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Conserved domains on  [gi|446062625|ref|WP_000140480|]
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MULTISPECIES: 23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI [Salmonella]

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;
8-403 0e+00

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


:

Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 864.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625   8 QYPRLVLSKGREKSLLRRHPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWTFDKAESIDIAFFT 87
Cdd:PRK15128   1 MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDESIDIAFFT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  88 RRLRQAQQWRDWLAKKDGLDSYRLIAGESDGLPGVTIDRFGHFLVLQLLSAGAEYQRAALISALQTCYPDCAIYDRSDVA 167
Cdd:PRK15128  81 RRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 168 VRKKEGMALTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENQRVLNCFSYTGGFAVSALM 247
Cdd:PRK15128 161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 248 GGCRQVVSVDTSQDALDIARQNVELNQLDLSKAEFVRDDVFKLLRAYREHGEKFDVIIMDPPKFVENKSQLMGACRGYKD 327
Cdd:PRK15128 241 GGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446062625 328 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 403
Cdd:PRK15128 321 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
 
Name Accession Description Interval E-value
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
8-403 0e+00

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


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 864.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625   8 QYPRLVLSKGREKSLLRRHPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWTFDKAESIDIAFFT 87
Cdd:PRK15128   1 MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDESIDIAFFT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  88 RRLRQAQQWRDWLAKKDGLDSYRLIAGESDGLPGVTIDRFGHFLVLQLLSAGAEYQRAALISALQTCYPDCAIYDRSDVA 167
Cdd:PRK15128  81 RRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 168 VRKKEGMALTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENQRVLNCFSYTGGFAVSALM 247
Cdd:PRK15128 161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 248 GGCRQVVSVDTSQDALDIARQNVELNQLDLSKAEFVRDDVFKLLRAYREHGEKFDVIIMDPPKFVENKSQLMGACRGYKD 327
Cdd:PRK15128 241 GGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446062625 328 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 403
Cdd:PRK15128 321 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 11-402 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: 557.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  11 RLVLSKGREKSLLRRHPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWTFDKAESIDIAFFTRRL 90
Cdd:COG1092    1 KVRLKPGKERRLRRGHPWVFSNEIDRVEGELEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEPIDAAFFANRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  91 RQAQQWRDWLAKKDGLDSYRLIAGESDGLPGVTIDRFGHFLVLQLLSAGAEYQRAALISALQTCYPDCAIYDRSDVAVRK 170
Cdd:COG1092   81 RKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEALVEVLGPEGIYLRSDVRVRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 171 KEGMALTQGPVTGELPPAlLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENQRVLNCFSYTGGFAVSALMGGC 250
Cdd:COG1092  161 LEGLPQYEGVLYGEAPEE-VEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSVHAAAGGA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 251 RQVVSVDTSQDALDIARQNVELNQLDlSKAEFVRDDVFKLLRAYREHGEKFDVIIMDPPKFVENKSQLMGACRGYKDINM 330
Cdd:COG1092  240 KSVTSVDLSATALEWAKENAALNGLD-DRHEFVQADAFDWLRELAREGERFDLIILDPPAFAKSKKDLFDAQRDYKDLNR 318

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446062625 331 LAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRV 402
Cdd:COG1092  319 LALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLRV 390
RlmI_M_like cd11572
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ...
 84-183 1.93e-35

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: 125.65  E-value: 1.93e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  84 AFFTRRLRQAQQWRDWLAKKDgLDSYRLIAGESDGLPGVTIDRFGHFLVLQLLSAGAEYQRAALISALQTCYPDCAIYDR 163
Cdd:cd11572    1 AFFKRRIEKALALRKRLLLDD-TNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKELLGPKGIYER 79

                         90       100
                 ....*....|....*....|
gi 446062625 164 SDVAVRKKEGMALTQGPVTG 183
Cdd:cd11572   80 SDAAVRELEGLPEEVGVLYG 99
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
 192-384 1.12e-26

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: 108.04  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  192 IEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENQRVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVE 271
Cdd:pfam10672  88 VVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARGSLNKGRDNHR 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  272 LNQLDLSKAEFVRDDVFKLLRAYREHGEkFDVIIMDPPKFVENKSQLMgacRGYKDINMLAIQLLNPGGILLTFSCSGLM 351
Cdd:pfam10672 168 LNGHDLGRVSFLGHDIFKSWGKIKKLGP-YDLVIIDPPSFQKGSFALT---KDYKKILRRLPELLVEGGTVLACVNSPAV 243

