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Conserved domains on  [gi|189409145|ref|NP_694781|]
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histone-arginine methyltransferase CARM1 isoform 2 [Mus musculus]

Protein Classification

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 ...
 35-139 1.15e-70

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: 222.41  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145   35 GARLLTIGDANGEIQRHAEQQALRLEVRAGPDAAGIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLIQFAT 114
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 189409145  115 PHDFCSFYNILKTCRGHTLERSVFS 139
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
160-347 4.38e-41

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: 148.65  E-value: 4.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 160 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 238
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 239 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 317
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 189409145 318 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 347
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 ...
 35-139 1.15e-70

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: 222.41  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145   35 GARLLTIGDANGEIQRHAEQQALRLEVRAGPDAAGIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLIQFAT 114
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 189409145  115 PHDFCSFYNILKTCRGHTLERSVFS 139
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 31-140 2.68e-61

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: 198.01  E-value: 2.68e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  31 SVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDaagIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLI 110
Cdd:cd13330    1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSV---LVLSTNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 189409145 111 QFATPHDFCSFYNILKTCRGHTLERSVFSE 140
Cdd:cd13330   78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
160-347 4.38e-41

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 148.65  E-value: 4.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 160 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 238
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 239 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 317
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 189409145 318 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 347
Cdd:COG4076  163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 189-284 4.65e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 4.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  189 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 266
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 189409145  267 ERMLESYLH-AKKYLKPSG 284
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 189-284 5.24e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 59.75  E-value: 5.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 189 VLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 266
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|
gi 189409145 267 --ERMLESylhAKKYLKPSG 284
Cdd:cd02440   82 dlARFLEE---ARRLLKPGG 98
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
170-214 2.85e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 2.85e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189409145 170 TGTYQ------RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV 214
Cdd:PRK00517 100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 183-284 2.77e-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: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  183 DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEVSLPeqVDIIISEpm 260
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 189409145  261 gymLFNERMLESYLHAKKYLKPSG 284
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 35-139 1.15e-70

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: 222.41  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145   35 GARLLTIGDANGEIQRHAEQQALRLEVRAGPDAAGIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLIQFAT 114
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 189409145  115 PHDFCSFYNILKTCRGHTLERSVFS 139
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 31-140 2.68e-61

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: 198.01  E-value: 2.68e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  31 SVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDaagIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLI 110
Cdd:cd13330    1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSV---LVLSTNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 189409145 111 QFATPHDFCSFYNILKTCRGHTLERSVFSE 140
Cdd:cd13330   78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
160-347 4.38e-41

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 148.65  E-value: 4.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 160 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 238
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 239 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 317
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 189409145 318 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 347
Cdd:COG4076  163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
175-256 6.79e-12

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 66.35  E-value: 6.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 175 RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIY-------AVEAStmAQHAEVlvksNNLTDRIVVIPGKVEEvs 247
Cdd:COG2264  140 EALEKL--LKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA--RENAEL----NGVEDRIEVVLGDLLE-- 209


                 ....*....
gi 189409145 248 lPEQVDIII 256
Cdd:COG2264  210 -DGPYDLVV 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 189-284 4.65e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 4.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  189 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 266
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 189409145  267 ERMLESYLH-AKKYLKPSG 284
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 189-284 5.24e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 59.75  E-value: 5.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 189 VLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 266
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|
gi 189409145 267 --ERMLESylhAKKYLKPSG 284
Cdd:cd02440   82 dlARFLEE---ARRLLKPGG 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 189-287 2.43e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 59.17  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 189 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMgYMLFNE 267
Cdd:COG2230   55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                         90       100
                 ....*....|....*....|.
gi 189409145 268 RMLESYL-HAKKYLKPSGNMF 287
Cdd:COG2230  134 ENYPAYFaKVARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 164-287 9.13e-10

