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Conserved domains on  [gi|1992466046|ref|XP_039543694|]
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histone-arginine methyltransferase CARM1 isoform X2 [Pimephales promelas]

Protein Classification

histone-arginine methyltransferase CARM1( domain architecture ID 11189515)

histone-arginine methyltransferase CARM1 (coactivator-associated arginine methyltransferase 1) catalyzes the methylation (mono- and asymmetric dimethylation) of the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 15-119 7.23e-72

Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine methyltransferase which methylates a variety of different proteins and plays a role in gene expression. This is the N terminal domain of the protein which has a PH domain, normally present to regulate protein-protein interactions.A molecular switch is also present on the N terminal domain.


:

Pssm-ID: 402914  Cd Length: 105  Bit Score: 225.49  E-value: 7.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046  15 GVRLLSIGDANGDIQRHSEQQPLRLEIKTNQDAALISLSNNEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFAS 94
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1992466046  95 PADFSSFYNLLKNCRGHRGERSVFS 119
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
140-327 4.34e-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: 151.34  E-value: 4.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 140 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLSERVVV 218
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 219 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPSGKMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 297
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1992466046 298 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 327
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 15-119 7.23e-72

Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine methyltransferase which methylates a variety of different proteins and plays a role in gene expression. This is the N terminal domain of the protein which has a PH domain, normally present to regulate protein-protein interactions.A molecular switch is also present on the N terminal domain.


Pssm-ID: 402914  Cd Length: 105  Bit Score: 225.49  E-value: 7.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046  15 GVRLLSIGDANGDIQRHSEQQPLRLEIKTNQDAALISLSNNEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFAS 94
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1992466046  95 PADFSSFYNLLKNCRGHRGERSVFS 119
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 11-120 1.52e-60

Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known as protein arginine methyltransferase 4/PRMT4) is a protein arginine methyltransferase recruited by several transcription factors. It methylates a variety of proteins and plays a role in gene expression. The N-terminal domain of CARM1 contains a N-terminal PH domain, a catalytic core module composed of two parts (a Rossmann fold topology (RF) and a beta-barrel), and a C-terminal domain. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may explain how CARM1 regulates its biological activities by protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241484  Cd Length: 107  Bit Score: 196.08  E-value: 1.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046  11 SVFPGVRLLSIGDANGDIQRHSEQQPLRLEIKTNQDAALislSNNEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLL 90
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVL---STNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1992466046  91 QFASPADFSSFYNLLKNCRGHRGERSVFSE 120
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
140-327 4.34e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 151.34  E-value: 4.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 140 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLSERVVV 218
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 219 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPSGKMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 297
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1992466046 298 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 327
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 169-270 1.42e-12

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: 64.37  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 169 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNRLSERVVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 246
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1992466046 247 --ERMLESYLHAkkfLKPSGKMFPTI 270
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 169-264 1.15e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.34  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 169 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLseRVVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 246
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1992466046 247 ERMLESYLH-AKKFLKPSG 264
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
150-194 1.55e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.93  E-value: 1.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1992466046 150 TGTYQ------RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAV 194
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 163-264 1.21e-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: 53.68  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 163 DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNRLSERVVVI-PGKVEEVSLPeqVDIIISEpm 240
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 1992466046 241 gymLFNERMLESYLHAKKFLKPSG 264
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 15-119 7.23e-72

Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine methyltransferase which methylates a variety of different proteins and plays a role in gene expression. This is the N terminal domain of the protein which has a PH domain, normally present to regulate protein-protein interactions.A molecular switch is also present on the N terminal domain.


