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 53.62  E-value: 6.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 244 AQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLLrkyrDGGEKFDVIVMDPPkFV--ENKSQLMGACR----- 316
Cdd:COG2890   137 ARVTAVDISPDALAVARRNAERLGLE-DRVRFLQGDLFEPL----PGDGRFDLIVSNPP-YIpeDEIALLPPEVRdhepr 210

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1168757051 317 --------GYKDINML---AIQLLNPGGVLL 336
Cdd:COG2890   211 laldggedGLDFYRRIiaqAPRLLKPGGWLL 241
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 206-302 1.59e-07

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: 50.72  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 206 LDQRDSRLATRQYVA--DKRVLNCFSYTGGFAVSALMGGCaQVVSVDTSQEALDVAKQNVELnkLDLSKAEFVRDDVFKL 283
Cdd:COG1041    10 LDPRLARALVNLAGAkeGDTVLDPFCGTGTILIEAGLLGR-RVIGSDIDPKMVEGARENLEH--YGYEDADVIRGDARDL 86

                          90
                  ....*....|....*....
gi 1168757051 284 lrKYRDggEKFDVIVMDPP 302
Cdd:COG1041    87 --PLAD--ESVDAIVTDPP 101
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 238-336 1.59e-07

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 50.96  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 238 ALMGGCAQVVSVDTSQEALDVAKQNVELNKLDlsKAEFVRDDVFKLLrkyrdGGEKFDVIVMDPPkFVENKSQLMGACRG 317
Cdd:COG2813    68 AKRNPEARVTLVDVNARAVELARANAAANGLE--NVEVLWSDGLSGV-----PDGSFDLILSNPP-FHAGRAVDKEVAHA 139

                          90       100
                  ....*....|....*....|.
gi 1168757051 318 ykdinML--AIQLLNPGGVLL 336
Cdd:COG2813   140 -----LIadAARHLRPGGELW 155
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 222-336 4.96e-07

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 50.81  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 222 KRVLNCFSYTGGFAVS-ALMGGCAQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLLRkyrdgGEKFDVIVMD 300
Cdd:TIGR00536 116 LHILDLGTGSGCIALAlAYEFPNAEVIAVDISPDALAVAEENAEKNQLE-HRVEFIQSNLFEPLA-----GQKIDIIVSN 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1168757051 301 PP-------------KFVENKSQLMGACRGYKD---INMLAIQLLNPGGVLL 336
Cdd:TIGR00536 190 PPyideedladlpnvVRFEPLLALVGGDDGLNIlrqIIELAPDYLKPNGFLV 241
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 244-336 1.55e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 49.39  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 244 AQVVSVDTSQEALDVAKQNVELNKLDlsKAEFVRDDVFKLLRkyrdgGEKFDVIVMDPP--------------KFVENKS 309
Cdd:PRK09328  133 AEVTAVDISPEALAVARRNAKHGLGA--RVEFLQGDWFEPLP-----GGRFDLIVSNPPyipeadihllqpevRDHEPHL 205

                          90       100       110
                  ....*....|....*....|....*....|
gi 1168757051 310 QLMGACRG---YKDINMLAIQLLNPGGVLL 336
Cdd:PRK09328  206 ALFGGEDGldfYRRIIEQAPRYLKPGGWLL 235
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 233-370 2.51e-06

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 47.54  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 233 GFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDLSkaeFVRDDVFKLLRKyrdggeKFDVIVMDPPkFVENKSQLM 312
Cdd:TIGR00537  31 GLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLD---VVMTDLFKGVRG------KFDVILFNPP-YLPLEDDLR 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168757051 313 ----------GACRGYKDINMLAIQL---LNPGGVLLTFSCSGLMTTDLFQKIIA---DAAIDAGRDVQFIEQF 370
Cdd:TIGR00537 101 rgdwldvaidGGKDGRKVIDRFLDELpeiLKEGGRVQLIQSSLNGEPDTFDKLDErgfRYEIVAERGLFFEELF 174
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 207-336 2.59e-06

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: 46.16  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 207 DQRDSRLATRQYVADKRVLNCFSYTGGFAVsALMGGCAQVVSVDTSQEALDVAKQnvelnKLDLSKAEFVRDDVFKLlrk 286
Cdd:COG2227    11 DRRLAALLARLLPAGGRVLDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARE-----RAAELNVDFVQGDLEDL--- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1168757051 287 yRDGGEKFDVIVM--------DPPKFVENksqlmgacrgykdinmlAIQLLNPGGVLL 336
Cdd:COG2227    82 -PLEDGSFDLVICsevlehlpDPAALLRE-----------------LARLLKPGGLLL 121
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 235-336 6.28e-06