                         170       180       190
                  ....*....|....*....|....*....|...
gi 446062625  352 TSDLFQKIIADAAidagRDVQFIEQFRQAADHP 384
Cdd:pfam10672 244 GPDFLIEEMAEEA----PSLHFVERLDNPPEFP 272
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
10-74 1.03e-08

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 51.87  E-value: 1.03e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446062625    10 PRLVLSKGREKSLLRRHpWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWT 74
Cdd:smart00359   1 GKVVVDDGAEKAILNGA-SLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKG 64
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 220-377 1.37e-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: 48.31  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  220 LATRRYVENQRVLNCFSYTGgFAVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDLSkaeFVRDDVFKLLRAyrehge 299
Cdd:TIGR00537  12 EANLRELKPDDVLEIGAGTG-LVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLD---VVMTDLFKGVRG------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  300 KFDVIIMDPPkFVENKSQLM----------GACRGYKDINMLAIQL---LNPGGILLTFSCSGLMTSDLFQKIIA---DA 363
Cdd:TIGR00537  82 KFDVILFNPP-YLPLEDDLRrgdwldvaidGGKDGRKVIDRFLDELpeiLKEGGRVQLIQSSLNGEPDTFDKLDErgfRY 160

                         170
                  ....*....|....
gi 446062625  364 AIDAGRDVQFIEQF 377
Cdd:TIGR00537 161 EIVAERGLFFEELF 174
 
Name Accession Description Interval E-value
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
8-403 0e+00

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


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 864.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625   8 QYPRLVLSKGREKSLLRRHPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWTFDKAESIDIAFFT 87
Cdd:PRK15128   1 MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDESIDIAFFT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  88 RRLRQAQQWRDWLAKKDGLDSYRLIAGESDGLPGVTIDRFGHFLVLQLLSAGAEYQRAALISALQTCYPDCAIYDRSDVA 167
Cdd:PRK15128  81 RRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 168 VRKKEGMALTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENQRVLNCFSYTGGFAVSALM 247
Cdd:PRK15128 161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 248 GGCRQVVSVDTSQDALDIARQNVELNQLDLSKAEFVRDDVFKLLRAYREHGEKFDVIIMDPPKFVENKSQLMGACRGYKD 327
Cdd:PRK15128 241 GGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKD 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446062625 328 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 403
Cdd:PRK15128 321 INMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 11-402 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: 557.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  11 RLVLSKGREKSLLRRHPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWTFDKAESIDIAFFTRRL 90
Cdd:COG1092    1 KVRLKPGKERRLRRGHPWVFSNEIDRVEGELEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEPIDAAFFANRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  91 RQAQQWRDWLAKKDGLDSYRLIAGESDGLPGVTIDRFGHFLVLQLLSAGAEYQRAALISALQTCYPDCAIYDRSDVAVRK 170
Cdd:COG1092   81 RKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEALVEVLGPEGIYLRSDVRVRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 171 KEGMALTQGPVTGELPPAlLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENQRVLNCFSYTGGFAVSALMGGC 250
Cdd:COG1092  161 LEGLPQYEGVLYGEAPEE-VEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSVHAAAGGA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 251 RQVVSVDTSQDALDIARQNVELNQLDlSKAEFVRDDVFKLLRAYREHGEKFDVIIMDPPKFVENKSQLMGACRGYKDINM 330
Cdd:COG1092  240 KSVTSVDLSATALEWAKENAALNGLD-DRHEFVQADAFDWLRELAREGERFDLIILDPPAFAKSKKDLFDAQRDYKDLNR 318

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446062625 331 LAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRV 402
Cdd:COG1092  319 LALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLRV 390
RlmI_M_like cd11572
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ...
 84-183 1.93e-35

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: 125.65  E-value: 1.93e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  84 AFFTRRLRQAQQWRDWLAKKDgLDSYRLIAGESDGLPGVTIDRFGHFLVLQLLSAGAEYQRAALISALQTCYPDCAIYDR 163
Cdd:cd11572    1 AFFKRRIEKALALRKRLLLDD-TNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKELLGPKGIYER 79

