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Conserved domains on  [gi|1721884171|ref|XP_030200464|]
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histone-arginine methyltransferase CARM1 isoform X1 [Gadus morhua]

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 ...
 8-112 2.77e-72

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


:

Pssm-ID: 402914  Cd Length: 105  Bit Score: 226.65  E-value: 2.77e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171   8 GVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLSNGEDTCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFAS 87
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1721884171  88 PADFSSFYNLLKNCRGHSGERSVFS 112
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
133-320 6.18e-43

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: 153.27  E-value: 6.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 133 QQNMMQDYVRTGTYQRAIlqNHVDFKDKVILDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGDRVVV 211
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 212 IPGKVEEVTLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGKMFPTLGDVHLAPftdeqlyMEQFTKANFWYQP 290
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1721884171 291 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 320
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 ...
 8-112 2.77e-72

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


Pssm-ID: 402914  Cd Length: 105  Bit Score: 226.65  E-value: 2.77e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171   8 GVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLSNGEDTCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFAS 87
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1721884171  88 PADFSSFYNLLKNCRGHSGERSVFS 112
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 4-113 3.87e-60

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


Pssm-ID: 241484  Cd Length: 107  Bit Score: 194.93  E-value: 3.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171   4 SVFPGVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLsngEDTCVFKCSVSRETECSRVGKQSFIITLGCNSVLL 83
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVLSTN---EDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1721884171  84 QFASPADFSSFYNLLKNCRGHSGERSVFSD 113
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
133-320 6.18e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 153.27  E-value: 6.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 133 QQNMMQDYVRTGTYQRAIlqNHVDFKDKVILDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGDRVVV 211
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 212 IPGKVEEVTLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGKMFPTLGDVHLAPftdeqlyMEQFTKANFWYQP 290
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1721884171 291 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 320
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 162-263 1.76e-13

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 66.68  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 162 ILDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNRLGDRVVVIPGKVEEVTL--PEQVDIIISEPMGYMLFN 239
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1721884171 240 --ERMLESYLHAkkfLKPNGKMFPTL 263
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 162-257 5.03e-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: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 162 ILDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEvlVNSNRLGDRVVVIPGKVEEVTLP-EQVDIIISePMGYMLFN 239
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERAR--ERAAEAGLNVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1721884171 240 ERMLESYLH-AKKFLKPNG 257
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
143-187 2.62e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.16  E-value: 2.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1721884171 143 TGTYQ------RAILQnhVDFKDKVILDVGCGSGILSFFAAQAGARKVYAV 187
Cdd:PRK00517  100 TGTHPttrlclEALEK--LVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 156-257 1.34e-07

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


Pssm-ID: 273061  Cd Length: 288  Bit Score: 53.30  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 156 DFKDKVILDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNRLGDRVVVI-PGKVEEVTLPeqVDIIISEpm 233
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 1721884171 234 gymLFNERMLESYLHAKKFLKPNG 257
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 8-112 2.77e-72

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


Pssm-ID: 402914  Cd Length: 105  Bit Score: 226.65  E-value: 2.77e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171   8 GVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLSNGEDTCVFKCSVSRETECSRVGKQSFIITLGCNSVLLQFAS 87
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1721884171  88 PADFSSFYNLLKNCRGHSGERSVFS 112
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 4-113 3.87e-60

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


Pssm-ID: 241484  Cd Length: 107  Bit Score: 194.93  E-value: 3.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171   4 SVFPGVRLLSIGDANGDIQRHSEQQPLRLEVKTTQDAALINLsngEDTCVFKCSVSRETECSRVGKQSFIITLGCNSVLL 83
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVLSTN---EDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1721884171  84 QFASPADFSSFYNLLKNCRGHSGERSVFSD 113
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
133-320 6.18e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 153.27  E-value: 6.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 133 QQNMMQDYVRTGTYQRAIlqNHVDFKDKVILDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGDRVVV 211
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 212 IPGKVEEVTLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGKMFPTLGDVHLAPftdeqlyMEQFTKANFWYQP 290
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1721884171 291 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 320
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 162-263 1.76e-13

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 66.68  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 162 ILDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNRLGDRVVVIPGKVEEVTL--PEQVDIIISEPMGYMLFN 239
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1721884171 240 --ERMLESYLHAkkfLKPNGKMFPTL 263
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
149-232 2.88e-12

