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Conserved domains on  [gi|1818940667|pdb|6S79|B]
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Chain B, Histone-arginine methyltransferase CARM1

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
25-212 1.39e-42

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 147.49  E-value: 1.39e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       25 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 103
Cdd:COG4076  12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B      104 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 182
Cdd:COG4076  90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162
                       170       180       190
                ....*....|....*....|....*....|
6S79_B      183 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 212
Cdd:COG4076 163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
25-212 1.39e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 147.49  E-value: 1.39e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       25 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 103
Cdd:COG4076  12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B      104 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 182
Cdd:COG4076  90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162
                       170       180       190
                ....*....|....*....|....*....|
6S79_B      183 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 212
Cdd:COG4076 163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
54-149 2.53e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         54 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77
                          90
                  ....*....|....*....
6S79_B        132 ERMLESYLH-AKKYLKPSG 149
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
54-149 2.81e-11

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: 59.75  E-value: 2.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       54 VLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 131
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81
                        90       100
                ....*....|....*....|
6S79_B      132 --ERMLESylhAKKYLKPSG 149
Cdd:cd02440  82 dlARFLEE---ARRLLKPGG 98
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
35-79 1.30e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 1.30e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
6S79_B        35 TGTYQ------RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV 79
Cdd:PRK00517 100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
48-149 1.23e-07

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 52.53  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         48 DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEVSLPeqVDIIISEpm 125
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232
                          90       100
                  ....*....|....*....|....
6S79_B        126 gymLFNERMLESYLHAKKYLKPSG 149
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
25-212 1.39e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 147.49  E-value: 1.39e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       25 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 103
Cdd:COG4076  12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B      104 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 182
Cdd:COG4076  90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162
                       170       180       190
                ....*....|....*....|....*....|
6S79_B      183 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 212
Cdd:COG4076 163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
40-121 2.65e-12

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 66.35  E-value: 2.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       40 RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIY-------AVEAStmAQHAEVlvksNNLTDRIVVIPGKVEEvs 112
Cdd:COG2264 140 EALEKL--LKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA--RENAEL----NGVEDRIEVVLGDLLE-- 209

                ....*....
6S79_B      113 lPEQVDIII 121
Cdd:COG2264 210 -DGPYDLVV 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
54-149 2.53e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         54 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77
                          90
                  ....*....|....*....
6S79_B        132 ERMLESYLH-AKKYLKPSG 149
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
54-149 2.81e-11

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: 59.75  E-value: 2.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       54 VLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 131
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81
                        90       100
                ....*....|....*....|
6S79_B      132 --ERMLESylhAKKYLKPSG 149
Cdd:cd02440  82 dlARFLEE---ARRLLKPGG 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
54-152 1.72e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 58.79  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       54 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMgYMLFNE 132
Cdd:COG2230  55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133
                        90       100
                ....*....|....*....|.
6S79_B      133 RMLESYL-HAKKYLKPSGNMF 152
Cdd:COG2230 134 ENYPAYFaKVARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
29-152 4.88e-10

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: 56.56  E-value: 4.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       29 MQDYVRTGTYQRAILQ--NHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLTdrivVIP 105
Cdd:COG2227   1 MSDPDARDFWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISpEALEIARERAAELNVD----FVQ 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
6S79_B      106 GKVEEVSLP-EQVDIIIS-EPMGYMLFNERMLEsylHAKKYLKPSGNMF 152
Cdd:COG2227  76 GDLEDLPLEdGSFDLVICsEVLEHLPDPAALLR---ELARLLKPGGLLL 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
41-124 5.83e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 57.99  E-value: 5.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       41 AILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAStmAQHAEVLvKSN--NLTDRIVVIPGKVEEVSLPEQVD 118
Cdd:COG2263  38 AYLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIA-RENaeRLGVRVDFIRADVTRIPLGGSVD 112

                ....*.
6S79_B      119 IIISEP 124
Cdd:COG2263 113 TVVMNP 118
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
40-121 5.60e-09

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 55.66  E-value: 5.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       40 RAILQnHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHA-EVLVKSNNLTdrIVVIPGKVEEVSLPEQVD 118
Cdd:COG3897  61 RYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAAlRLNAALNGVA--ITTRLGDWRDPPAAGGFD 137

                ...
6S79_B      119 III 121
Cdd:COG3897 138 LIL 140
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
54-124 6.48e-09

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: 55.54  E-value: 6.48e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6S79_B       54 VLDVGCGSGILSFFAAQ-AGARKIYAVE----ASTMAQHAevlVKSNNLTDRIVVIPGKVEEVS---LPEQVDIIISEP 124
Cdd:COG4123  41 VLDLGTGTGVIALMLAQrSPGARITGVEiqpeAAELARRN---VALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP 116
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
50-149 9.09e-09

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 55.73  E-value: 9.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         50 KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEvslpEQVDI----IISE 123
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAvRAAKENAELNGVEARLEVYlPGDLPK----EKADVvvanILAD 236
                          90       100
                  ....*....|....*....|....*.
6S79_B        124 PMgymlfnERMLEsylHAKKYLKPSG 149
Cdd:pfam06325 237 PL------IELAP---DIYALVKPGG 253
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
35-79 1.30e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 1.30e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
6S79_B        35 TGTYQ------RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV 79
Cdd:PRK00517 100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
40-152 1.58e-08

