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Conserved domains on  [gi|1708794369|ref|XP_029914725|]
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histone-arginine methyltransferase CARM1 [Myripristis murdjan]

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 ...
 32-136 3.98e-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: 226.65  E-value: 3.98e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369  32 GVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLSNGEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFSS 111
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1708794369 112 PADFSSFYNLLKNCRGHSGERSVFS 136
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
157-344 1.32e-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: 152.88  E-value: 1.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 157 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGERVVV 235
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 236 IPGKVEEVTLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGKMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 314
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1708794369 315 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 344
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 ...
 32-136 3.98e-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: 226.65  E-value: 3.98e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369  32 GVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLSNGEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFSS 111
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1708794369 112 PADFSSFYNLLKNCRGHSGERSVFS 136
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 28-137 8.18e-58

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: 189.15  E-value: 8.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369  28 SVFPGVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLsngEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLL 107
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVLSTN---EDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1708794369 108 QFSSPADFSSFYNLLKNCRGHSGERSVFSE 137
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
157-344 1.32e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.88  E-value: 1.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 157 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGERVVV 235
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 236 IPGKVEEVTLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGKMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 314
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1708794369 315 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 344
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 186-287 1.75e-13

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: 66.68  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 186 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNRLGERVVVIPGKVEEVTL--PEQVDIIISEPMGYMLFN 263
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1708794369 264 --ERMLESYLHAkkfLKPNGKMFPTI 287
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 186-281 3.60e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 186 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEvlVNSNRLGERVVVIPGKVEEVTLP-EQVDIIISePMGYMLFN 263
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERAR--ERAAEAGLNVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1708794369 264 ERMLESYLH-AKKFLKPNG 281
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
167-211 1.61e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.93  E-value: 1.61e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1708794369 167 TGTYQ------RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAV 211
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 180-281 3.03e-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: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 180 DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNRLGERVVVI-PGKVEEVTLPeqVDIIISEpm 257
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 1708794369 258 gymLFNERMLESYLHAKKFLKPNG 281
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 32-136 3.98e-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: 226.65  E-value: 3.98e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369  32 GVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLSNGEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFSS 111
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1708794369 112 PADFSSFYNLLKNCRGHSGERSVFS 136
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 28-137 8.18e-58

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: 189.15  E-value: 8.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369  28 SVFPGVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLsngEETCVFKCSVSRETECSRVGKQSFIITLGCNSVLL 107
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVLSTN---EDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1708794369 108 QFSSPADFSSFYNLLKNCRGHSGERSVFSE 137
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
157-344 1.32e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.88  E-value: 1.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 157 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGERVVV 235
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 236 IPGKVEEVTLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGKMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 314
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1708794369 315 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 344
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 186-287 1.75e-13

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: 66.68  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 186 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNRLGERVVVIPGKVEEVTL--PEQVDIIISEPMGYMLFN 263
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1708794369 264 --ERMLESYLHAkkfLKPNGKMFPTI 287
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
173-256 1.07e-12

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 67.24  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 173 AILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAStmAQHAEVLV-NSNRLGERVVVIPGKVEEVTLPEQVDI 251
Cdd:COG2263    38 AYLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIAReNAERLGVRVDFIRADVTRIPLGGSVDT 113


                  ....*
gi 1708794369 252 IISEP 256
Cdd:COG2263   114 VVMNP 118
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
172-281 1.08e-11

