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Conserved domains on  [gi|1207194531|ref|XP_021329875|]
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histone-arginine methyltransferase CARM1 isoform X3 [Danio rerio]

Protein Classification

histone-arginine methyltransferase( domain architecture ID 10351171)

histone-arginine methyltransferase is a type I arginine methyltransferase belonging to the class I SAM-dependent methyltransferase superfamily, similar to Drosophila histone-arginine methyltransferase CARMER that methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins, using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110|2.30.29.30
EC:  2.1.1.319
Gene Ontology:  GO:1904047|GO:0035097|GO:0042054|GO:0018216
PubMed:  12504684|12826405|22728242|15493994
SCOP:  3000118|4002395

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
132-317 5.15e-37

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: 135.16  E-value: 5.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 132 QQNMLQDFLRTATYQKAmlLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEAS-TVAKYAEMLVRSNGLSNKITV 210
Cdd:COG4076    12 HHPMLNDVERNDAFKAA--IERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 211 LSGRIEEVSCPEKVDVIISEPMGYMLLNERMLESFLHA-KHWLKPKGMMFPTQSDIHLAPFTDEhLYMEHHARSNFWnqs 289
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHArKRLLKPGGRIIPERITNAAQPVESP-VDAEGFEDWQFD--- 165

                         170       180
                  ....*....|....*....|....*...
gi 1207194531 290 cFYGVNLSGlhssaVDEFFKQPIVDTFD 317
Cdd:COG4076   166 -GFDFRLFG-----FLLYAEPLLHLTRL 187
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 32-119 6.70e-27

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13330:

Pssm-ID: 473070  Cd Length: 107  Bit Score: 104.02  E-value: 6.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531  32 QHQELTLQVHRELEDINLNITDdagVCVFKFSITKETECCRVATRSFLITLGCFSVLMRFSTQSEFQDFHRMLISWMHLR 111
Cdd:cd13330    23 EQQPLRLEVKAGSVLVLSTNED---VCVFKCSVNRETECSRVGKQSFLITLGCNSVLLQFATPSEFSSFYNALKNCRGQT 99


                  ....*...
gi 1207194531 112 RDQSVFRQ 119
Cdd:cd13330   100 NEKSVFSQ 107
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
132-317 5.15e-37

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 135.16  E-value: 5.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 132 QQNMLQDFLRTATYQKAmlLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEAS-TVAKYAEMLVRSNGLSNKITV 210
Cdd:COG4076    12 HHPMLNDVERNDAFKAA--IERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 211 LSGRIEEVSCPEKVDVIISEPMGYMLLNERMLESFLHA-KHWLKPKGMMFPTQSDIHLAPFTDEhLYMEHHARSNFWnqs 289
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHArKRLLKPGGRIIPERITNAAQPVESP-VDAEGFEDWQFD--- 165

                         170       180
                  ....*....|....*....|....*...
gi 1207194531 290 cFYGVNLSGlhssaVDEFFKQPIVDTFD 317
Cdd:COG4076   166 -GFDFRLFG-----FLLYAEPLLHLTRL 187
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 32-119 6.70e-27

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: 104.02  E-value: 6.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531  32 QHQELTLQVHRELEDINLNITDdagVCVFKFSITKETECCRVATRSFLITLGCFSVLMRFSTQSEFQDFHRMLISWMHLR 111
Cdd:cd13330    23 EQQPLRLEVKAGSVLVLSTNED---VCVFKCSVNRETECSRVGKQSFLITLGCNSVLLQFATPSEFSSFYNALKNCRGQT 99


                  ....*...
gi 1207194531 112 RDQSVFRQ 119
Cdd:cd13330   100 NEKSVFSQ 107
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 32-117 1.06e-21

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: 89.52  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531  32 QHQELTLQVHRELEDINLNITDDAGVCVFKFSITKETECCRVATRSFLITLGCFSVLMRFSTQSEFQDFHRMLISWMHLR 111
Cdd:pfam11531  19 EQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFASPADFCSFYNILKNCRGHK 98