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 56.56  E-value: 9.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 164 MQDYVRTGTYQRAILQ--NHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLTdrivVIP 240
Cdd:COG2227    1 MSDPDARDFWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISpEALEIARERAAELNVD----FVQ 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 189409145 241 GKVEEVSLP-EQVDIIIS-EPMGYMLFNERMLEsylHAKKYLKPSGNMF 287
Cdd:COG2227   76 GDLEDLPLEdGSFDLVICsEVLEHLPDPAALLR---ELARLLKPGGLLL 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
176-259 1.01e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 58.38  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 176 AILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAStmAQHAEVLvKSN--NLTDRIVVIPGKVEEVSLPEQVD 253
Cdd:COG2263   38 AYLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIA-RENaeRLGVRVDFIRADVTRIPLGGSVD 112


                 ....*.
gi 189409145 254 IIISEP 259
Cdd:COG2263  113 TVVMNP 118
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 175-256 1.17e-08

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


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 55.66  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 175 RAILQnHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHA-EVLVKSNNLTdrIVVIPGKVEEVSLPEQVD 253
Cdd:COG3897   61 RYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAAlRLNAALNGVA--ITTRLGDWRDPPAAGGFD 137


                 ...
gi 189409145 254 III 256
Cdd:COG3897  138 LIL 140
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 189-259 1.40e-08

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 55.54  E-value: 1.40e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189409145 189 VLDVGCGSGILSFFAAQ-AGARKIYAVE----ASTMAQHAevlVKSNNLTDRIVVIPGKVEEVS---LPEQVDIIISEP 259
Cdd:COG4123   41 VLDLGTGTGVIALMLAQrSPGARITGVEiqpeAAELARRN---VALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP 116
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 185-284 2.12e-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: 55.73  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  185 KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEvslpEQVDI----IISE 258
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAvRAAKENAELNGVEARLEVYlPGDLPK----EKADVvvanILAD 236

                          90       100
                  ....*....|....*....|....*.
gi 189409145  259 PMgymlfnERMLEsylHAKKYLKPSG 284
Cdd:pfam06325 237 PL------IELAP---DIYALVKPGG 253
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
170-214 2.85e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 2.85e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189409145 170 TGTYQ------RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV 214
Cdd:PRK00517 100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 175-287 3.09e-08

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 53.36  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  175 RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGAR-KIYAVEASTMA-QHAEVLVKSNNLtDRIVVIPGKVEEVSLPEQV 252
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 189409145  253 DIIISEP-------MGYMLfNERMLEsylHAKKYLKPSGNMF 287
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 175-284 2.44e-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: 50.38  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 175 RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQV 252
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISpEMLELARERAAEAGL--NVEFVVGDAEDLPFPdGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 189409145 253 DIIISePMGYMLFN--ERMLEsylHAKKYLKPSG 284
Cdd:COG2226   89 DLVIS-SFVLHHLPdpERALA---EIARVLKPGG 118
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 183-284 2.77e-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: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  183 DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEVSLPeqVDIIISEpm 260
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 189409145  261 gymLFNERMLESYLHAKKYLKPSG 284
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 165-284 4.87e-07

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


Pssm-ID: 428356  Cd Length: 171  Bit Score: 49.90  E-value: 4.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  165 QDYVRTGTYQRAI---LQNHTDFKDK-----IVLDVGCGSGIL---SFFAAQAGAR--KIYAVEASTMA----QHaevLV 227
Cdd:pfam05185  35 KDPVKYDLYERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEETGTkvKIYAVEKNPNAyvtlQK---RI 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 189409145  228 KSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG 284
Cdd:pfam05185 112 NFEKWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 190-284 5.70e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.96  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  190 LDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLTdrivVIPGKVEEVSLP-EQVDIIISEpmgYMLFNE 267
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISpEMLELAREKAPREGLT----FVVGDAEDLPFPdNSFDLVLSS---EVLHHV 72

                          90
                  ....*....|....*...
gi 189409145  268 RMLESYLH-AKKYLKPSG 284
Cdd:pfam08241  73 EDPERALReIARVLKPGG 90
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
189-257 5.88e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 45.20  E-value: 5.88e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 189 VLDVGCGSGILS-FFAAQAGARKIYAVEAStmaqhAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIIS 257
Cdd:COG4106    5 VLDLGCGTGRLTaLLAERFPGARVTGVDLS-----PEMLARARARLPNVRFVVADLRDLDPPEPFDLVVS 69
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 166-284 3.30e-05