Pssm-ID: 402914  Cd Length: 105  Bit Score: 225.49  E-value: 7.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046  15 GVRLLSIGDANGDIQRHSEQQPLRLEIKTNQDAALISLSNNEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFAS 94
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1992466046  95 PADFSSFYNLLKNCRGHRGERSVFS 119
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 11-120 1.52e-60

Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known as protein arginine methyltransferase 4/PRMT4) is a protein arginine methyltransferase recruited by several transcription factors. It methylates a variety of proteins and plays a role in gene expression. The N-terminal domain of CARM1 contains a N-terminal PH domain, a catalytic core module composed of two parts (a Rossmann fold topology (RF) and a beta-barrel), and a C-terminal domain. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may explain how CARM1 regulates its biological activities by protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241484  Cd Length: 107  Bit Score: 196.08  E-value: 1.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046  11 SVFPGVRLLSIGDANGDIQRHSEQQPLRLEIKTNQDAALislSNNEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLL 90
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVL---STNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1992466046  91 QFASPADFSSFYNLLKNCRGHRGERSVFSE 120
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
140-327 4.34e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 151.34  E-value: 4.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 140 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLSERVVV 218
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 219 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPSGKMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 297
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1992466046 298 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 327
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 169-270 1.42e-12

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: 64.37  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 169 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNRLSERVVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 246
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1992466046 247 --ERMLESYLHAkkfLKPSGKMFPTI 270
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
156-239 2.97e-12

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 65.70  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 156 AILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAStmAQHAEVLV-NSNRLSERVVVIPGKVEEVSLPEQVDI 234
Cdd:COG2263    38 AYLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIAReNAERLGVRVDFIRADVTRIPLGGSVDT 113


                  ....*
gi 1992466046 235 IISEP 239
Cdd:COG2263   114 VVMNP 118
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
155-236 5.49e-12

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 66.74  E-value: 5.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 155 RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNRLSERVVVIPGKVEEvs 227
Cdd:COG2264   140 EALEKL--LKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA--RENAEL----NGVEDRIEVVLGDLLE-- 209


                  ....*....
gi 1992466046 228 lPEQVDIII 236
Cdd:COG2264   210 -DGPYDLVV 217
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 144-267 3.87e-11

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: 60.80  E-value: 3.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 144 MQDYVRTGTYQRAILQ--NHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNRLSERVVVIP 220
Cdd:COG2227     1 MSDPDARDFWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISpEALEIAR----ERAAELNVDFVQ 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1992466046 221 GKVEEVSLP-EQVDIIIS-EPMGYMLFNERMLEsylHAKKFLKPSGKMF 267
Cdd:COG2227    76 GDLEDLPLEdGSFDLVICsEVLEHLPDPAALLR---ELARLLKPGGLLL 121
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 169-267 5.12e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 61.10  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 169 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLSERVVVIPGKVEEVSLPEQVDIIISEPMgYMLFNE 247
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                          90       100
                  ....*....|....*....|.
gi 1992466046 248 RMLESYL-HAKKFLKPSGKMF 267
Cdd:COG2230   134 ENYPAYFaKVARLLKPGGRLL 154
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 169-264 1.15e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.34  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 169 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLseRVVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 246
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1992466046 247 ERMLESYLH-AKKFLKPSG 264
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 155-281 2.48e-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: 57.59  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 155 RAILQnHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHA-EVLVNSNRLSerVVVIPGKVEEVSLPEQVD 233
Cdd:COG3897    61 RYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAAlRLNAALNGVA--ITTRLGDWRDPPAAGGFD 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1992466046 234 IIIsepMGYMLFNERMLEsYLHA--KKFLKPSGKMFptIGD---VHLAPFTDE 281
Cdd:COG3897   138 LIL---GGDVLYERDLAE-PLLPflDRLAAPGGEVL--IGDpgrGYLPAFRER 184
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 145-264 1.03e-08

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: 54.90  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 145 QDYVRTGTYQRAI---LQNHTDFKDK-----VVLDVGCGSGIL---SFFAAQAGAR--KVYAVEASTMA----QHaevLV 207
Cdd:pfam05185  35 KDPVKYDLYERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEETGTkvKIYAVEKNPNAyvtlQK---RI 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1992466046 208 NSNRLSERVVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKFLKPSG 264
Cdd:pfam05185 112 NFEKWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
150-194 1.55e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.93  E-value: 1.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1992466046 150 TGTYQ------RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAV 194
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 155-267 1.69e-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: 54.13  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 155 RAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNRLsERVVVIPGKVEEVSLPEQV 232
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1992466046 233 DIIISEP-------MGYMLfNERMLEsylHAKKFLKPSGKMF 267
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 155-293 3.49e-08