                         90       100
                 ....*....|....*....|
gi 446062625 164 SDVAVRKKEGMALTQGPVTG 183
Cdd:cd11572   80 SDAAVRELEGLPEEVGVLYG 99
PUA_RlmI cd21153
PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related proteins; The ...
 10-79 8.93e-31

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: 112.29  E-value: 8.93e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  10 PRLVLSKGREKSLLRRHPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWTFDKAE 79
Cdd:cd21153    1 PRIVLKKGKEKSLRRGHPWIFSGAIDRIEGKPEPGDLVDVYDHKGKFLGTGLYNPHSQIRVRVLSFDKEE 70
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 86-347 6.86e-29

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: 118.75  E-value: 6.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  86 FTRRLRQ-AQQWRDWlAKKDGLDSYRLIagESDgLP--GVTIDRFGHFLVLQllsagaEY------------QR-----A 145
Cdd:PRK11783 395 FANRLRKnLKKLKKW-AKQEGIECYRLY--DAD-LPeyNVAVDRYGDWVVVQ------EYaapktideekarQRlfdalA 464

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 146 ALISALQTcypdcaiyDRSDVA--VRKK-EGMA----LTQgpvTGELppalLPIEEHGMKLLVDIQGGHKTGYYLDQRDS 218
Cdd:PRK11783 465 ATPEVLGI--------PPNKVVlkTRERqKGKNqyqkLAE---KGEF----LEVTEYGAKLLVNLTDYLDTGLFLDHRPT 529

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 219 RLATRRYVENQRVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDLSKAEFVRDDVFKLLrayREHG 298
Cdd:PRK11783 530 RRMIGQMAKGKDFLNLFAYTGTASVHAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWL---KEAR 606

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446062625 299 EKFDVIIMDPPKFVENKS------------QLMGacrgykdinmLAIQLLNPGGILLtFSC 347
Cdd:PRK11783 607 EQFDLIFIDPPTFSNSKRmedsfdvqrdhvALIK----------DAKRLLRPGGTLY-FSN 656
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
 192-384 1.12e-26

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: 108.04  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  192 IEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENQRVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVE 271
Cdd:pfam10672  88 VVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARGSLNKGRDNHR 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  272 LNQLDLSKAEFVRDDVFKLLRAYREHGEkFDVIIMDPPKFVENKSQLMgacRGYKDINMLAIQLLNPGGILLTFSCSGLM 351
Cdd:pfam10672 168 LNGHDLGRVSFLGHDIFKSWGKIKKLGP-YDLVIIDPPSFQKGSFALT---KDYKKILRRLPELLVEGGTVLACVNSPAV 243

                         170       180       190
                  ....*....|....*....|....*....|...
gi 446062625  352 TSDLFQKIIADAAidagRDVQFIEQFRQAADHP 384
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 ...
 12-75 1.26e-20

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: 84.84  E-value: 1.26e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446062625   12 LVLSKGREKSLLRRHPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWTF 75
Cdd:pfam17785   1 VTLKKKAEKRLKRGHPWIYSNEIERVEGDLEEGDLVRVVDSDGRFLGTGYYNPQSKIAVRVLSR 64
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 225-342 2.53e-12

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: 65.10  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 225 YVENQRVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVELnqLDLS-KAEFVRDDVFKLLRAYRehGEKFDV 303
Cdd:COG0742   39 DIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAAAVIRKNLEK--LGLEdRARVIRGDALRFLKRLA--GEPFDL 114

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446062625 304 IIMDPPkFveNKSQLMGACRgykdiNMLAIQLLNPGGIL 342
Cdd:COG0742  115 VFLDPP-Y--AKGLLEKALE-----LLAENGLLAPGGLI 145
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 227-309 7.64e-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: 63.27  E-value: 7.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 227 ENQRVLNCFSYTGGFAVsALMGGCRQVVSVDTSQDALDIARQNVELNQLDlsKAEFVRDDVFKLLRAyREHGEKFDVIIM 306
Cdd:COG2265  233 GGERVLDLYCGVGTFAL-PLARRAKKVIGVEIVPEAVEDARENARLNGLK--NVEFVAGDLEEVLPE-LLWGGRPDVVVL 308