                  ....*.
gi 1207194531 112 RDQSVF 117
Cdd:pfam11531  99 GERSVF 104
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 161-256 3.04e-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: 62.83  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQKVYAVEASTVA-KYAEmLVRSNGLSNKITVLSGRIEEVSC--PEKVDVIISEPMGYMLL 237
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELAR-KAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLV 80

                          90
                  ....*....|....*....
gi 1207194531 238 nERMLESFLHAKHWLKPKG 256
Cdd:cd02440    81 -EDLARFLEEARRLLKPGG 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 161-256 8.78e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.04  E-value: 8.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQKVYAVEASTVA-KYAEMLVRSNGLsnKITVLSGRIEEVSCP-EKVDVIISePMGYMLLN 238
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMlERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1207194531 239 ERMLESFLH-AKHWLKPKG 256
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
155-228 2.37e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 2.37e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207194531 155 DFKDKVVLDVGCGTGILSFFAVQAGAQKVYAV----EASTVAKY-AEMlvrsNGLSNKITVLSGRieevscpEKVDVII 228
Cdd:PRK00517  117 VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVdidpQAVEAAREnAEL----NGVELNVYLPQGD-------LKADVIV 184
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 150-228 4.23e-08

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: 54.45  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 150 LLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEASTVAKYAEMLVRS-NGLSNKITVLSGRIEEVScPEKVDVII 228
Cdd:TIGR00406 152 WLEDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAElNQVSDRLQVKLIYLEQPI-EGKADVIV 230
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
132-317 5.15e-37

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 135.16  E-value: 5.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 132 QQNMLQDFLRTATYQKAmlLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEAS-TVAKYAEMLVRSNGLSNKITV 210
Cdd:COG4076    12 HHPMLNDVERNDAFKAA--IERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 211 LSGRIEEVSCPEKVDVIISEPMGYMLLNERMLESFLHA-KHWLKPKGMMFPTQSDIHLAPFTDEhLYMEHHARSNFWnqs 289
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHArKRLLKPGGRIIPERITNAAQPVESP-VDAEGFEDWQFD--- 165

                         170       180
                  ....*....|....*....|....*...
gi 1207194531 290 cFYGVNLSGlhssaVDEFFKQPIVDTFD 317
Cdd:COG4076   166 -GFDFRLFG-----FLLYAEPLLHLTRL 187
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 32-119 6.70e-27

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: 104.02  E-value: 6.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531  32 QHQELTLQVHRELEDINLNITDdagVCVFKFSITKETECCRVATRSFLITLGCFSVLMRFSTQSEFQDFHRMLISWMHLR 111
Cdd:cd13330    23 EQQPLRLEVKAGSVLVLSTNED---VCVFKCSVNRETECSRVGKQSFLITLGCNSVLLQFATPSEFSSFYNALKNCRGQT 99


                  ....*...
gi 1207194531 112 RDQSVFRQ 119
Cdd:cd13330   100 NEKSVFSQ 107
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 32-117 1.06e-21

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: 89.52  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531  32 QHQELTLQVHRELEDINLNITDDAGVCVFKFSITKETECCRVATRSFLITLGCFSVLMRFSTQSEFQDFHRMLISWMHLR 111
Cdd:pfam11531  19 EQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFASPADFCSFYNILKNCRGHK 98


                  ....*.
gi 1207194531 112 RDQSVF 117
Cdd:pfam11531  99 GERSVF 104
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 161-259 4.52e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.88  E-value: 4.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQKVYAVEASTVA-KYAEMLVRSNGLSNKITVLSGRIEEVSCPEKVDVIISEPMGYMLLNE 239
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSPEQlEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPE 134

                          90       100
                  ....*....|....*....|
gi 1207194531 240 RMLESFLHAKHWLKPKGMMF 259
Cdd:COG2230   135 NYPAYFAKVARLLKPGGRLL 154
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
150-228 2.65e-12

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 67.12  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 150 LLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAV----EASTVAKY-AEMlvrsNGLSNKITVLSGRIEEvscPEKV 224
Cdd:COG2264   141 ALEKLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVdidpVAVEAAREnAEL----NGVEDRIEVVLGDLLE---DGPY 213


