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Conserved domains on  [gi|1865689338|ref|XP_035262763|]
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histone-arginine methyltransferase CARM1 isoform X2 [Anguilla anguilla]

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 ...
 36-140 1.96e-71

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


:

Pssm-ID: 402914  Cd Length: 105  Bit Score: 225.11  E-value: 1.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338  36 GVRLLSIGDANGEIQRHSEQQPLRLEVKTTPDAALINLSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLLQFSS 115
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1865689338 116 PADFSSFYNILKNCRGHSSERSVFS 140
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
161-346 1.05e-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: 155.96  E-value: 1.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 161 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLKDRVEV 239
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 240 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGNLFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 318
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180
                  ....*....|....*....|....*...
gi 1865689338 319 SFHGVDLSALrgaAVDEYFRQPIVDTFD 346
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRL 187
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 36-140 1.96e-71

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


Pssm-ID: 402914  Cd Length: 105  Bit Score: 225.11  E-value: 1.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338  36 GVRLLSIGDANGEIQRHSEQQPLRLEVKTTPDAALINLSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLLQFSS 115
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1865689338 116 PADFSSFYNILKNCRGHSSERSVFS 140
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 32-141 1.66e-58

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


Pssm-ID: 241484  Cd Length: 107  Bit Score: 191.07  E-value: 1.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338  32 SVFPGVRLLSIGDANGEIQRHSEQQPLRLEVKTTPDAALinlSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLL 111
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVL---STNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1865689338 112 QFSSPADFSSFYNILKNCRGHSSERSVFSE 141
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
161-346 1.05e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 155.96  E-value: 1.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 161 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLKDRVEV 239
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 240 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGNLFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 318
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180
                  ....*....|....*....|....*...
gi 1865689338 319 SFHGVDLSALrgaAVDEYFRQPIVDTFD 346
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRL 187
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 190-285 5.14e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 65.28  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 190 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLkdRVEVIPGKVEEVSLP-EQVDIIISePMGYMLFN 267
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1865689338 268 ERMLESYLH-AKKFLKPNG 285
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 190-291 5.67e-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: 65.53  E-value: 5.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 190 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNGLKDRVEVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 267
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1865689338 268 --ERMLESYLHAkkfLKPNGNLFPTI 291
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
171-287 3.76e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 60.55  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 171 TGTYQ------RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNGLKDRV 237
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAA--RENAEL----NGVELNV 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1865689338 238 EVIPGKveevslpEQVDI----IISEPMgymlfnERMLESYlhaKKFLKPNGNL 287
Cdd:PRK00517  172 YLPQGD-------LKADVivanILANPL------LELAPDL---ARLLKPGGRL 209
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 184-287 1.12e-09

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: 59.85  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 184 DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNGLKDRVEVI-PGKVEEVSLPeqVDIIISEpm 261
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....*.
gi 1865689338 262 gymLFNERMLESYLHAKKFLKPNGNL 287
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGGWL 255
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 36-140 1.96e-71

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


Pssm-ID: 402914  Cd Length: 105  Bit Score: 225.11  E-value: 1.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338  36 GVRLLSIGDANGEIQRHSEQQPLRLEVKTTPDAALINLSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLLQFSS 115
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 1865689338 116 PADFSSFYNILKNCRGHSSERSVFS 140
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 32-141 1.66e-58

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


Pssm-ID: 241484  Cd Length: 107  Bit Score: 191.07  E-value: 1.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338  32 SVFPGVRLLSIGDANGEIQRHSEQQPLRLEVKTTPDAALinlSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLL 111
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVL---STNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1865689338 112 QFSSPADFSSFYNILKNCRGHSSERSVFSE 141
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
161-346 1.05e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 155.96  E-value: 1.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 161 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLKDRVEV 239
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 240 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPNGNLFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 318
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180
                  ....*....|....*....|....*...
gi 1865689338 319 SFHGVDLSALrgaAVDEYFRQPIVDTFD 346
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRL 187
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
176-287 1.49e-13