                 ...
gi 446062625 307 DPP 309
Cdd:COG2265  309 DPP 311
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 230-344 2.81e-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: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 230 RVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDlsKAEFVRDDVFKLLrayREHGEKFDVIIMDPP 309
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLAD--NVEVLKGDAEELP---PEADESFDVIISDPP 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446062625 310 kfvenksqLMGACRGYKDINMLAIQLLNPGGILLT 344
Cdd:cd02440   76 --------LHHLVEDLARFLEEARRLLKPGGVLVL 102
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
230-311 6.14e-10

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 59.54  E-value: 6.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 230 RVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDLSKAEFVRDDVFKLLRAYREhgEKFDVIIMDPP 309
Cdd:COG2521  135 RVLDTCTGLGYTAIEALKRGAREVITVEKDPNVLELAELNPWSRELANERIKIILGDASEVIKTFPD--ESFDAIIHDPP 212


                 ..
gi 446062625 310 KF 311
Cdd:COG2521  213 RF 214
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 10-75 6.64e-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: 54.99  E-value: 6.64e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446062625  10 PRLVLSKGREKSLLRRhPWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQ--------IRARVWTF 75
Cdd:cd07953    1 PVVVVDKGAEKAVLNG-ADLMAPGVVSADGDFKRGDLVRIVSEGGRPLAIGVAEMSSDemkeelkgIAVRVLHF 73
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 213-309 8.56e-10

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: 57.27  E-value: 8.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 213 LDQRDSRLATRRYV--ENQRVLNCFSYTGGFAVSALMGGCRqVVSVDTSQDALDIARQNveLNQLDLSKAEFVRDDVFKL 290
Cdd:COG1041   10 LDPRLARALVNLAGakEGDTVLDPFCGTGTILIEAGLLGRR-VIGSDIDPKMVEGAREN--LEHYGYEDADVIRGDARDL 86

                         90
                 ....*....|....*....
gi 446062625 291 lrayREHGEKFDVIIMDPP 309
Cdd:COG1041   87 ----PLADESVDAIVTDPP 101
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
225-309 1.01e-09

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 57.25  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  225 YVENQRVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVELnqLDLSKAEFVRDDVFKLLRAYREhGEKFDVI 304
Cdd:pfam03602  39 YIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQL--LGLPGAVLVMDALLALLRLAGK-GPVFDIV 115


                  ....*
gi 446062625  305 IMDPP 309
Cdd:pfam03602 116 FLDPP 120
PRK14968 PRK14968
putative methyltransferase; Provisional
 226-309 2.31e-09

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 56.45  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 226 VENQRVLNCFSYTGGFAVSALMGGCRqVVSVDTSQDALDIARQNVELNQLDLSKAEFVRDDVFKLLRayrehGEKFDVII 305
Cdd:PRK14968  22 KKGDRVLEVGTGSGIVAIVAAKNGKK-VVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLFEPFR-----GDKFDVIL 95


                 ....
gi 446062625 306 MDPP 309
Cdd:PRK14968  96 FNPP 99
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 194-375 4.11e-09

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: 57.56  E-value: 4.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 194 EHGMKLLVDIQgghKTgYYldqrDSRLAT-RRYV-----ENQRVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIAR 267
Cdd:COG2520  149 ENGCRFKLDVA---KV-YF----SPRLATeRLRIaelvkPGERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLK 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 268 QNVELNQLDlSKAEFVRDDVFKLLRAYRehgEKFDVIIMDPPKFVENksqlmgacrgYKDInmlAIQLLNPGGIL----L 343
Cdd:COG2520  221 ENIRLNKVE-DRVTPILGDAREVAPELE---GKADRIIMNLPHSADE----------FLDA---ALRALKPGGVIhyyeI 283

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446062625 344 TFSCSGLmtsDLFQKIIADAAIDAGRDVQFIE 375
Cdd:COG2520  284 VPEEDPF---ERAEERIEEAAEEAGYEVEILE 312
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
10-74 1.03e-08

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


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 51.87  E-value: 1.03e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446062625    10 PRLVLSKGREKSLLRRHpWVFSGAVSRLEGKANLGETIDIVDHQGKWLARGAWSPASQIRARVWT 74
Cdd:smart00359   1 GKVVVDDGAEKAILNGA-SLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKG 64
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
238-309 1.49e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 54.52  E-value: 1.49e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446062625 238 TGGFAVSALMGGCRQVVSVDTSQDALDIARQNVElnQLDlSKAEFVRDDVFKLlrayrEHGEKFDVIIMDPP 309
Cdd:COG2263   56 TGMLAIGAALLGAKKVVGVDIDPEALEIARENAE--RLG-VRVDFIRADVTRI-----PLGGSVDTVVMNPP 119
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 245-343 4.91e-08