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 65.70  E-value: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 149 AILQNhvDFKDKVILDVGCGSGILSFFAAQAGARKVYAVEAStmAQHAEVLV-NSNRLGDRVVVIPGKVEEVTLPEQVDI 227
Cdd:COG2263    38 AYLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIAReNAERLGVRVDFIRADVTRIPLGGSVDT 113


                  ....*
gi 1721884171 228 IISEP 232
Cdd:COG2263   114 VVMNP 118
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
148-257 1.49e-11

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 65.19  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 148 RAILQnhVDFKDKVILDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNRLGDRVVVIPGKVEEvt 220
Cdd:COG2264   140 EALEK--LLKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA--RENAEL----NGVEDRIEVVLGDLLE-- 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1721884171 221 lPEQVDI----IISEPmgymLfnERMLESYlhaKKFLKPNG 257
Cdd:COG2264   210 -DGPYDLvvanILANP----L--IELAPDL---AALLKPGG 240
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 137-260 1.74e-11

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 61.57  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 137 MQDYVRTGTYQRAI---LQNHVDfKDKVILDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNRLGDRVVVI 212
Cdd:COG2227     1 MSDPDARDFWDRRLaalLARLLP-AGGRVLDVGCGTGRLALALARRGAD-VTGVDISpEALEIAR----ERAAELNVDFV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1721884171 213 PGKVEEVTLP-EQVDIIIS-EPMGYMLFNERMLEsylHAKKFLKPNGKMF 260
Cdd:COG2227    75 QGDLEDLPLEdGSFDLVICsEVLEHLPDPAALLR---ELARLLKPGGLLL 121
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 162-260 1.81e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 62.64  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 162 ILDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGDRVVVIPGKVEEVTLPEQVDIIISEPMgYMLFNE 240
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                          90       100
                  ....*....|....*....|.
gi 1721884171 241 RMLESYL-HAKKFLKPNGKMF 260
Cdd:COG2230   134 ENYPAYFaKVARLLKPGGRLL 154
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 162-257 5.03e-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: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 162 ILDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEvlVNSNRLGDRVVVIPGKVEEVTLP-EQVDIIISePMGYMLFN 239
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERAR--ERAAEAGLNVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1721884171 240 ERMLESYLH-AKKFLKPNG 257
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 138-257 6.17e-10

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: 58.37  E-value: 6.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 138 QDYVRTGTYQRAI---LQNHVDFKDK-----VILDVGCGSGIL---SFFAAQAGAR--KVYAVEASTMA----QHaevLV 200
Cdd:pfam05185  35 KDPVKYDLYERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEETGTkvKIYAVEKNPNAyvtlQK---RI 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1721884171 201 NSNRLGDRVVVIPGKVEEVTLPEQVDIIISEPMGYMLFNERMLESYLHAKKFLKPNG 257
Cdd:pfam05185 112 NFEKWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 148-260 3.04e-09

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 56.44  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 148 RAILQNHVDFKDKVILDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNRLgDRVVVIPGKVEEVTLPEQV 225
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1721884171 226 DIIISEP-------MGYMLfNERMLEsylHAKKFLKPNGKMF 260
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 148-260 2.59e-08

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 53.07  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 148 RAILQNHVDFKDKVILDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVnsNRLGDRVVVIPGKVEEVTLP-EQV 225
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISpEMLELARERA--AEAGLNVEFVVGDAEDLPFPdGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1721884171 226 DIIISePMGYMLFN--ERMLEsylHAKKFLKPNGKMF 260
Cdd:COG2226    89 DLVIS-SFVLHHLPdpERALA---EIARVLKPGGRLV 121
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
143-187 2.62e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.16  E-value: 2.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1721884171 143 TGTYQ------RAILQnhVDFKDKVILDVGCGSGILSFFAAQAGARKVYAV 187
Cdd:PRK00517  100 TGTHPttrlclEALEK--LVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 162-260 5.61e-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: 54.00  E-value: 5.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 162 ILDVGCGSGILSFFAAQ-AGARKVYAVE----ASTMAQHAevlVNSNRLGDRVVVIPGKVEEVT---LPEQVDIIISEPm 233
Cdd:COG4123    41 VLDLGTGTGVIALMLAQrSPGARITGVEiqpeAAELARRN---VALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP- 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1721884171 234 GYMLFNE------------RM-----LESYLH-AKKFLKPNGKMF 260
Cdd:COG4123   117 PYFKAGSgrkspdearaiaRHedaltLEDLIRaAARLLKPGGRFA 161
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 156-257 1.34e-07