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 71.36  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 176 RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNGLKDRVEVIPGKVEEvs 248
Cdd:COG2264   140 EALEKL--LKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA--RENAEL----NGVEDRIEVVLGDLLE-- 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1865689338 249 lPEQVDI----IISEPmgymLfnERMLESYlhaKKFLKPNGNL 287
Cdd:COG2264   210 -DGPYDLvvanILANP----L--IELAPDL---AALLKPGGYL 242
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 190-285 5.14e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 65.28  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 190 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLkdRVEVIPGKVEEVSLP-EQVDIIISePMGYMLFN 267
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1865689338 268 ERMLESYLH-AKKFLKPNG 285
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 190-291 5.67e-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: 65.53  E-value: 5.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 190 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNGLKDRVEVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 267
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 1865689338 268 --ERMLESYLHAkkfLKPNGNLFPTI 291
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 190-288 9.75e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.11  E-value: 9.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 190 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLKDRVEVIPGKVEEVSLPEQVDIIISEPMgYMLFNE 268
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                          90       100
                  ....*....|....*....|.
gi 1865689338 269 RMLESYL-HAKKFLKPNGNLF 288
Cdd:COG2230   134 ENYPAYFaKVARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 165-288 2.05e-12

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: 64.27  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 165 MQDYVRTGTYQRAILQ--NHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNGLKDRVEVIP 241
Cdd:COG2227     1 MSDPDARDFWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISpEALEIAR----ERAAELNVDFVQ 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1865689338 242 GKVEEVSLP-EQVDIIIS-EPMGYMLFNERMLEsylHAKKFLKPNGNLF 288
Cdd:COG2227    76 GDLEDLPLEdGSFDLVICsEVLEHLPDPAALLR---ELARLLKPGGLLL 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
177-260 2.35e-12

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 66.08  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 177 AILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAStmAQHAEVLV-NSNGLKDRVEVIPGKVEEVSLPEQVDI 255
Cdd:COG2263    38 AYLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIAReNAERLGVRVDFIRADVTRIPLGGSVDT 113


                  ....*
gi 1865689338 256 IISEP 260
Cdd:COG2263   114 VVMNP 118
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 176-302 1.25e-10

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


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 61.44  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 176 RAILQnHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHA-EVLVNSNGLKdrVEVIPGKVEEVSLPEQVD 254
Cdd:COG3897    61 RYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAAlRLNAALNGVA--ITTRLGDWRDPPAAGGFD 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1865689338 255 IIIsepMGYMLFNERMLEsYLHA--KKFLKPNGNLFptIGD---VHLAPFTDE 302
Cdd:COG3897   138 LIL---GGDVLYERDLAE-PLLPflDRLAAPGGEVL--IGDpgrGYLPAFRER 184
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 166-285 2.27e-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: 59.91  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 166 QDYVRTGTYQRAI---LQNHTDFKDK-----VVLDVGCGSGIL---SFFAAQAGAR--KVYAVEASTMA----QHaevLV 228
Cdd:pfam05185  35 KDPVKYDLYERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEETGTkvKIYAVEKNPNAyvtlQK---RI 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1865689338 229 NSNGLKDRVEVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKFLKPNG 285
Cdd:pfam05185 112 NFEKWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
171-287 3.76e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 60.55  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 171 TGTYQ------RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNGLKDRV 237
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAA--RENAEL----NGVELNV 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1865689338 238 EVIPGKveevslpEQVDI----IISEPMgymlfnERMLESYlhaKKFLKPNGNL 287
Cdd:PRK00517  172 YLPQGD-------LKADVivanILANPL------LELAPDL---ARLLKPGGRL 209
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 176-285 9.61e-10

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: 57.31  E-value: 9.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 176 RAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNGLkdRVEVIPGKVEEVSLP-EQV 253
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISpEMLELARERAAEAGL--NVEFVVGDAEDLPFPdGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1865689338 254 DIIISePMGYMLFN--ERMLEsylHAKKFLKPNG 285
Cdd:COG2226    89 DLVIS-SFVLHHLPdpERALA---EIARVLKPGG 118
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 184-287 1.12e-09

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: 59.85  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 184 DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNGLKDRVEVI-PGKVEEVSLPeqVDIIISEpm 261
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....*.
gi 1865689338 262 gymLFNERMLESYLHAKKFLKPNGNL 287
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGGWL 255
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 176-288 1.43e-09