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: 52.50  E-value: 4.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 245 ALMGGCRQVVSVDTSQDALDIARQNVELNQLDlsKAEFVRDDVFKLLRayrehGEKFDVIIMDPPkFVENKSQLMGACRG 324
Cdd:COG2813   68 AKRNPEARVTLVDVNARAVELARANAAANGLE--NVEVLWSDGLSGVP-----DGSFDLILSNPP-FHAGRAVDKEVAHA 139

                         90       100
                 ....*....|....*....|.
gi 446062625 325 ykdinML--AIQLLNPGGILL 343
Cdd:COG2813  140 -----LIadAARHLRPGGELW 155
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 230-350 1.97e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.11  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  230 RVLNCFSYTG--GFAVSALMGGCRQVVSVDTSQDALDIARQNVElnQLDLSKAEFVRDDVFKLLRAYreHGEKFDVIIMD 307
Cdd:pfam13847   6 RVLDLGCGTGhlSFELAEELGPNAEVVGIDISEEAIEKARENAQ--KLGFDNVEFEQGDIEELPELL--EDDKFDVVISN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446062625  308 ppkfveNKSQLMGACRgykDINMLAIQLLNPGGILLTFSCSGL 350
Cdd:pfam13847  82 ------CVLNHIPDPD---KVLQEILRVLKPGGRLIISDPDSL 115
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 252-343 1.14e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 49.76  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 252 QVVSVDTSQDALDIARQNVELNQLDlSKAEFVRDDVFKLLrayrEHGEKFDVIIMDPPkFV--ENKSQLMGACR------ 323
Cdd:COG2890  138 RVTAVDISPDALAVARRNAERLGLE-DRVRFLQGDLFEPL----PGDGRFDLIVSNPP-YIpeDEIALLPPEVRdheprl 211

                         90       100       110
                 ....*....|....*....|....*....|
gi 446062625 324 -------GYKDINML---AIQLLNPGGILL 343
Cdd:COG2890  212 aldggedGLDFYRRIiaqAPRLLKPGGWLL 241
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 220-377 1.37e-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: 48.31  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  220 LATRRYVENQRVLNCFSYTGgFAVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDLSkaeFVRDDVFKLLRAyrehge 299
Cdd:TIGR00537  12 EANLRELKPDDVLEIGAGTG-LVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLD---VVMTDLFKGVRG------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  300 KFDVIIMDPPkFVENKSQLM----------GACRGYKDINMLAIQL---LNPGGILLTFSCSGLMTSDLFQKIIA---DA 363
Cdd:TIGR00537  82 KFDVILFNPP-YLPLEDDLRrgdwldvaidGGKDGRKVIDRFLDELpeiLKEGGRVQLIQSSLNGEPDTFDKLDErgfRY 160

                         170
                  ....*....|....
gi 446062625  364 AIDAGRDVQFIEQF 377
Cdd:TIGR00537 161 EIVAERGLFFEELF 174
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
242-368 8.73e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 47.09  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 242 AVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDlSKAEFVRDDVFKllrayrehGEKFDV----IIMDPpkfvenksq 317
Cdd:COG2264  163 AIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVE-DRIEVVLGDLLE--------DGPYDLvvanILANP--------- 224

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446062625 318 LMgacrgyKDINMLAiQLLNPGGILLtfsCSGLMTSDLfqKIIADAAIDAG 368
Cdd:COG2264  225 LI------ELAPDLA-ALLKPGGYLI---LSGILEEQA--DEVLAAYEAAG 263
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 229-343 1.02e-05