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


Pssm-ID: 273061  Cd Length: 288  Bit Score: 53.30  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 156 DFKDKVILDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNRLGDRVVVI-PGKVEEVTLPeqVDIIISEpm 233
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 1721884171 234 gymLFNERMLESYLHAKKFLKPNG 257
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 163-260 5.33e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 48.04  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 163 LDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNRLGDRVvvipGKVEEVTLP-EQVDIIISEpmgYMLFNE 240
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISpEMLELAREKAPREGLTFVV----GDAEDLPFPdNSFDLVLSS---EVLHHV 72

                          90       100
                  ....*....|....*....|.
gi 1721884171 241 RMLESYLH-AKKFLKPNGKMF 260
Cdd:pfam08241  73 EDPERALReIARVLKPGGILI 93
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
162-230 5.74e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.90  E-value: 5.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721884171 162 ILDVGCGSGILS-FFAAQAGARKVYAVEAS-TMAQHAevlvnsNRLGDRVVVIPGKVEEVTLPEQVDIIIS 230
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVDLSpEMLARA------RARLPNVRFVVADLRDLDPPEPFDLVVS 69
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 158-257 2.13e-06

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: 49.57  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 158 KDKVILDVGCGSGILSFFAAQAGARKVYAVE----ASTMAQH-AEVlvnsNRLGDRVVVI-PGKVEEvtlpEQVDI---- 227
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDidpvAVRAAKEnAEL----NGVEARLEVYlPGDLPK----EKADVvvan 232

                          90       100       110
                  ....*....|....*....|....*....|
gi 1721884171 228 IISEPMgymlfnERMLEsylHAKKFLKPNG 257
Cdd:pfam06325 233 ILADPL------IELAP---DIYALVKPGG 253
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 151-203 9.74e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 47.14  E-value: 9.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1721884171 151 LQNHVDFKDKVILDVGCGSGILSFFAAQAGARkVYAVE-ASTMAQHA-----EVLVNSN 203
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEArerapEAGLAGN 113
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 139-260 2.03e-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: 45.57  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 139 DYVRTGTyqrAILQNHVDFKDK-VILDVGCGSGILSFFAAQAGA-RKVYAVEASTMA-QHAEVLVNSNRLgDRVVVIPGK 215
Cdd:COG2813    32 DRLDIGT---RLLLEHLPEPLGgRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGL-ENVEVLWSD 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1721884171 216 VEEVTLPEQVDIIISEP-----------MGYMLFNErmlesylhAKKFLKPNGKMF 260
Cdd:COG2813   108 GLSGVPDGSFDLILSNPpfhagravdkeVAHALIAD--------AARHLRPGGELW 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
139-230 5.27e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.22  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 139 DYVRTGTYQRAILQNHVDFKDKVILDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNRLGDRVVVipGKVE 217
Cdd:COG4976    27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSeEMLAKAR----EKGVYDRLLV--ADLA 99

                          90
                  ....*....|....
gi 1721884171 218 EVT-LPEQVDIIIS 230
Cdd:COG4976   100 DLAePDGRFDLIVA 113
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
160-260 1.11e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.13  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 160 KVILDVGCGSGILSFFAAQAGARKVYAVEAStmaqhAEVL----VN--SNRL-GDRVVVIPGKVEEV--TLP-EQVDIII 229
Cdd:COG2521   134 DRVLDTCTGLGYTAIEALKRGAREVITVEKD-----PNVLelaeLNpwSRELaNERIKIILGDASEVikTFPdESFDAII 208

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1721884171 230 SEPmgyMLFNermLESYLHAKKF-------LKPNGKMF 260
Cdd:COG2521   209 HDP---PRFS---LAGELYSLEFyrelyrvLKPGGRLF 240
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
156-230 1.56e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 43.74  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721884171 156 DFKDKVILDVGCGSGILSFFAAQAgARKVYAVEA-STMAQHAEVLVNSNrlgDRVVVIPGKVEEVTLPEqVDIIIS 230
Cdd:PRK14896   27 DTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIAA---GNVEIIEGDALKVDLPE-FNKVVS 97
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 156-291 2.29e-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: 43.55  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 156 DFKDKVILDVGCGSGILSFFAAQAGARKVYAVEASTMA----QHAEVLVNSNRlgdRVVVIPGKVEEVTLPEQVDIIISe 231
Cdd:pfam08003 113 PLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFlcqfEAVRKLLGNDQ---RAHLLPLGIEQLPALAAFDTVFS- 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721884171 232 pMGYMLFNERMLESYLHAKKFLKPNGKM-FPTL---GDVHLAPFTDEQlYMEQftkANFWYQPS 291
Cdd:pfam08003 189 -MGVLYHRRSPLDHLLQLKDQLVKGGELvLETLvidGDENTVLVPGDR-YAQM---RNVYFIPS 247
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 148-232 2.52e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 43.21  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 148 RAILQNHVDFKDKVILDVGCGSGI--LSFFAAQAGARkVYAVEAST----MAQHaevlvNSNRLG--DRVVVIPGKV-EE 218
Cdd:COG2890   102 ELALALLPAGAPPRVLDLGTGSGAiaLALAKERPDAR-VTAVDISPdalaVARR-----NAERLGleDRVRFLQGDLfEP 175