                  ....
gi 1207194531 225 DVII 228
Cdd:COG2264   214 DLVV 217
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 161-256 3.04e-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: 62.83  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQKVYAVEASTVA-KYAEmLVRSNGLSNKITVLSGRIEEVSC--PEKVDVIISEPMGYMLL 237
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELAR-KAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLV 80

                          90
                  ....*....|....*....
gi 1207194531 238 nERMLESFLHAKHWLKPKG 256
Cdd:cd02440    81 -EDLARFLEEARRLLKPGG 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 161-256 8.78e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.04  E-value: 8.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQKVYAVEASTVA-KYAEMLVRSNGLsnKITVLSGRIEEVSCP-EKVDVIISePMGYMLLN 238
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMlERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1207194531 239 ERMLESFLH-AKHWLKPKG 256
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
154-231 3.03e-11

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 62.23  E-value: 3.03e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207194531 154 DDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEAS-TVAKYAEMLVRSngLSNKITVLSGRIEEVSCPEKVDVIISEP 231
Cdd:COG2263    42 GDIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDpEALEIARENAER--LGVRVDFIRADVTRIPLGGSVDTVVMNP 118
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 150-259 3.23e-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: 60.42  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 150 LLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQkVYAVEAStvakyAEML--VRSNGLSNKITVLSGRIEEVSCP-EKVDV 226
Cdd:COG2227    17 LLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDIS-----PEALeiARERAAELNVDFVQGDLEDLPLEdGSFDL 90

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207194531 227 IISepmGYMLLNERMLESFL-HAKHWLKPKGMMF 259
Cdd:COG2227    91 VIC---SEVLEHLPDPAALLrELARLLKPGGLLL 121
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 161-259 1.01e-10

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: 61.70  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQ-AGAQKVYAVEAStvAKYAEMLVRS---NGLSNKITVLSGRIEEVS---CPEKVDVIISEPmG 233
Cdd:COG4123    41 VLDLGTGTGVIALMLAQrSPGARITGVEIQ--PEAAELARRNvalNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP-P 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1207194531 234 YMLLNE------------RM-----LESFLH-AKHWLKPKGMMF 259
Cdd:COG4123   118 YFKAGSgrkspdearaiaRHedaltLEDLIRaAARLLKPGGRFA 161
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 150-228 3.23e-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: 56.82  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 150 LLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEASTVA-KYAEMLVRSNGLsnKITVLSGRIEEVSCPEKVDVII 228
Cdd:COG3897    63 LLDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEAlAALRLNAALNGV--AITTRLGDWRDPPAAGGFDLIL 140
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
155-228 2.37e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 2.37e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207194531 155 DFKDKVVLDVGCGTGILSFFAVQAGAQKVYAV----EASTVAKY-AEMlvrsNGLSNKITVLSGRieevscpEKVDVII 228
Cdd:PRK00517  117 VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVdidpQAVEAAREnAEL----NGVELNVYLPQGD-------LKADVIV 184
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 150-228 4.23e-08

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: 54.45  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 150 LLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEASTVAKYAEMLVRS-NGLSNKITVLSGRIEEVScPEKVDVII 228
Cdd:TIGR00406 152 WLEDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAElNQVSDRLQVKLIYLEQPI-EGKADVIV 230
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 157-228 5.32e-08

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: 54.19  E-value: 5.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207194531 157 KDKVVLDVGCGTGILSFFAVQAGAQKVYAVE----ASTVAKY-AEMlvrsNGLSNKITV-LSGRIEEvscpEKVDVII 228
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDidpvAVRAAKEnAEL----NGVEARLEVyLPGDLPK----EKADVVV 230
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 150-260 5.97e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 50.22  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 150 LLNEDDFKDKVVLDVGCGTGILSFFAVQAGAqKVYAVE-ASTVAKYAEMLVRSNGLSNKITVLSGRIEEVS-------Cp 221
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLLgrfdtvvC- 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207194531 222 ekVDVII---SEPMGYMLLN------ERMLESF------LHAKHWLkpkGMMFP 260
Cdd:PRK07580  134 --LDVLIhypQEDAARMLAHlasltrGSLIFTFapytplLALLHWI---GGLFP 182
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 161-256 6.47e-07