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 65.96  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 172 RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNRLGERVVVIPGKVEEvt 244
Cdd:COG2264   140 EALEKL--LKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA--RENAEL----NGVEDRIEVVLGDLLE-- 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1708794369 245 lPEQVDI----IISEPmgymLfnERMLESYlhaKKFLKPNG 281
Cdd:COG2264   210 -DGPYDLvvanILANP----L--IELAPDL---AALLKPGG 240
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 161-284 1.69e-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: 61.57  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 161 MQDYVRTGTYQRAILQ--NHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNRLGERVVVIP 237
Cdd:COG2227     1 MSDPDARDFWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISpEALEIAR----ERAAELNVDFVQ 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1708794369 238 GKVEEVTLP-EQVDIIIS-EPMGYMLFNERMLEsylHAKKFLKPNGKMF 284
Cdd:COG2227    76 GDLEDLPLEdGSFDLVICsEVLEHLPDPAALLR---ELARLLKPGGLLL 121
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 186-284 3.60e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 61.87  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 186 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGERVVVIPGKVEEVTLPEQVDIIISEPMgYMLFNE 264
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                          90       100
                  ....*....|....*....|.
gi 1708794369 265 RMLESYL-HAKKFLKPNGKMF 284
Cdd:COG2230   134 ENYPAYFaKVARLLKPGGRLL 154
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 186-281 3.60e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 186 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEvlVNSNRLGERVVVIPGKVEEVTLP-EQVDIIISePMGYMLFN 263
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERAR--ERAAEAGLNVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1708794369 264 ERMLESYLH-AKKFLKPNG 281
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 172-298 2.31e-10

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: 60.67  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 172 RAILQnHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAeVLVNSNRLGERVVVIPGKVEEVTLPEQVDI 251
Cdd:COG3897    61 RYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAA-LRLNAALNGVAITTRLGDWRDPPAAGGFDL 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1708794369 252 IIsepMGYMLFNERMLEsYLHA--KKFLKPNGKMFptIGD---VHLAPFTDE 298
Cdd:COG3897   139 IL---GGDVLYERDLAE-PLLPflDRLAAPGGEVL--IGDpgrGYLPAFRER 184
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 172-284 1.66e-09

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: 57.22  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 172 RAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNRLgERVVVIPGKVEEVTLPEQV 249
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1708794369 250 DIIISEP-------MGYMLfNERMLEsylHAKKFLKPNGKMF 284
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 162-281 7.48e-09

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: 55.29  E-value: 7.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 162 QDYVRTGTYQRAI---LQNHTDFKDK-----VVLDVGCGSGIL---SFFAAQAGAR--KVYAVEASTMA----QHaevLV 224
Cdd:pfam05185  35 KDPVKYDLYERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEETGTkvKIYAVEKNPNAyvtlQK---RI 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1708794369 225 NSNRLGERVVVIPGKVEEVTLPEQVDIIISEPMGYMLFNERMLESYLHAKKFLKPNG 281
Cdd:pfam05185 112 NFEKWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 172-310 1.06e-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: 54.23  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 172 RAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVnsNRLGERVVVIPGKVEEVTLP-EQV 249
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISpEMLELARERA--AEAGLNVEFVVGDAEDLPFPdGSF 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708794369 250 DIIISePMGYMLFN--ERMLEsylHAKKFLKPNGKMFptIGDVHlAPFTDEqlYMEQFTKANF 310
Cdd:COG2226    89 DLVIS-SFVLHHLPdpERALA---EIARVLKPGGRLV--VVDFS-PPDLAE--LEELLAEAGF 142
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
167-211 1.61e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.93  E-value: 1.61e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1708794369 167 TGTYQ------RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAV 211
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 186-284 1.18e-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: 52.84  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 186 VLDVGCGSGILSFFAAQ-AGARKVYAVE----ASTMAQHAevlVNSNRLGERVVVIPGKVEEVT---LPEQVDIIISEPm 257
Cdd:COG4123    41 VLDLGTGTGVIALMLAQrSPGARITGVEiqpeAAELARRN---VALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP- 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1708794369 258 GYMLFNE------------RM-----LESYLH-AKKFLKPNGKMF 284
Cdd:COG4123   117 PYFKAGSgrkspdearaiaRHedaltLEDLIRaAARLLKPGGRFA 161
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 180-281 3.03e-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: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 180 DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNRLGERVVVI-PGKVEEVTLPeqVDIIISEpm 257
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 1708794369 258 gymLFNERMLESYLHAKKFLKPNG 281
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 182-281 5.13e-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: 51.50  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 182 KDKVVLDVGCGSGILSFFAAQAGARKVYAVE----ASTMAQH-AEVlvnsNRLGERVVVI-PGKVEEvtlpEQVDI---- 251
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDidpvAVRAAKEnAEL----NGVEARLEVYlPGDLPK----EKADVvvan 232