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 46.04  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 235 AVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDLskAEFVRDDVFKLLrkyrdGGEKFDVIVMDPPKFVENKSQLMGA 314
Cdd:pfam05175  47 AALAKESPDAELTMVDINARALESARENLAANGLEN--GEVVASDVYSGV-----EDGKFDLIISNPPFHAGLATTYNVA 119

                          90       100
                  ....*....|....*....|..
gi 1168757051 315 CRGYKDinmlAIQLLNPGGVLL 336
Cdd:pfam05175 120 QRFIAD----AKRHLRPGGELW 137
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 236-341 1.27e-05

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: 45.49  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 236 VSALMGGCAQVVSVDTSQEALDVAKQNveLNKLDLSKAEFVRDDVfkllRKYRD--GGEKFDVIVMDPP---KFVENKSQ 310
Cdd:pfam01189  26 IAELMKNQGTVVAVDINKHRLKRVAEN--IHRLGVTNTIILNGDG----RQPDQwlGGVLFDRILLDAPcsgTGVIRRHP 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1168757051 311 LMGACRGYKDINMLA----------IQLLNPGGVLLTFSCS 341
Cdd:pfam01189 100 DVKWLRQEADIAQLAqlqkellsaaIDLLKPGGVLVYSTCS 140
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
235-361 1.52e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 45.91  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 235 AVSALMGGCAQVVSVDTSQEALDVAKQNVELNKldlskaefVRDDVFKLlrkyrDGGEKFDVIV----MDPpkfvenksq 310
Cdd:PRK00517  134 AIAAAKLGAKKVLAVDIDPQAVEAARENAELNG--------VELNVYLP-----QGDLKADVIVanilANP--------- 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1168757051 311 LMgacrgyKDINMLAiQLLNPGGVLLTfscSGLMTTDLfqKIIADAAIDAG 361
Cdd:PRK00517  192 LL------ELAPDLA-RLLKPGGRLIL---SGILEEQA--DEVLEAYEEAG 230
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 233-336 2.49e-05

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 44.40  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 233 GFAVSAL-----MGGCAQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLLRKYRDGgeKFDVIVMDPPKfven 307
Cdd:COG4122    26 GTGYSTLwlaraLPDDGRLTTIEIDPERAAIARENFARAGLA-DRIRLILGDALEVLPRLADG--PFDLVFIDADK---- 98

                          90       100
                  ....*....|....*....|....*....
gi 1168757051 308 ksqlmgacRGYKDINMLAIQLLNPGGVLL 336
Cdd:COG4122    99 --------SNYPDYLELALPLLRPGGLIV 119
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
235-361 2.82e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 45.55  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 235 AVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKllrkyrdgGEKFDVIV----MDPpkfvenksq 310
Cdd:COG2264   163 AIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVE-DRIEVVLGDLLE--------DGPYDLVVanilANP--------- 224

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1168757051 311 LMgacrgyKDINMLAiQLLNPGGVLLtfsCSGLMTTDLfqKIIADAAIDAG 361
Cdd:COG2264   225 LI------ELAPDLA-ALLKPGGYLI---LSGILEEQA--DEVLAAYEAAG 263
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 231-299 3.47e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.17  E-value: 3.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168757051 231 TGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLdlsKAEFVRDDVFKLlrkyRDGGEKFDVIVM 299
Cdd:pfam13649   8 TGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL---NVEFVQGDAEDL----PFPDGSFDLVVS 69
PRK14967 PRK14967
putative methyltransferase; Provisional
 203-302 4.12e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 44.27  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 203 GYYLDQRDSRL-----ATRQYVADKRVLNCFSYTGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDLskaEFVR 277
Cdd:PRK14967   14 GVYRPQEDTQLladalAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDV---DVRR 90

                          90       100
                  ....*....|....*....|....*
gi 1168757051 278 DDVFKLLRkyrdgGEKFDVIVMDPP 302
Cdd:PRK14967   91 GDWARAVE-----FRPFDVVVSNPP 110
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 244-335 1.61e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 42.82  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 244 AQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLLRKYRDggEKFDVIVMDPPKFVENKSQL-----------M 312
Cdd:COG4123    62 ARITGVEIQPEAAELARRNVALNGLE-DRITVIHGDLKEFAAELPP--GSFDLVVSNPPYFKAGSGRKspdearaiarhE 138