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: 52.69  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 155 RAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNRLseRVVVIPGKVEEVSLP-EQV 232
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISpEMLELARERAAEAGL--NVEFVVGDAEDLPFPdGSF 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1992466046 233 DIIISePMGYMLFN--ERMLEsylHAKKFLKPSGKMFptIGDVHlAPFTDEqlYMEQFTKANF 293
Cdd:COG2226    89 DLVIS-SFVLHHLPdpERALA---EIARVLKPGGRLV--VVDFS-PPDLAE--LEELLAEAGF 142
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 163-264 1.21e-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: 53.68  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 163 DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNRLSERVVVI-PGKVEEVSLPeqVDIIISEpm 240
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 1992466046 241 gymLFNERMLESYLHAKKFLKPSG 264
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 165-264 1.51e-07

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: 53.42  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 165 KDKVVLDVGCGSGILSFFAAQAGARKVYAVE----ASTMAQH-AEVlvnsNRLSERVVVI-PGKVEEvslpEQVDI---- 234
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDidpvAVRAAKEnAEL----NGVEARLEVYlPGDLPK----EKADVvvan 232

                          90       100       110
                  ....*....|....*....|....*....|
gi 1992466046 235 IISEPMgymlfnERMLEsylHAKKFLKPSG 264
Cdd:pfam06325 233 ILADPL------IELAP---DIYALVKPGG 253
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 169-267 2.15e-07

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: 52.07  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 169 VLDVGCGSGILSFFAAQ-AGARKVYAVE----ASTMAQHAevlVNSNRLSERVVVIPGKVEEVS---LPEQVDIIISEPm 240
Cdd:COG4123    41 VLDLGTGTGVIALMLAQrSPGARITGVEiqpeAAELARRN---VALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP- 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1992466046 241 GYMLFNE------------RM-----LESYLH-AKKFLKPSGKMF 267
Cdd:COG4123   117 PYFKAGSgrkspdearaiaRHedaltLEDLIRaAARLLKPGGRFA 161
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
169-237 1.16e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.13  E-value: 1.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1992466046 169 VLDVGCGSGILS-FFAAQAGARKVYAVEAS-TMAQHAevlvnsNRLSERVVVIPGKVEEVSLPEQVDIIIS 237
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVDLSpEMLARA------RARLPNVRFVVADLRDLDPPEPFDLVVS 69
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 170-267 1.49e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 46.50  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 170 LDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNRLSERVvvipGKVEEVSLP-EQVDIIISEpmgYMLFNE 247
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISpEMLELAREKAPREGLTFVV----GDAEDLPFPdNSFDLVLSS---EVLHHV 72

                          90       100
                  ....*....|....*....|.
gi 1992466046 248 RMLESYLH-AKKFLKPSGKMF 267
Cdd:pfam08241  73 EDPERALReIARVLKPGGILI 93
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 158-210 1.72e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 46.37  E-value: 1.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1992466046 158 LQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVE-ASTMAQHA-----EVLVNSN 210
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEArerapEAGLAGN 113
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
157-237 2.33e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 46.05  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 157 ILQNHTDFKDKVVLDVGCGSGILSFFAAQAgARKVYAVEA-STMAQHAEvlvnsNRLSE--RVVVIPGKVEEVSLPEqVD 233
Cdd:PRK14896   21 IVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLR-----DDEIAagNVEIIEGDALKVDLPE-FN 93