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 44.80  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 166 DYVRTGTyqRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGA-RKIYAVEASTMA-QHAEVLVKSNNLTDrIVVIPGKV 243
Cdd:COG2813   32 DRLDIGT--RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGLEN-VEVLWSDG 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189409145 244 EEVSLPEQVDIIISEP-----------MGYMLFNErmlesylhAKKYLKPSG 284
Cdd:COG2813  109 LSGVPDGSFDLILSNPpfhagravdkeVAHALIAD--------AARHLRPGG 152
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 177-255 4.76e-05

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 44.30  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 177 ILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAStmAQHAEVLvKSN----NLTDRIVVIPGKVEEV---SLP 249
Cdd:COG0742   35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEKD--RKAAAVI-RKNleklGLEDRARVIRGDALRFlkrLAG 109


                 ....*.
gi 189409145 250 EQVDII 255
Cdd:COG0742  110 EPFDLV 115
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 178-247 4.90e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 44.83  E-value: 4.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189409145 178 LQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVE-ASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVS 247
Cdd:PRK07580  56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL 125
PRK14968 PRK14968
putative methyltransferase; Provisional
 170-313 1.93e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.58  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 170 TGTYQRA-----ILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKI------YAVEAstmaqhAEVLVKSNNLTDR-IV 237
Cdd:PRK14968   3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC------AKCNAKLNNIRNNgVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 238 VIPGK-VEEVS-------------LPEQVDIIISEPMGYMLF----NERMLESYL-HAKKYLKPSGNMFPTIGDvhlapF 298
Cdd:PRK14968  77 VIRSDlFEPFRgdkfdvilfnppyLPTEEEEEWDDWLNYALSggkdGREVIDRFLdEVGRYLKPGGRILLLQSS-----L 151

                        170
                 ....*....|....*
gi 189409145 299 TDEQLYMEQFTKANF 313
Cdd:PRK14968 152 TGEDEVLEYLEKLGF 166
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
177-257 2.19e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 43.35  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 177 ILQNHTDFKDKIVLDVGCGSGILSFFAAQAgARKIYAVEA-STMAQHA-EVLVKSNNLTdrivVIPGKVEEVSLPEqVDI 254
Cdd:PRK14896  21 IVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLrDDEIAAGNVE----IIEGDALKVDLPE-FNK 94


                 ...
gi 189409145 255 IIS 257
Cdd:PRK14896  95 VVS 97
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
166-257 2.79e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.91  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 166 DYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAevlvKSNNLTDRIVVipGKVE 244
Cdd:COG4976   27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSeEMLAKA----REKGVYDRLLV--ADLA 99

                         90
                 ....*....|....
gi 189409145 245 EVS-LPEQVDIIIS 257
Cdd:COG4976  100 DLAePDGRFDLIVA 113
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 175-259 3.64e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.83  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 175 RAILQNHTDFKDKIVLDVGCGSGI--LSFFAAQAGARkIYAVEASTMA-QHAEVLVKSNNLTDRIVVIPGKV-EEVSLPE 250
Cdd:COG2890  102 ELALALLPAGAPPRVLDLGTGSGAiaLALAKERPDAR-VTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDG 180


                 ....*....
gi 189409145 251 QVDIIISEP 259
Cdd:COG2890  181 RFDLIVSNP 189
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
173-261 6.53e-04

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.15  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 173 YQRaiLQNHT-DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS--TMAQ-HA-EVLVKSNNltdRIVVIPGKVEEVS 247
Cdd:PRK15068 111 WDR--VLPHLsPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSqlFLCQfEAvRKLLGNDQ---RAHLLPLGIEQLP 185