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 49.42  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQ-KVYAVEASTVA-KYAEMLVRSNGLSNKITVLSGRIEEVScPEKVDVIISEP------- 231
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNPEaRVTLVDVNARAvELARANAAANGLENVEVLWSDGLSGVP-DGSFDLILSNPpfhagra 131

                          90       100
                  ....*....|....*....|....*
gi 1207194531 232 MGYMLLnERMLEsflHAKHWLKPKG 256
Cdd:COG2813   132 VDKEVA-HALIA---DAARHLRPGG 152
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 157-259 9.01e-07

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 48.07  E-value: 9.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 157 KDKVVLDVGCGTGILSFFAVQAGAqKVYAVEAStvakyAEMLV----RSNGLSNKITVLSGRIEEVSCP-EKVDVIISeP 231
Cdd:COG2226    22 PGARVLDLGCGTGRLALALAERGA-RVTGVDIS-----PEMLElareRAAEAGLNVEFVVGDAEDLPFPdGSFDLVIS-S 94

                          90       100
                  ....*....|....*....|....*...
gi 1207194531 232 MGYMLLNERmLESFLHAKHWLKPKGMMF 259
Cdd:COG2226    95 FVLHHLPDP-ERALAEIARVLKPGGRLV 121
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
161-229 1.18e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 46.74  E-value: 1.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILS-FFAVQAGAQKVYAVEAStvakyAEMLVRSNGLSNKITVLSGRIEEVSCPEKVDVIIS 229
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVDLS-----PEMLARARARLPNVRFVVADLRDLDPPEPFDLVVS 69
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 145-258 2.29e-06

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: 47.58  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 145 YQKAM---LLNEDDFKDK-----VVLDVGCGTGIL---SFFAVQ-AGAQ-KVYAVEASTVA-KYAEMLVRSNGLSNKITV 210
Cdd:pfam05185  43 YERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEeTGTKvKIYAVEKNPNAyVTLQKRINFEKWGDKVTI 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1207194531 211 LSGRIEEVSCPEKVDVIISEPMGYMLLNERMLESFLHAKHWLKPKGMM 258
Cdd:pfam05185 123 ISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDGIS 170
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 161-256 4.86e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.22  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQKVYAVEASTVA-KYAEMLVRSNGLSNkITVLSGRIEEV--SCPEKVDVIISepMGYM-L 236
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGN-VEFLVADLAELdpLPAESFDLVVA--FGVLhH 106

                          90       100
                  ....*....|....*....|.
gi 1207194531 237 LNERMLESFLHAKH-WLKPKG 256
Cdd:COG0500   107 LPPEEREALLRELArALKPGG 127
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 155-285 6.28e-06

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: 46.61  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 155 DFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEASTVA-----KYAEMLvrsnGLSNKITVLSGRIEEV---SCPEKVDV 226
Cdd:COG0742    39 DIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAaavirKNLEKL----GLEDRARVIRGDALRFlkrLAGEPFDL 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207194531 227 IISEP---MGYMllnERMLEsFLHAKHWLKPKGMmfptqsdihlapftdehLYMEHHARSNF 285
Cdd:COG0742   115 VFLDPpyaKGLL---EKALE-LLAENGLLAPGGL-----------------IVVEHSKREEL 155
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 147-259 6.70e-06

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 46.04  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 147 KAMLLNEDDFKDKVVLDVGCGTGILSFFAVQAGAQ-KVYAVEASTVA-KYAEMLVRSNGLSNKITVLSGRIEEVScPEKV 224
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGLENGEVVASDVYSGVE-DGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207194531 225 DVIISEP-------MGYMLLnERMLEsflHAKHWLKPKGMMF 259
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNVA-QRFIA---DAKRHLRPGGELW 137
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 160-282 1.20e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 46.68  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 160 VVLDVGCGTGI--LSFFAVQAGAQkVYAVEASTVA-KYAEMLVRSNGLSNKITVLSGRI-EEVSCPEKVDVIIS------ 229
Cdd:COG2890   115 RVLDLGTGSGAiaLALAKERPDAR-VTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDGRFDLIVSnppyip 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207194531 230 --------------EPM--------GYMLLnERMLEsflHAKHWLKPKGmmfptqsdihlapftdeHLYMEHHAR 282
Cdd:COG2890   194 edeiallppevrdhEPRlaldggedGLDFY-RRIIA---QAPRLLKPGG-----------------WLLLEIGED 247
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 118-258 1.61e-05