                  ....
gi 1992466046 234 IIIS 237
Cdd:PRK14896   94 KVVS 97
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 157-235 2.84e-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: 45.07  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 157 ILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVE-----ASTMAQHAEVLvnsnRLSERVVVIPGKVEEV---SL 228
Cdd:COG0742    35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEkdrkaAAVIRKNLEKL----GLEDRARVIRGDALRFlkrLA 108


                  ....*..
gi 1992466046 229 PEQVDII 235
Cdd:COG0742   109 GEPFDLV 115
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
167-271 9.50e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.51  E-value: 9.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 167 KVVLDVGCGSGILSFFAAQAGARKVYAVEAStmaqhAEVL----VN--SNRLS-ERVVVIPGKVEEV--SLP-EQVDIII 236
Cdd:COG2521   134 DRVLDTCTGLGYTAIEALKRGAREVITVEKD-----PNVLelaeLNpwSRELAnERIKIILGDASEVikTFPdESFDAII 208

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1992466046 237 SEPmgyMLFNermLESYLHAKKF-------LKPSGKMFPTIG 271
Cdd:COG2521   209 HDP---PRFS---LAGELYSLEFyrelyrvLKPGGRLFHYTG 244
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 146-267 1.05e-04

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: 43.64  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 146 DYVRTGTyqRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGA-RKVYAVEASTMAqhaevlVNSNRLS------ERVVV 218
Cdd:COG2813    32 DRLDIGT--RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARA------VELARANaaanglENVEV 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 219 IPGKVEEVSLPEQVDIIISEP-----------MGYMLFNErmlesylhAKKFLKPSGKMF 267
Cdd:COG2813   104 LWSDGLSGVPDGSFDLILSNPpfhagravdkeVAHALIAD--------AARHLRPGGELW 155
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 156-237 1.69e-04

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: 43.43  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 156 AILQNHTDFKDKVVLDVGCGSGILSF-FAAQAGARKVYAVEAS-TMAQHAEvlvnsNRLSERVVVIPGKVEEVSLPE-QV 232
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISaGMLAQAK-----TKLSENVQFICGDAEKLPLEDsSF 99


                  ....*
gi 1992466046 233 DIIIS 237
Cdd:TIGR02072 100 DLIVS 104
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
153-241 2.56e-04

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 43.31  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 153 YQRaiLQNHT-DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS--TMAQ-HA-EVLVNSNRlseRVVVIPGKVEEVS 227
Cdd:PRK15068  111 WDR--VLPHLsPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSqlFLCQfEAvRKLLGNDQ---RAHLLPLGIEQLP 185

                          90
                  ....*....|....
gi 1992466046 228 LPEQVDIIISepMG 241
Cdd:PRK15068  186 ALKAFDTVFS--MG 197
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 155-239 2.97e-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: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 155 RAILQNHTDFKDKVVLDVGCGSGI--LSFFAAQAGARkVYAVEASTMA-QHAEVLVNSNRLSERVVVIPGKV-EEVSLPE 230
Cdd:COG2890   102 ELALALLPAGAPPRVLDLGTGSGAiaLALAKERPDAR-VTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDG 180


                  ....*....
gi 1992466046 231 QVDIIISEP 239
Cdd:COG2890   181 RFDLIVSNP 189
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 163-235 5.10e-04

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 41.97  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 163 DFKDKVVLDVGCGSG-----ILsffaaQAGARKVYAVEastmaqhaevlVNSNRLS------ERVVVIPG----KVEEVS 227
Cdd:COG1189    75 DVAGKVCLDIGASTGgftdcLL-----QRGAAKVYAVD-----------VGYGQLAwklrqdPRVVVLERtnarYLTPED 138


                  ....*...
gi 1992466046 228 LPEQVDII 235
Cdd:COG1189   139 LPEPPDLV 146
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 165-267 5.95e-04