                          90
                  ....*....|....
gi 1721884171 219 VTLPEQVDIIISEP 232
Cdd:COG2890   176 LPGDGRFDLIVSNP 189
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 162-257 3.23e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.21  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 162 ILDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNRLGD-RVVVIPGKVEEVTLPEQVDIIISepMGYM-LF 238
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVA--FGVLhHL 107

                          90       100
                  ....*....|....*....|
gi 1721884171 239 NERMLESYLH-AKKFLKPNG 257
Cdd:COG0500   108 PPEEREALLReLARALKPGG 127
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
150-260 3.41e-04

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 41.84  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 150 ILQNHVDFKdkVILDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAeVLVNSNRLGDRVVVIPGKVEEVTL-----PEQ 224
Cdd:pfam03602  35 WLAPYIEGA--RVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQI-LKENLQLLGLPGAVLVMDALLALLrlagkGPV 111

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1721884171 225 VDIIISEPmGYM--LFNERMleSYLHAKKFLKPNGKMF 260
Cdd:pfam03602 112 FDIVFLDP-PYAkgLIEEVL--DLLAEKGWLKPNALIY 146
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 158-259 5.01e-04

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


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 40.39  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 158 KDKVILDVGCGSGILSFFAA-QAGARKVYAVEAStmAQHAEVL-VNSNRLG-DRVVVIPGKVEEVT--LPEQVDIIISEP 232
Cdd:TIGR02469  19 PGDVLWDIGAGTGSVTIEAArLVPNGRVYAIERN--PEALDLIeRNLRRFGvSNIVIVEGDAPEAPeaLLPDPDAVFVGG 96

                          90       100
                  ....*....|....*....|....*...
gi 1721884171 233 MGymlfneRMLESYLHA-KKFLKPNGKM 259
Cdd:TIGR02469  97 SG------GLLQEILEAvERRLRPGGRI 118
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 158-260 8.26e-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: 40.65  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 158 KDKVILDVGCGSGilSF--FAAQAGARKVYAVEASTMAqhaevlVNSNRLGDRVVVIPG---------KVEEvTLPEQVD 226
Cdd:pfam01728  21 PGKTVLDLGAAPG--GWsqVALQRGAGKVVGVDLGPMQ------LWKPRNDPGVTFIQGdirdpetldLLEE-LLGRKVD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1721884171 227 III---SEPMGYMLFNERMLESYLH------AKKFLKPNG----KMF 260
Cdd:pfam01728  92 LVLsdgSPFISGNKVLDHLRSLDLVkaalevALELLRKGGnfvcKVF 138
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 163-258 8.77e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.89  E-value: 8.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 163 LDVGCGSGILSFFAAQAGAR-KVYAVEAS-TMAQHAEVLVNSNRLGDRVVV-IPGKVEEVTLPEQVDIIISEpmGYMLFN 239
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISpAALEAARERLAALGLLNAVRVeLFQLDLGELDPGSFDVVVAS--NVLHHL 78

                          90
                  ....*....|....*....
gi 1721884171 240 ERMLESYLHAKKFLKPNGK 258
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGV 97
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
146-234 9.18e-04

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 41.77  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 146 YQRaiLQNHV-DFKDKVILDVGCGSGILSFFAAQAGARKVYAVEAS--TMAQ-HA-EVLVNSNRlgdRVVVIPGKVEEVT 220
Cdd:PRK15068  111 WDR--VLPHLsPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSqlFLCQfEAvRKLLGNDQ---RAHLLPLGIEQLP 185

                          90
                  ....*....|....
gi 1721884171 221 LPEQVDIIISepMG 234
Cdd:PRK15068  186 ALKAFDTVFS--MG 197
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 158-229 1.28e-03