                          90       100       110
                  ....*....|....*....|....*....|
gi 1708794369 252 IISEPMgymlfnERMLEsylHAKKFLKPNG 281
Cdd:pfam06325 233 ILADPL------IELAP---DIYALVKPGG 253
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 187-284 6.98e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 47.66  E-value: 6.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 187 LDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNRLGERVvvipGKVEEVTLP-EQVDIIISEpmgYMLFNE 264
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISpEMLELAREKAPREGLTFVV----GDAEDLPFPdNSFDLVLSS---EVLHHV 72

                          90       100
                  ....*....|....*....|.
gi 1708794369 265 RMLESYLH-AKKFLKPNGKMF 284
Cdd:pfam08241  73 EDPERALReIARVLKPGGILI 93
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
186-254 7.97e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.51  E-value: 7.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708794369 186 VLDVGCGSGILS-FFAAQAGARKVYAVEAS-TMAQHAevlvnsNRLGERVVVIPGKVEEVTLPEQVDIIIS 254
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVDLSpEMLARA------RARLPNVRFVVADLRDLDPPEPFDLVVS 69
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 163-284 1.19e-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: 46.34  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 163 DYVRTGTyqRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGA-RKVYAVEASTMA-QHAEVLVNSNRLgERVVVIPGKV 240
Cdd:COG2813    32 DRLDIGT--RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGL-ENVEVLWSDG 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1708794369 241 EEVTLPEQVDIIISEP-----------MGYMLFNErmlesylhAKKFLKPNGKMF 284
Cdd:COG2813   109 LSGVPDGSFDLILSNPpfhagravdkeVAHALIAD--------AARHLRPGGELW 155
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
184-288 1.21e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 47.21  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 184 KVVLDVGCGSGILSFFAAQAGARKVYAVEAStmaqhAEVL----VN--SNRL-GERVVVIPGKVEEV--TLP-EQVDIII 253
Cdd:COG2521   134 DRVLDTCTGLGYTAIEALKRGAREVITVEKD-----PNVLelaeLNpwSRELaNERIKIILGDASEVikTFPdESFDAII 208

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1708794369 254 SEPmgyMLFNermLESYLHAKKF-------LKPNGKMFPTIG 288
Cdd:COG2521   209 HDP---PRFS---LAGELYSLEFyrelyrvLKPGGRLFHYTG 244
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 174-281 1.33e-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: 45.84  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 174 ILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAStmAQHAEVLV-NSNRLG--ERVVVIPGKVEEV---TLPE 247
Cdd:COG0742    35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEKD--RKAAAVIRkNLEKLGleDRARVIRGDALRFlkrLAGE 110

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1708794369 248 QVDIIISEP---MGYMlfnERMLESyLHAKKFLKPNG 281
Cdd:COG0742   111 PFDLVFLDPpyaKGLL---EKALEL-LAENGLLAPGG 143
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 175-227 1.78e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 46.37  E-value: 1.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1708794369 175 LQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVE-ASTMAQHA-----EVLVNSN 227
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEArerapEAGLAGN 113
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
174-284 2.57e-05

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 45.31  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 174 ILQNHtdFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAeVLVNSNRLGERVVVIPGKVEEVTL-----PEQ 248
Cdd:pfam03602  35 WLAPY--IEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQI-LKENLQLLGLPGAVLVMDALLALLrlagkGPV 111

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1708794369 249 VDIIISEPmGYM--LFNERMleSYLHAKKFLKPNGKMF 284
Cdd:pfam03602 112 FDIVFLDP-PYAkgLIEEVL--DLLAEKGWLKPNALIY 146
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
174-254 5.69e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 45.28  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 174 ILQNHTDFKDKVVLDVGCGSGILSFFAAQAgARKVYAVEA-STMAQHAEVLVNSNrlgERVVVIPGKVEEVTLPEqVDII 252
Cdd:PRK14896   21 IVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIAA---GNVEIIEGDALKVDLPE-FNKV 95