                         90
                 ....*....|....
gi 189409145 248 LPEQVDIIISepMG 261
Cdd:PRK15068 186 ALKAFDTVFS--MG 197
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 176-257 1.13e-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: 40.73  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  176 AILQNHTDFKDKIVLDVGCGSGILSF-FAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTdrivvIPGKVEEVSLPE-QV 252
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISaGMLAQAKTKLSENVQF-----ICGDAEKLPLEDsSF 99


                  ....*
gi 189409145  253 DIIIS 257
Cdd:TIGR02072 100 DLIVS 104
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 188-232 1.44e-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: 39.22  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 189409145  188 IVLDVGCGSGILSFFAAQAGAR-KIYAVEAST-MAQHAEVLVKSNNL 232
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNL 47
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 173-318 1.76e-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: 40.85  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  173 YQRaILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTM--AQHaEVLVKSNNLTDRIVVIPGKVEEVSLPE 250
Cdd:pfam08003 104 WDR-VLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELflCQF-EAVRKLLGNDQRAHLLPLGIEQLPALA 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189409145  251 QVDIIISepMGYMLFNERMLESYLHAKKYLKPSGNM-FPTI---GDVHLAPFTDEQlYMEQftkANFWYQPS 318
Cdd:pfam08003 182 AFDTVFS--MGVLYHRRSPLDHLLQLKDQLVKGGELvLETLvidGDENTVLVPGDR-YAQM---RNVYFIPS 247
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 175-327 1.79e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  175 RAILQNHTDFKdkiVLDVGCGSGILSFFAAQAGAR-KIYAVEASTMA-QHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQV 252
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145  253 DIIISEPmGYMLFNE--RMLESYLH----------------------AKKYLKPSGNMFPTIGDVHLApftdeqLYMEQF 308
Cdd:TIGR00536 184 DIIVSNP-PYIDEEDlaDLPNVVRFepllalvggddglnilrqiielAPDYLKPNGFLVCEIGNWQQK------SLKELL 256

                         170
                  ....*....|....*....
gi 189409145  309 TKANFWYQPSFHGvDLSAL 327
Cdd:TIGR00536 257 RIKFTWYDVENGR-DLNGK 274
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 185-256 2.61e-03

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 40.54  E-value: 2.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189409145 185 KDKIVLDVGCGSGILSFFAAQAgARKIYAVEAS-TMAQHAEVLVKSNNLtDRIVVIPGKVEEVsLPEQV-----DIII 256
Cdd:COG2265  233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDARENARLNGL-KNVEFVAGDLEEV-LPELLwggrpDVVV 307
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
187-259 3.20e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 39.89  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 187 KIVLDVGCGSGILSFFAAQAGARKIYAVEAStmaqhAEVLVK------SNNLTD-RIVVIPGKVEEV--SLP-EQVDIII 256
Cdd:COG2521  134 DRVLDTCTGLGYTAIEALKRGAREVITVEKD-----PNVLELaelnpwSRELANeRIKIILGDASEVikTFPdESFDAII 208


                 ...
gi 189409145 257 SEP 259
Cdd:COG2521  209 HDP 211
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 189-284 4.56e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.74  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 189 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTD-RIVVIPGKVEEVSLPEQVDIIISepMGYM-LF 265
Cdd:COG0500   30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVA--FGVLhHL 107

                         90       100
                 ....*....|....*....|
gi 189409145 266 NERMLESYLH-AKKYLKPSG 284
Cdd:COG0500  108 PPEEREALLReLARALKPGG 127
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
182-284 7.09e-03

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 38.78  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409145 182 TDFKDKIVLDVGCGSGILSFFAAQAGARKI--YAVEA-STMAQhaeVLVKSNNLTDR-IVVIPGKVEEVSLPEQVDIIIS 257
Cdd:COG0827  112 TKKEGLRILDPAVGTGNLLTTVLNQLKKKVnaYGVEVdDLLIR---LAAVLANLQGHpVELFHQDALQPLLIDPVDVVIS 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 189409145 258 E-PMGY-----------MLFNERMleSYLH------AKKYLKPSG 284
Cdd:COG0827  189 DlPVGYypnderakrfkLKADEGH--SYAHhlfieqSLNYLKPGG 231
 
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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