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 46.49  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 118 RQRSEDSSALQYFQQQNMLQDFLRT---ATYQKA-MLLNE-----DDFKDKVVLDVGCGTG--ILSFFAVQAGAQKVYAV 186
Cdd:COG5459    32 RYRAERGSRRPYLADEADALAYAAYrlpATYAAVrAALAElaeagPDFAPLTVLDVGAGPGtaAWAAADAWPSLLDATLL 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207194531 187 EASTVA-KYAEMLVRSNGLSNKITV--LSGRIEEVSCPEKVDVIIsepMGYML--LNERMLESFLhAKHWLKPKGMM 258
Cdd:COG5459   112 ERSAAAlALGRRLARAAANPALETAewRLADLAAALPAPPADLVV---ASYVLneLADAARAALV-DRLWLAPDGAL 184
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 157-229 3.57e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 43.56  E-value: 3.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207194531 157 KDKVVLDVGCGTGILSFF-AVQAGAQ-KVYAVEASTVA-KYAEMLVRSNGLSNkITVLSGRIEEVSC---PEKVDVIIS 229
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFElAEELGPNaEVVGIDISEEAiEKARENAQKLGFDN-VEFEQGDIEELPElleDDKFDVVIS 80
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 162-259 4.66e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 41.88  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 162 LDVGCGTGILSFFAVQAGAQkVYAVEAStvakyAEML--VRSNGLSNKITVLSGRIEEVSCPEK-VDVIISepmGYMLLN 238
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDIS-----PEMLelAREKAPREGLTFVVGDAEDLPFPDNsFDLVLS---SEVLHH 71

                          90       100
                  ....*....|....*....|..
gi 1207194531 239 ERMLESFLH-AKHWLKPKGMMF 259
Cdd:pfam08241  72 VEDPERALReIARVLKPGGILI 93
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 144-263 1.05e-04

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 44.08  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 144 TYQKA--MLLNEDDFKDKVVLDVGCGTGILSFFAVQAGAqKVYA--VEASTVAKyAEMLVRSNGLSNKITV--------- 210
Cdd:PLN02585  129 TVEKVllWLAEDGSLAGVTVCDAGCGTGSLAIPLALEGA-IVSAsdISAAMVAE-AERRAKEALAALPPEVlpkfeandl 206

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207194531 211 --LSGRIEEVSCpekVDVIISEP---MGYM------LLNERMLESFLhAKHW----LKPKGMMFPTQS 263
Cdd:PLN02585  207 esLSGKYDTVTC---LDVLIHYPqdkADGMiahlasLAEKRLIISFA-PKTLyydiLKRIGELFPGPS 270
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 155-259 3.37e-04

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 41.68  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 155 DFKDKVVLDVGCGTG----ILSFFAVQAgaqKVYAVEAstVAKYA---EMLVRSNGLSNkITVLSGRIEEVSCPEKVDVI 227
Cdd:COG0357    65 PKEGARVLDVGSGAGfpgiPLAIARPDL---QVTLVDS--LGKKIaflREVVRELGLKN-VTVVHGRAEELAPREKFDVV 138

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1207194531 228 IS---EPMgymllnERMLEsflHAKHWLKPKGMMF 259
Cdd:COG0357   139 TAravAPL------PDLLE---LALPLLKPGGRLL 164
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 154-228 3.50e-04