                  ..
gi 1708794369 253 IS 254
Cdd:PRK14896   96 VS 97
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 182-284 1.57e-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: 42.96  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 182 KDKVVLDVGCGSGilSF--FAAQAGARKVYAVEASTMAqhaevlVNSNRLGERVVVIPG---------KVEEvTLPEQVD 250
Cdd:pfam01728  21 PGKTVLDLGAAPG--GWsqVALQRGAGKVVGVDLGPMQ------LWKPRNDPGVTFIQGdirdpetldLLEE-LLGRKVD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1708794369 251 III---SEPMGYMLFNERMLESYLH------AKKFLKPNG----KMF 284
Cdd:pfam01728  92 LVLsdgSPFISGNKVLDHLRSLDLVkaalevALELLRKGGnfvcKVF 138
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 172-256 2.23e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 43.60  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 172 RAILQNHTDFKDKVVLDVGCGSGI--LSFFAAQAGARkVYAVEAST----MAQHaevlvNSNRLG--ERVVVIPGKV-EE 242
Cdd:COG2890   102 ELALALLPAGAPPRVLDLGTGSGAiaLALAKERPDAR-VTAVDISPdalaVARR-----NAERLGleDRVRFLQGDLfEP 175

                          90
                  ....*....|....
gi 1708794369 243 VTLPEQVDIIISEP 256
Cdd:COG2890   176 LPGDGRFDLIVSNP 189
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 186-281 3.31e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.21  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 186 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGE-RVVVIPGKVEEVTLPEQVDIIISepMGYM-LF 262
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVA--FGVLhHL 107

                          90       100
                  ....*....|....*....|
gi 1708794369 263 NERMLESYLH-AKKFLKPNG 281
Cdd:COG0500   108 PPEEREALLReLARALKPGG 127
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
170-258 6.19e-04

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.15  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 170 YQRaiLQNHT-DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS--TMAQ-HA-EVLVNSNRlgeRVVVIPGKVEEVT 244
Cdd:PRK15068  111 WDR--VLPHLsPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSqlFLCQfEAvRKLLGNDQ---RAHLLPLGIEQLP 185

                          90
                  ....*....|....
gi 1708794369 245 LPEQVDIIISepMG 258
Cdd:PRK15068  186 ALKAFDTVFS--MG 197
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 173-254 6.61e-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: 41.50  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 173 AILQNHTDFKDKVVLDVGCGSGILSF-FAAQAGARKVYAVEAS-TMAQHAEvlvnsNRLGERVVVIPGKVEEVTLPE-QV 249
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISaGMLAQAK-----TKLSENVQFICGDAEKLPLEDsSF 99


                  ....*
gi 1708794369 250 DIIIS 254
Cdd:TIGR02072 100 DLIVS 104
PRK14967 PRK14967
putative methyltransferase; Provisional
 186-256 6.81e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 41.58  E-value: 6.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708794369 186 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQhAEVLVNSNRLGERVVVIPGKVEEVTLPEQVDIIISEP 256
Cdd:PRK14967   40 VLDLCTGSGALAVAAAAAGAGSVTAVDISRRAV-RSARLNALLAGVDVDVRRGDWARAVEFRPFDVVVSNP 109
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
163-254 8.44e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 40.75  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 163 DYVRTGTYQRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNRLGERVVVipGKVE 241
Cdd:COG4976    27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSeEMLAKAR----EKGVYDRLLV--ADLA 99

                          90
                  ....*....|....
gi 1708794369 242 EVT-LPEQVDIIIS 254
Cdd:COG4976   100 DLAePDGRFDLIVA 113
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 172-324 8.95e-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: 41.57  E-value: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 172 RAILQNHTDFKdkvVLDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNRLGERVVVIPGKVEEVTLPEQV 249
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 250 DIIISEPmGYMLFNE--RMLESYLH----------------------AKKFLKPNGKMFPTIGDVHLApftdeqLYMEQF 305
Cdd:TIGR00536 184 DIIVSNP-PYIDEEDlaDLPNVVRFepllalvggddglnilrqiielAPDYLKPNGFLVCEIGNWQQK------SLKELL 256