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: 53.36  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         40 RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGAR-KIYAVEASTMA-QHAEVLVKSNNLtDRIVVIPGKVEEVSLPEQV 117
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKF 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
6S79_B        118 DIIISEP-------MGYMLfNERMLEsylHAKKYLKPSGNMF 152
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
48-149 1.23e-07

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 52.53  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         48 DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEVSLPeqVDIIISEpm 125
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232
                          90       100
                  ....*....|....*....|....
6S79_B        126 gymLFNERMLESYLHAKKYLKPSG 149
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
40-149 1.67e-07

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 49.99  E-value: 1.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       40 RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQV 117
Cdd:COG2226  12 EALLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISpEMLELARERAAEAGL--NVEFVVGDAEDLPFPdGSF 88
                        90       100       110
                ....*....|....*....|....*....|....
6S79_B      118 DIIISePMGYMLFN--ERMLEsylHAKKYLKPSG 149
Cdd:COG2226  89 DLVIS-SFVLHHLPdpERALA---EIARVLKPGG 118
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
30-149 2.51e-07

PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding protein 1) is PRMT5, an arginine-N-methyltransferase. These proteins appear to be key mitotic regulators. They play a role in Jak signalling in higher eukaryotes.


Pssm-ID: 428356  Cd Length: 171  Bit Score: 49.90  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         30 QDYVRTGTYQRAI---LQNHTDFKDK-----IVLDVGCGSGIL---SFFAAQAGAR--KIYAVEASTMA----QHaevLV 92
Cdd:pfam05185  35 KDPVKYDLYERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEETGTkvKIYAVEKNPNAyvtlQK---RI 111
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
6S79_B         93 KSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG 149
Cdd:pfam05185 112 NFEKWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
54-122 3.32e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 45.20  E-value: 3.32e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       54 VLDVGCGSGILS-FFAAQAGARKIYAVEAStmaqhAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIIS 122
Cdd:COG4106   5 VLDLGCGTGRLTaLLAERFPGARVTGVDLS-----PEMLARARARLPNVRFVVADLRDLDPPEPFDLVVS 69
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
55-149 4.79e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.58  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         55 LDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLTdrivVIPGKVEEVSLP-EQVDIIISepmGYMLFNE 132
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISpEMLELAREKAPREGLT----FVVGDAEDLPFPdNSFDLVLS---SEVLHHV 72
                          90
                  ....*....|....*...
6S79_B        133 RMLESYLH-AKKYLKPSG 149
Cdd:pfam08241  73 EDPERALReIARVLKPGG 90
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
31-149 1.68e-05

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: 44.80  E-value: 1.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       31 DYVRTGTyqRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGA-RKIYAVEASTMA-QHAEVLVKSNNLTDrIVVIPGKV 108
Cdd:COG2813  32 DRLDIGT--RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGLEN-VEVLWSDG 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
6S79_B      109 EEVSLPEQVDIIISEP-----------MGYMLFNErmlesylhAKKYLKPSG 149
Cdd:COG2813 109 LSGVPDGSFDLILSNPpfhagravdkeVAHALIAD--------AARHLRPGG 152
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
42-120 2.45e-05

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: 44.30  E-value: 2.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       42 ILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAStmAQHAEVLvKSN----NLTDRIVVIPGKVEEV---SLP 114
Cdd:COG0742  35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEKD--RKAAAVI-RKNleklGLEDRARVIRGDALRFlkrLAG 109

                ....*.
6S79_B      115 EQVDII 120
Cdd:COG0742 110 EPFDLV 115
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
43-112 2.61e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 44.83  E-value: 2.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6S79_B        43 LQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVE-ASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVS 112
Cdd:PRK07580  56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL 125
PRK14968 PRK14968
putative methyltransferase; Provisional
35-178 9.92e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.58  E-value: 9.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B        35 TGTYQRA-----ILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKI------YAVEAstmaqhAEVLVKSNNLTDR-IV 102
Cdd:PRK14968   3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC------AKCNAKLNNIRNNgVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       103 VIPGK-VEEVS-------------LPEQVDIIISEPMGYMLF----NERMLESYL-HAKKYLKPSGNMFPTIGDvhlapF 163
Cdd:PRK14968  77 VIRSDlFEPFRgdkfdvilfnppyLPTEEEEEWDDWLNYALSggkdGREVIDRFLdEVGRYLKPGGRILLLQSS-----L 151
                        170
                 ....*....|....*
6S79_B       164 TDEQLYMEQFTKANF 178
Cdd:PRK14968 152 TGEDEVLEYLEKLGF 166
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
42-122 1.06e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 43.35  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B        42 ILQNHTDFKDKIVLDVGCGSGILSFFAAQAgARKIYAVEA-STMAQHA-EVLVKSNNLTdrivVIPGKVEEVSLPEqVDI 119
Cdd:PRK14896  21 IVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLrDDEIAAGNVE----IIEGDALKVDLPE-FNK 94