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: 42.47  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 154 DDFKDKVVLDVGCGTGILSFFAVQAGAqKVYAVEASTVA-KYAEMLVRSNGLSNkITVLSGRIEEV----SCPEKVDVII 228
Cdd:COG2265   230 DLTGGERVLDLYCGVGTFALPLARRAK-KVIGVEIVPEAvEDARENARLNGLKN-VEFVAGDLEEVlpelLWGGRPDVVV 307
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
144-231 7.15e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 41.43  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 144 TYQKAMLLNEDdfKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEAS-TVAKYAEMLVRSNGLSN-KITVLSGRIEEV--S 219
Cdd:COG2521   121 ARRKVKLVGVR--RGDRVLDTCTGLGYTAIEALKRGAREVITVEKDpNVLELAELNPWSRELANeRIKIILGDASEVikT 198

                          90
                  ....*....|...
gi 1207194531 220 CPEK-VDVIISEP 231
Cdd:COG2521   199 FPDEsFDAIIHDP 211
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 155-256 7.21e-04

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


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 41.62  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 155 DFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEASTVAKYA-EMLVRSNGLSNKITVLSGRIEEVSCPEKVDVIISepMG 233
Cdd:pfam08003 113 PLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFLCQfEAVRKLLGNDQRAHLLPLGIEQLPALAAFDTVFS--MG 190

                          90       100
                  ....*....|....*....|...
gi 1207194531 234 YMLLNERMLESFLHAKHWLKPKG 256
Cdd:pfam08003 191 VLYHRRSPLDHLLQLKDQLVKGG 213
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
127-256 7.79e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 40.37  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 127 LQYFQQQNMLQDFLRTAtyqkamllneDDFKDKVVLDVGCGTGILSFFAVQAGaQKVYAVEAStvakyAEMLVRSNGLSN 206
Cdd:COG4976    26 LGYEAPALLAEELLARL----------PPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLS-----EEMLAKAREKGV 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207194531 207 KITVLSGRIEEVSCP-EKVDVIIS-EPMGYMllneRMLESFL-HAKHWLKPKG 256
Cdd:COG4976    90 YDRLLVADLADLAEPdGRFDLIVAaDVLTYL----GDLAAVFaGVARALKPGG 138
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 157-256 9.95e-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: 39.88  E-value: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 157 KDKVVLDVGCGTGilSF--FAVQAGAQKVYAVeasTVAKYAEMLVRSNglsNKITVLSGRIEEVSCPE--------KVDV 226
Cdd:pfam01728  21 PGKTVLDLGAAPG--GWsqVALQRGAGKVVGV---DLGPMQLWKPRND---PGVTFIQGDIRDPETLDlleellgrKVDL 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207194531 227 IIS------------EPMGYMLLNERMLEsflHAKHWLKPKG 256
Cdd:pfam01728  93 VLSdgspfisgnkvlDHLRSLDLVKAALE---VALELLRKGG 131
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 162-257 1.09e-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: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 162 LDVGCGTGILSFFAVQAGAQ-KVYAVEAST--VAKYAEMLVRSNGLSNKITVLSGRIEEVSCPEKVDVIIsepMGYMLLN 238
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISPaaLEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVV---ASNVLHH 77

                          90       100
                  ....*....|....*....|
gi 1207194531 239 ERMLESFL-HAKHWLKPKGM 257
Cdd:pfam08242  78 LADPRAVLrNIRRLLKPGGV 97
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 155-186 2.18e-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: 39.66  E-value: 2.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1207194531 155 DFKDKVVLDVGCGTGilSF--FAVQAGAQKVYAV 186
Cdd:COG1189    75 DVAGKVCLDIGASTG--GFtdCLLQRGAAKVYAV 106
PRK14967 PRK14967
putative methyltransferase; Provisional
 161-231 2.22e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 2.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQKVYAVEastVAKYAEMLVRSNGLSN--KITVLSGRIEEVSCPEKVDVIISEP 231
Cdd:PRK14967   40 VLDLCTGSGALAVAAAAAGAGSVTAVD---ISRRAVRSARLNALLAgvDVDVRRGDWARAVEFRPFDVVVSNP 109
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 135-227 2.64e-03