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 41.04  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 165 KDKVVLDVGCGSGilSF--FAAQAGARKVYAVEASTMAqhaevlVNSNRLSERVVVIPG---------KVEEVsLPEQVD 233
Cdd:pfam01728  21 PGKTVLDLGAAPG--GWsqVALQRGAGKVVGVDLGPMQ------LWKPRNDPGVTFIQGdirdpetldLLEEL-LGRKVD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1992466046 234 III---SEPMGYMLFNERMLESYLH------AKKFLKPSG----KMF 267
Cdd:pfam01728  92 LVLsdgSPFISGNKVLDHLRSLDLVkaalevALELLRKGGnfvcKVF 138
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
146-237 7.17e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 40.75  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 146 DYVRTGTYQRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNRLSERVVvipgkVE 224
Cdd:COG4976    27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSeEMLAKAREKGVYDRLLVADL-----AD 100

                          90
                  ....*....|...
gi 1992466046 225 EVSLPEQVDIIIS 237
Cdd:COG4976   101 LAEPDGRFDLIVA 113
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 169-264 1.01e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 40.67  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 169 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLSE-RVVVIPGKVEEVSLPEQVDIIISepMGYM-LF 245
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVA--FGVLhHL 107

                          90       100
                  ....*....|....*....|
gi 1992466046 246 NERMLESYLH-AKKFLKPSG 264
Cdd:COG0500   108 PPEEREALLReLARALKPGG 127
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
157-267 1.01e-03

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 40.30  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 157 ILQNHtdFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAeVLVNSNRLSERVVVIPGKVEE-----VSLPEQ 231
Cdd:pfam03602  35 WLAPY--IEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQI-LKENLQLLGLPGAVLVMDALLallrlAGKGPV 111

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1992466046 232 VDIIISEPmGYM--LFNERMleSYLHAKKFLKPSGKMF 267
Cdd:pfam03602 112 FDIVFLDP-PYAkgLIEEVL--DLLAEKGWLKPNALIY 146
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 153-298 1.17e-03

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: 41.24  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 153 YQRaILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA----QHAEVLVNSNRlseRVVVIPGKVEEVSL 228
Cdd:pfam08003 104 WDR-VLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFlcqfEAVRKLLGNDQ---RAHLLPLGIEQLPA 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1992466046 229 PEQVDIIISepMGYMLFNERMLESYLHAKKFLKPSGKM-FPTI---GDVHLAPFTDEQlYMEQftkANFWYQPS 298
Cdd:pfam08003 180 LAAFDTVFS--MGVLYHRRSPLDHLLQLKDQLVKGGELvLETLvidGDENTVLVPGDR-YAQM---RNVYFIPS 247
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 165-236 1.83e-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: 40.93  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1992466046 165 KDKVVLDVGCGSGILSFFAAQAgARKVYAVEAS-TMAQHAEVLVNSNRLsERVVVIPGKVEEVsLPEQV-----DIII 236
Cdd:COG2265   233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDARENARLNGL-KNVEFVAGDLEEV-LPELLwggrpDVVV 307
PRK14967 PRK14967
putative methyltransferase; Provisional
 169-239 3.33e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 3.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1992466046 169 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAqhaevlVNSNRLSERVVVIPGKVEEVSLPEQV-----DIIISEP 239
Cdd:PRK14967   40 VLDLCTGSGALAVAAAAAGAGSVTAVDISRRA------VRSARLNALLAGVDVDVRRGDWARAVefrpfDVVVSNP 109
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 168-213 3.81e-03

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: 38.06  E-value: 3.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1992466046 168 VVLDVGCGSGILSFFAAQAGAR-KVYAVEAST-MAQHAEVLVNSNRLS 213
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNLP 48
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 155-239 4.31e-03

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: 39.26  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992466046 155 RAILQNHTDFKdkvVLDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNRLSERVVVIPGKVEEVSLPEQV 232
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKI 183


                  ....*..
gi 1992466046 233 DIIISEP 239
Cdd:TIGR00536 184 DIIVSNP 190
PRK14968 PRK14968
putative methyltransferase; Provisional
 150-196 4.70e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 4.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1992466046 150 TGTYQRA-----ILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKV------YAVEA 196
Cdd:PRK14968    3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC 60
 
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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