                 ...
6S79_B       120 IIS 122
Cdd:PRK14896  95 VVS 97
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
40-124 1.74e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.83  E-value: 1.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       40 RAILQNHTDFKDKIVLDVGCGSGI--LSFFAAQAGARkIYAVEASTMA-QHAEVLVKSNNLTDRIVVIPGKV-EEVSLPE 115
Cdd:COG2890 102 ELALALLPAGAPPRVLDLGTGSGAiaLALAKERPDAR-VTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDG 180

                ....*....
6S79_B      116 QVDIIISEP 124
Cdd:COG2890 181 RFDLIVSNP 189
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
38-126 3.08e-04

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.15  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B        38 YQRaiLQNHT-DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS--TMAQ-HA-EVLVKSNNltdRIVVIPGKVEEVS 112
Cdd:PRK15068 111 WDR--VLPHLsPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSqlFLCQfEAvRKLLGNDQ---RAHLLPLGIEQLP 185
                         90
                 ....*....|....
6S79_B       113 LPEQVDIIISepMG 126
Cdd:PRK15068 186 ALKAFDTVFS--MG 197
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
31-122 3.22e-04

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.14  E-value: 3.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       31 DYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAevlvKSNNLTDRIVVipGKVE 109
Cdd:COG4976  27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSeEMLAKA----REKGVYDRLLV--ADLA 99
                        90
                ....*....|....
6S79_B      110 EVS-LPEQVDIIIS 122
Cdd:COG4976 100 DLAePDGRFDLIVA 113
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
53-97 7.82e-04

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 39.22  E-value: 7.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
6S79_B         53 IVLDVGCGSGILSFFAAQAGAR-KIYAVEAST-MAQHAEVLVKSNNL 97
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNL 47
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
38-183 8.47e-04

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 40.85  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         38 YQRaILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTM--AQHaEVLVKSNNLTDRIVVIPGKVEEVSLPE 115
Cdd:pfam08003 104 WDR-VLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELflCQF-EAVRKLLGNDQRAHLLPLGIEQLPALA 181
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6S79_B        116 QVDIIISepMGYMLFNERMLESYLHAKKYLKPSGNM-FPTI---GDVHLAPFTDEQlYMEQftkANFWYQPS 183
Cdd:pfam08003 182 AFDTVFS--MGVLYHRRSPLDHLLQLKDQLVKGGELvLETLvidGDENTVLVPGDR-YAQM---RNVYFIPS 247
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
40-192 8.70e-04

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: 40.41  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         40 RAILQNHTDFKdkiVLDVGCGSGILSFFAAQAGAR-KIYAVEASTMA-QHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQV 117
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKI 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B        118 DIIISEPmGYMLFNE--RMLESYLH----------------------AKKYLKPSGNMFPTIGDVHLApftdeqLYMEQF 173
Cdd:TIGR00536 184 DIIVSNP-PYIDEEDlaDLPNVVRFepllalvggddglnilrqiielAPDYLKPNGFLVCEIGNWQQK------SLKELL 256
                         170
                  ....*....|....*....
6S79_B        174 TKANFWYQPSFHGvDLSAL 192
Cdd:TIGR00536 257 RIKFTWYDVENGR-DLNGK 274
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
50-121 1.24e-03

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: 40.54  E-value: 1.24e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6S79_B       50 KDKIVLDVGCGSGILSFFAAQAgARKIYAVEAS-TMAQHAEVLVKSNNLtDRIVVIPGKVEEVsLPEQV-----DIII 121
Cdd:COG2265 233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDARENARLNGL-KNVEFVAGDLEEV-LPELLwggrpDVVV 307
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
41-122 1.43e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 39.58  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B         41 AILQNHTDFKDKIVLDVGCGSGILSF-FAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTdrivvIPGKVEEVSLPE-QV 117
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISaGMLAQAKTKLSENVQF-----ICGDAEKLPLEDsSF 99

                  ....*
6S79_B        118 DIIIS 122
Cdd:TIGR02072 100 DLIVS 104
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
52-124 1.56e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 39.89  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       52 KIVLDVGCGSGILSFFAAQAGARKIYAVEAStmaqhAEVLVK------SNNLTD-RIVVIPGKVEEV--SLP-EQVDIII 121
Cdd:COG2521 134 DRVLDTCTGLGYTAIEALKRGAREVITVEKD-----PNVLELaelnpwSRELANeRIKIILGDASEVikTFPdESFDAII 208

                ...
6S79_B      122 SEP 124
Cdd:COG2521 209 HDP 211
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
54-149 3.34e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.36  E-value: 3.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6S79_B       54 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTD-RIVVIPGKVEEVSLPEQVDIIISepMGYM-LF 130
Cdd:COG0500  30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVA--FGVLhHL 107
                        90       100
                ....*....|....*....|
6S79_B      131 NERMLESYLH-AKKYLKPSG 149
Cdd:COG0500 108 PPEEREALLReLARALKPGG 127
 
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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