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 39.01  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 135 MLQDFLRTATYQKAMLlneddFKDKVVLDVGCGTGILSffaVQAG-----AQKVYAVEAStvaKYAEMLVRSN----GLS 205
Cdd:PRK00377   23 MTKEEIRALALSKLRL-----RKGDMILDIGCGTGSVT---VEASllvgeTGKVYAVDKD---EKAINLTRRNaekfGVL 91

                          90       100
                  ....*....|....*....|....
gi 1207194531 206 NKITVLSGRIEEV--SCPEKVDVI 227
Cdd:PRK00377   92 NNIVLIKGEAPEIlfTINEKFDRI 115
PRK14968 PRK14968
putative methyltransferase; Provisional
 140-265 3.93e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 140 LRTATYQKAmllnEDDF---------KDKVVLDVGCGTGILSFFAVQAGAqKVYAVEASTVA-KYAEMLVRSNGLSN-KI 208
Cdd:PRK14968    1 LNDEVYEPA----EDSFllaenavdkKGDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAvECAKCNAKLNNIRNnGV 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207194531 209 TVLSGRIeeVSC--PEKVDVII--------------SEPMGYMLL----NERMLESFL-HAKHWLKPKGMMFPTQSDI 265
Cdd:PRK14968   76 EVIRSDL--FEPfrGDKFDVILfnppylpteeeeewDDWLNYALSggkdGREVIDRFLdEVGRYLKPGGRILLLQSSL 151
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
154-233 4.30e-03

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 39.07  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 154 DDFKDKVVLDVGCGTGILSFFAVQAGAQKVYAVEASTVAKYAEMLVRS-NGLSNKITVLSGRIEEVSCPEKVDVIISepM 232
Cdd:PRK15068  119 SPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSQLFLCQFEAVRKlLGNDQRAHLLPLGIEQLPALKAFDTVFS--M 196


                  .
gi 1207194531 233 G 233
Cdd:PRK15068  197 G 197
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 160-206 5.23e-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: 37.29  E-value: 5.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1207194531 160 VVLDVGCGTGILSFFAVQAGAQ-KVYAVEAST-VAKYAEMLVRSNGLSN 206
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNLPN 49
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 124-257 6.91e-03

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.04  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 124 SSALQYFQQQNMLQDFLrtATYQKAMLLNEDDFKDKVVLDVGCGTGILSF-FAVQAGAQKVYAVEAStvakyAEMLVRS- 201
Cdd:TIGR02072   3 NKAAKTYDRHAKIQREM--AKRLLALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDIS-----AGMLAQAk 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207194531 202 NGLSNKITVLSGRIEEVS-CPEKVDVIISEpMGYMLLNErmLESFL-HAKHWLKPKGM 257
Cdd:TIGR02072  76 TKLSENVQFICGDAEKLPlEDSSFDLIVSN-LALQWCDD--LSQALsELARVLKPGGL 130
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 150-231 8.47e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 37.83  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 150 LLNEDDFKDKVVLDVGCGTG-----ILSFFAvQAgaqKVYAVEASTVA-KYAemlvRSN---GLSNKITVLSGRIEEVSC 220
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGaialaLAKERP-DA---EVTAVDISPEAlAVA----RRNakhGLGARVEFLQGDWFEPLP 172

                          90
                  ....*....|.
gi 1207194531 221 PEKVDVIISEP 231
Cdd:PRK09328  173 GGRFDLIVSNP 183
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 161-258 9.42e-03

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 37.69  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207194531 161 VLDVGCGTGILSFFAVQAGAQKVYAVEAST-VAKYAEMLVRSNGLSNKITVLSGRIEEVscPEKVDVIIS----EPMGYm 235
Cdd:pfam02353  65 LLDIGCGWGGLMRRAAERYDVNVVGLTLSKnQYKLARKRVAAEGLARKVEVLLQDYRDF--DEPFDRIVSvgmfEHVGH- 141

                          90       100
                  ....*....|....*....|...
gi 1207194531 236 llnERMLESFLHAKHWLKPKGMM 258
Cdd:pfam02353 142 ---ENYDTFFKKLYNLLPPGGLM 161
 
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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