                         170
                  ....*....|....*....
gi 1708794369 306 TKANFWYQPSFHGvDLSAL 324
Cdd:TIGR00536 257 RIKFTWYDVENGR-DLNGK 274
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 182-253 1.00e-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: 41.70  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708794369 182 KDKVVLDVGCGSGILSFFAAQAgARKVYAVEAS-TMAQHAEvlVNSNRLG-ERVVVIPGKVEEVtLPEQV-----DIII 253
Cdd:COG2265   233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDAR--ENARLNGlKNVEFVAGDLEEV-LPELLwggrpDVVV 307
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 170-315 1.25e-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: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 170 YQRaILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA----QHAEVLVNSNRlgeRVVVIPGKVEEVTL 245
Cdd:pfam08003 104 WDR-VLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFlcqfEAVRKLLGNDQ---RAHLLPLGIEQLPA 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708794369 246 PEQVDIIISepMGYMLFNERMLESYLHAKKFLKPNGKM-FPTI---GDVHLAPFTDEQlYMEQftkANFWYQPS 315
Cdd:pfam08003 180 LAAFDTVFS--MGVLYHRRSPLDHLLQLKDQLVKGGELvLETLvidGDENTVLVPGDR-YAQM---RNVYFIPS 247
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 182-283 1.50e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 38.85  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 182 KDKVVLDVGCGSGILSFFAA-QAGARKVYAVEAStmAQHAEVL-VNSNRLGE-RVVVIPGKVEEVT--LPEQVDIIISEP 256
Cdd:TIGR02469  19 PGDVLWDIGAGTGSVTIEAArLVPNGRVYAIERN--PEALDLIeRNLRRFGVsNIVIVEGDAPEAPeaLLPDPDAVFVGG 96

                          90       100
                  ....*....|....*....|....*...
gi 1708794369 257 MGymlfneRMLESYLHA-KKFLKPNGKM 283
Cdd:TIGR02469  97 SG------GLLQEILEAvERRLRPGGRI 118
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 180-252 1.66e-03

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


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 40.43  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 180 DFKDKVVLDVGCGSG-----ILsffaaQAGARKVYAVEASTmAQHAEVLVNSnrlgERVVVIPG----KVEEVTLPEQVD 250
Cdd:COG1189    75 DVAGKVCLDIGASTGgftdcLL-----QRGAAKVYAVDVGY-GQLAWKLRQD----PRVVVLERtnarYLTPEDLPEPPD 144


                  ..
gi 1708794369 251 II 252
Cdd:COG1189   145 LV 146
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 187-282 1.71e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.12  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 187 LDVGCGSGILSFFAAQAGAR-KVYAVEAST--MAQHAEVLVNSNRLGERVVVIPGKVEEVTLPEQVDIIISEpmGYMLFN 263
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISPaaLEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS--NVLHHL 78

                          90
                  ....*....|....*....
gi 1708794369 264 ERMLESYLHAKKFLKPNGK 282
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGV 97
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 182-243 3.05e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 40.15  E-value: 3.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708794369 182 KDKVVLDVGCGSGILSFFAAQAGAR-KVYAVEastmaQHAEVLV----NSNRLG-ERVVVIPGKVEEV 243
Cdd:COG2242   247 PGDVLWDIGAGSGSVSIEAARLAPGgRVYAIE-----RDPERAAliraNARRFGvPNVEVVEGEAPEA 309
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 185-237 4.40e-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: 4.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1708794369 185 VVLDVGCGSGILSFFAAQAGAR-KVYAVEAST-MAQHAEVLVNSNRLgERVVVIP 237
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNL-PNVVLLN 54
PRK14968 PRK14968
putative methyltransferase; Provisional
 167-213 4.85e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 4.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1708794369 167 TGTYQRA-----ILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKV------YAVEA 213
Cdd:PRK14968    3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC 60
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 173-256 6.33e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.99  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708794369 173 AILQNHTDFKDKVVLDVGCGSGILSffAAQAGAR---KVYAVEAS----TMAQH-AEvlvnsNRLGERVVVIPGKVEEVT 244
Cdd:PRK09328   99 WALEALLLKEPLRVLDLGTGSGAIA--LALAKERpdaEVTAVDISpealAVARRnAK-----HGLGARVEFLQGDWFEPL 171

                          90
                  ....*....|..
gi 1708794369 245 LPEQVDIIISEP 256
Cdd:PRK09328  172 PGGRFDLIVSNP 183
 
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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