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: 46.96  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  229 QRVLNCFSYTGGFAVS-ALMGGCRQVVSVDTSQDALDIARQNVELNQLDlSKAEFVRDDVFKLLRayrehGEKFDVIIMD 307
Cdd:TIGR00536 116 LHILDLGTGSGCIALAlAYEFPNAEVIAVDISPDALAVAEENAEKNQLE-HRVEFIQSNLFEPLA-----GQKIDIIVSN 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446062625  308 PP-------------KFVENKSQLMGACRGYKD---INMLAIQLLNPGGILL 343
Cdd:TIGR00536 190 PPyideedladlpnvVRFEPLLALVGGDDGLNIlrqIIELAPDYLKPNGFLV 241
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 252-343 1.78e-05

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.92  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 252 QVVSVDTSQDALDIARQNVELNQLDlsKAEFVRDDVFKLLRayrehGEKFDVIIMDPP--------------KFVENKSQ 317
Cdd:PRK09328 134 EVTAVDISPEALAVARRNAKHGLGA--RVEFLQGDWFEPLP-----GGRFDLIVSNPPyipeadihllqpevRDHEPHLA 206

                         90       100
                 ....*....|....*....|....*....
gi 446062625 318 LMGACRG---YKDINMLAIQLLNPGGILL 343
Cdd:PRK09328 207 LFGGEDGldfYRRIIEQAPRYLKPGGWLL 235
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 238-306 2.26e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.94  E-value: 2.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446062625  238 TGGFAVSALMGGCRQVVSVDTSQDALDIARQNVELNQLdlsKAEFVRDDVfkllRAYREHGEKFDVIIM 306
Cdd:pfam13649   8 TGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL---NVEFVQGDA----EDLPFPDGSFDLVVS 69
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 214-343 3.49e-05

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: 43.08  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 214 DQRDSRLATRRYVENQRVLNCFSYTGGFAVSALMGGCRqVVSVDTSQDALDIARQNVELNQLDlskaeFVRDDVFKLlra 293
Cdd:COG2227   11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAELNVD-----FVQGDLEDL--- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446062625 294 yREHGEKFDVIIM--------DPPKFVENksqlmgacrgykdinmlAIQLLNPGGILL 343
Cdd:COG2227   82 -PLEDGSFDLVICsevlehlpDPAALLRE-----------------LARLLKPGGLLL 121
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
242-368 3.99e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 44.76  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 242 AVSALMGGCRQVVSVDTSQDALDIARQNVELNQldlskaefVRDDVFKLlrayrEHGEKFDV----IIMDPpkfvenksq 317
Cdd:PRK00517 134 AIAAAKLGAKKVLAVDIDPQAVEAARENAELNG--------VELNVYLP-----QGDLKADVivanILANP--------- 191

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446062625 318 LMgacrgyKDINMLAiQLLNPGGILLTfscSGLMTSDLfqKIIADAAIDAG 368
Cdd:PRK00517 192 LL------ELAPDLA-RLLKPGGRLIL---SGILEEQA--DEVLEAYEEAG 230
PRK14967 PRK14967
putative methyltransferase; Provisional
 210-309 4.03e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 44.66  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 210 GYYLDQRDSRL-----ATRRYVENQRVLNCFSYTGGFAVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDLskaEFVR 284
Cdd:PRK14967  14 GVYRPQEDTQLladalAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDV---DVRR 90

                         90       100
                 ....*....|....*....|....*
gi 446062625 285 DDvfkLLRAYRehGEKFDVIIMDPP 309
Cdd:PRK14967  91 GD---WARAVE--FRPFDVVVSNPP 110
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 242-343 6.16e-05

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: 43.35  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  242 AVSALMGGCRQVVSVDTSQDALDIARQNVELNQLDLskAEFVRDDVFkllrAYREHGeKFDVIIMDPPKFVENKSQLMGA 321
Cdd:pfam05175  47 AALAKESPDAELTMVDINARALESARENLAANGLEN--GEVVASDVY----SGVEDG-KFDLIISNPPFHAGLATTYNVA 119

                          90       100
                  ....*....|....*....|..
gi 446062625  322 CRGYKDinmlAIQLLNPGGILL 343
Cdd:pfam05175 120 QRFIAD----AKRHLRPGGELW 137
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 252-342 1.42e-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: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 252 QVVSVDTSQDALDIARQNVELNQLDlSKAEFVRDDVFKLLRAYREhgEKFDVIIMDPPKFVENKSQL-----------MG 320
Cdd:COG4123   63 RITGVEIQPEAAELARRNVALNGLE-DRITVIHGDLKEFAAELPP--GSFDLVVSNPPYFKAGSGRKspdearaiarhED 139