                          90       100
                  ....*....|....*....|...
gi 1168757051 313 GACrGYKDINMLAIQLLNPGGVL 335
Cdd:COG4123   139 DAL-TLEDLIRAAARLLKPGGRF 160
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 231-336 3.58e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 40.68  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 231 TGGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLlrkyrDGGEKFDVIV-------MDPpk 303
Cdd:COG2230    62 WGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLA-DRVEVRLADYRDL-----PADGQFDAIVsigmfehVGP-- 133

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1168757051 304 fvENKSQLMGACRgykdinmlaiQLLNPGGVLL 336
Cdd:COG2230   134 --ENYPAYFAKVA----------RLLKPGGRLL 154
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
 222-302 1.16e-03

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 39.24  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 222 KRVLNCFSYTGGFAVSALMGGCaQVVSVDTSQEALDVAKQNVELNKLDlSKAEFVRDDVFKLLRKYRDGGEKFDVIVMDP 301
Cdd:pfam09445   2 TRILDVFCGGGGNTIQFANVFD-SVISIDINLEHLACAQHNAEVYGVS-DRIWLIHGDWFELLAKLKFEKIKYDCVFASP 79


                  .
gi 1168757051 302 P 302
Cdd:pfam09445  80 P 80
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 232-336 1.43e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.64  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 232 GGFAVSALMGGCAQVVSVDTSQEALDVAKQNVELNKLdlskaEFVRDDVFKLlrKYRDggEKFDVIVM--------DPPK 303
Cdd:pfam08241   7 TGLLTELLARLGARVTGVDISPEMLELAREKAPREGL-----TFVVGDAEDL--PFPD--NSFDLVLSsevlhhveDPER 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1168757051 304 FVENksqlmgacrgykdinmlAIQLLNPGGVLL 336
Cdd:pfam08241  78 ALRE-----------------IARVLKPGGILI 93
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
244-336 1.65e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 37.50  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 244 AQVVSVDTSQEALDVAKQNvelnkldLSKAEFVRDDVFKLlrkyrDGGEKFDVIVM--------DPPKFVENksqlmgac 315
Cdd:COG4106    26 ARVTGVDLSPEMLARARAR-------LPNVRFVVADLRDL-----DPPEPFDLVVSnaalhwlpDHAALLAR-------- 85

                          90       100
                  ....*....|....*....|.
gi 1168757051 316 rgykdinmlAIQLLNPGGVLL 336
Cdd:COG4106    86 ---------LAAALAPGGVLA 97
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 209-301 4.02e-03

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 39.13  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 209 RD-SRLATRQYVADK---RVLNCFSYTGGFAVS-ALMGGCAQVVSVDTSQEALDVAKQNVELNklDLSKAEFVRDDVFKL 283
Cdd:PRK04338   42 RDiSVLVLRAFGPKLpreSVLDALSASGIRGIRyALETGVEKVTLNDINPDAVELIKKNLELN--GLENEKVFNKDANAL 119

                          90
                  ....*....|....*...
gi 1168757051 284 LRKYRdggeKFDVIVMDP 301
Cdd:PRK04338  120 LHEER----KFDVVDIDP 133
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 245-387 6.21e-03

Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.


Pssm-ID: 396237 [Multi-domain]  Cd Length: 183  Bit Score: 37.30  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 245 QVVSVDTSQEALDVAKQN-VELN-KLDLSKAEFVRDDVFKLLRKYRDggeKFDVIVMD---PPKFVENKSQlmgacrgyK 319
Cdd:pfam01564  44 KITLVDIDEKVIDFSKKFlPSLAiGFQDPRVKVVIGDGFKFLKDYLN---TFDVIIVDstdPVGPAENLFS--------K 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168757051 320 DINMLAIQLLNPGGVLLTFSCSGLMTTDLFQKIIADaaidaGRDVQFIEQFRQAAdhpvIATYPEGLY 387
Cdd:pfam01564 113 PFFDLLKKALKEDGVFITQAESPWLHLELIINILKN-----GKQVFPVVMPYVAT----IPTYPSGGW 171
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 245-349 7.06e-03

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 38.31  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168757051 245 QVVSVDTSQEALDVAKQN---VELNK--LDLSKAEFVRDDVFKLLRkyrDGGEKFDVIVMDPP---KFVENK---SQLMG 313
Cdd:COG4262   312 SVTLVDLDPEVTDLAKTNpflRELNGgaLNDPRVTVVNADAFQFLR---ETDEKYDVIIVDLPdpsNFSLGKlysVEFYR 388

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1168757051 314 ACRgykdinmlaiQLLNPGGVLLTFSCSGLMTTDLF 349
Cdd:COG4262   389 LVR----------RHLAPGGVLVVQATSPYFAPKAF 414
 
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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