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 41.32  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721884171 158 KDKVILDVGCGSGILSFFAAQAgARKVYAVEAS-TMAQHAEvlVNSNRLG-DRVVVIPGKVEEVtLPEQV-----DIII 229
Cdd:COG2265   233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDAR--ENARLNGlKNVEFVAGDLEEV-LPELLwggrpDVVV 307
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 155-228 2.11e-03

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


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 40.04  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 155 VDFKDKVILDVGCGSG-----ILsffaaQAGARKVYAVEastmaqhaevlVNSNRL-----GD-RVVVIPG----KVEEV 219
Cdd:COG1189    74 IDVAGKVCLDIGASTGgftdcLL-----QRGAAKVYAVD-----------VGYGQLawklrQDpRVVVLERtnarYLTPE 137


                  ....*....
gi 1721884171 220 TLPEQVDII 228
Cdd:COG1189   138 DLPEPPDLV 146
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 163-229 2.14e-03

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 38.06  E-value: 2.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721884171 163 LDVGCGSGILSFFAAQA----GARKVYAVEASTMAQHAEVLVNSNRLGDRVVVIPGKVEEVT---LPEQVDIII 229
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAAlrdnGLGRLTAVDPDPGAEEAGALLRKAGLDDRVRLIVGDSREALpslADGPIDLLF 74
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 149-232 2.51e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 149 AILQNHVDFKDKVILDVGCGSGILSffAAQAGAR---KVYAVEAS----TMAQH-AEvlvnsNRLGDRVVVIPGKVEEVT 220
Cdd:PRK09328   99 WALEALLLKEPLRVLDLGTGSGAIA--LALAKERpdaEVTAVDISpealAVARRnAK-----HGLGARVEFLQGDWFEPL 171

                          90
                  ....*....|..
gi 1721884171 221 LPEQVDIIISEP 232
Cdd:PRK09328  172 PGGRFDLIVSNP 183
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 148-232 2.97e-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: 40.03  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 148 RAILQNHVDFKdkvILDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNRLGDRVVVIPGKVEEVTLPEQV 225
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKI 183


                  ....*..
gi 1721884171 226 DIIISEP 232
Cdd:TIGR00536 184 DIIVSNP 190
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 158-219 3.37e-03

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


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 40.15  E-value: 3.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721884171 158 KDKVILDVGCGSGILSFFAAQAGAR-KVYAVEastmaQHAEVLV----NSNRLG-DRVVVIPGKVEEV 219
Cdd:COG2242   247 PGDVLWDIGAGSGSVSIEAARLAPGgRVYAIE-----RDPERAAliraNARRFGvPNVEVVEGEAPEA 309
PRK14967 PRK14967
putative methyltransferase; Provisional
 162-232 3.58e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 3.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721884171 162 ILDVGCGSGILSFFAAQAGARKVYAVEASTMAQhAEVLVNSNRLGDRVVVIPGKVEEVTLPEQVDIIISEP 232
Cdd:PRK14967   40 VLDLCTGSGALAVAAAAAGAGSVTAVDISRRAV-RSARLNALLAGVDVDVRRGDWARAVEFRPFDVVVSNP 109
PRK14968 PRK14968
putative methyltransferase; Provisional
 143-189 4.57e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 4.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1721884171 143 TGTYQRA-----ILQNHVDFKDKVILDVGCGSGILSFFAAQAGARKV------YAVEA 189
Cdd:PRK14968    3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC 60
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 157-228 4.90e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 38.62  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 157 FKDKVILDVGCGSGILSFFAA--QAGARKVYAVEASTMA-----QHAEVLvnsnRLGDRVVVIPGKVEEV--TLPEQVDI 227
Cdd:PRK00377   39 RKGDMILDIGCGTGSVTVEASllVGETGKVYAVDKDEKAinltrRNAEKF----GVLNNIVLIKGEAPEIlfTINEKFDR 114


                  .
gi 1721884171 228 I 228
Cdd:PRK00377  115 I 115
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 149-230 6.04e-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: 38.81  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721884171 149 AILQNHVDFKDKVILDVGCGSGILSF-FAAQAGARKVYAVEAS-TMAQHAEvlvnsNRLGDRVVVIPGKVEEVTLPE-QV 225
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISaGMLAQAK-----TKLSENVQFICGDAEKLPLEDsSF 99


                  ....*
gi 1721884171 226 DIIIS 230
Cdd:TIGR02072 100 DLIVS 104
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 161-213 7.42e-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: 7.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1721884171 161 VILDVGCGSGILSFFAAQAGAR-KVYAVEAST-MAQHAEVLVNSNRLGDrVVVIP 213
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNLPN-VVLLN 54
 
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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