                         90       100
                 ....*....|....*....|..
gi 446062625 321 ACrGYKDINMLAIQLLNPGGIL 342
Cdd:COG4123  140 AL-TLEDLIRAAARLLKPGGRF 160
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 251-356 3.59e-04

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 42.54  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 251 RQVVSVDTSQDALDIARQN---VELNQ--LDLSKAEFVRDDVFKLLRayrEHGEKFDVIIMDPP---KFVENK---SQLM 319
Cdd:COG4262  311 ESVTLVDLDPEVTDLAKTNpflRELNGgaLNDPRVTVVNADAFQFLR---ETDEKYDVIIVDLPdpsNFSLGKlysVEFY 387

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446062625 320 GACRgykdinmlaiQLLNPGGILLTFSCSGLMTSDLF 356
Cdd:COG4262  388 RLVR----------RHLAPGGVLVVQATSPYFAPKAF 414
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 252-343 7.27e-04

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: 40.17  E-value: 7.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 252 QVVSVDTSQDALDIARQNVELNQLDlSKAEFVRDDVFKLLRAYREhgEKFDVIIMDPPKfvenksqlmgacRGYKDINML 331
Cdd:COG4122   43 RLTTIEIDPERAAIARENFARAGLA-DRIRLILGDALEVLPRLAD--GPFDLVFIDADK------------SNYPDYLEL 107

                         90
                 ....*....|..
gi 446062625 332 AIQLLNPGGILL 343
Cdd:COG4122  108 ALPLLRPGGLIV 119
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 238-343 9.84e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 39.90  E-value: 9.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 238 TGGFAVSALMGGCRQVVSVDTSQDALDIARQNVElnQLDLSKAEFVRDDVFKLLRAYrehGEKFDVIIMDppkFV---EN 314
Cdd:COG0500   37 TGRNLLALAARFGGRVIGIDLSPEAIALARARAA--KAGLGNVEFLVADLAELDPLP---AESFDLVVAF---GVlhhLP 108

                         90       100
                 ....*....|....*....|....*....
gi 446062625 315 KSQLMGACRgykdinmLAIQLLNPGGILL 343
Cdd:COG0500  109 PEEREALLR-------ELARALKPGGVLL 130
PRK03612 PRK03612
polyamine aminopropyltransferase;
251-348 2.02e-03

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 40.21  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 251 RQVVSVDTSQDALDIARQN---VELNQ--LDLSKAEFVRDDVFKLLRayrEHGEKFDVIIM---DPPKFVENK--SQLMg 320
Cdd:PRK03612 322 EQVTLVDLDPAMTELARTSpalRALNGgaLDDPRVTVVNDDAFNWLR---KLAEKFDVIIVdlpDPSNPALGKlySVEF- 397

                         90       100
                 ....*....|....*....|....*...
gi 446062625 321 acrgYkdinMLAIQLLNPGGILLTFSCS 348
Cdd:PRK03612 398 ----Y----RLLKRRLAPDGLLVVQSTS 417
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 238-343 4.61e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 37.60  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625 238 TGGFAVS-ALMGGCRqVVSVDTSQDALDIARQNVELNQLDlSKAEFVRDDVFKLlrayrEHGEKFDVII-------MDPp 309
Cdd:COG2230   62 WGGLALYlARRYGVR-VTGVTLSPEQLEYARERAAEAGLA-DRVEVRLADYRDL-----PADGQFDAIVsigmfehVGP- 133

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446062625 310 kfvENKSQLMGACRgykdinmlaiQLLNPGGILL 343
Cdd:COG2230  134 ---ENYPAYFAKVA----------RLLKPGGRLL 154
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 252-342 5.97e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.81  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446062625  252 QVVSVDTSQDALDIARQnvELNQLDLSKAEFVRddvFKLLRAYREHGEKFDVIIMdppKFV----ENKSQLMGACRgykd 327
Cdd:pfam08242  22 EYTGLDISPAALEAARE--RLAALGLLNAVRVE---LFQLDLGELDPGSFDVVVA---SNVlhhlADPRAVLRNIR---- 89

                          90
                  ....*....|....*
gi 446062625  328 inmlaiQLLNPGGIL 342
Cdd:pfam08242  90 ------RLLKPGGVL 98
 
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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