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 57.22  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 176 RAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNGLkDRVEVIPGKVEEVSLPEQV 253
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1865689338 254 DIIISEP-------MGYMLfNERMLEsylHAKKFLKPNGNLF 288
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 190-288 1.26e-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: 55.92  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 190 VLDVGCGSGILSFFAAQ-AGARKVYAVE----ASTMAQHAevlVNSNGLKDRVEVIPGKVEEVS---LPEQVDIIISEPm 261
Cdd:COG4123    41 VLDLGTGTGVIALMLAQrSPGARITGVEiqpeAAELARRN---VALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP- 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1865689338 262 GYMLFNE------------RM-----LESYLH-AKKFLKPNGNLF 288
Cdd:COG4123   117 PYFKAGSgrkspdearaiaRHedaltLEDLIRaAARLLKPGGRFA 161
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 186-285 4.22e-08

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 54.96  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 186 KDKVVLDVGCGSGILSFFAAQAGARKVYAVE----ASTMAQH-AEVlvnsNGLKDRVEVI-PGKVEEvslpEQVDI---- 255
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDidpvAVRAAKEnAEL----NGVEARLEVYlPGDLPK----EKADVvvan 232

                          90       100       110
                  ....*....|....*....|....*....|
gi 1865689338 256 IISEPMgymlfnERMLEsylHAKKFLKPNG 285
Cdd:pfam06325 233 ILADPL------IELAP---DIYALVKPGG 253
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 191-288 1.53e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.59  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 191 LDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNGLKDRVevipGKVEEVSLP-EQVDIIISEpmgYMLFNE 268
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISpEMLELAREKAPREGLTFVV----GDAEDLPFPdNSFDLVLSS---EVLHHV 72

                          90       100
                  ....*....|....*....|.
gi 1865689338 269 RMLESYLH-AKKFLKPNGNLF 288
Cdd:pfam08241  73 EDPERALReIARVLKPGGILI 93
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 179-248 3.76e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 51.38  E-value: 3.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865689338 179 LQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVE-ASTMAQHAEVLVNSNGLKDRVEVIPGKVEEVS 248
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL 125
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 178-285 8.75e-07

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: 49.69  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 178 ILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVE-----ASTMAQHAEVLvnsnGLKDRVEVIPGKVEEV---SL 249
Cdd:COG0742    35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEkdrkaAAVIRKNLEKL----GLEDRARVIRGDALRFlkrLA 108

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1865689338 250 PEQVDIIISEP---MGYMlfnERMLESyLHAKKFLKPNG 285
Cdd:COG0742   109 GEPFDLVFLDPpyaKGLL---EKALEL-LAENGLLAPGG 143
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
190-258 9.65e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.51  E-value: 9.65e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865689338 190 VLDVGCGSGILS-FFAAQAGARKVYAVEAS-TMAQHAEVLVnsnglkDRVEVIPGKVEEVSLPEQVDIIIS 258
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVDLSpEMLARARARL------PNVRFVVADLRDLDPPEPFDLVVS 69
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 167-288 2.74e-06

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: 48.26  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 167 DYVRTGTyqRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGA-RKVYAVEASTMA-QHAEVLVNSNGLkDRVEVIPGKV 244
Cdd:COG2813    32 DRLDIGT--RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGL-ENVEVLWSDG 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1865689338 245 EEVSLPEQVDIIISEP-----------MGYMLFNErmlesylhAKKFLKPNGNLF 288
Cdd:COG2813   109 LSGVPDGSFDLILSNPpfhagravdkeVAHALIAD--------AARHLRPGGELW 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 190-288 6.68e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.22  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 190 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLkDRVEVIPGKVEEV--SLPEQVDIIISepMGYM-L 265
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGL-GNVEFLVADLAELdpLPAESFDLVVA--FGVLhH 106

                          90       100
                  ....*....|....*....|....
gi 1865689338 266 FNERMLESYLH-AKKFLKPNGNLF 288
Cdd:COG0500   107 LPPEEREALLReLARALKPGGVLL 130
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 176-260 6.77e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 48.22  E-value: 6.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 176 RAILQNHTDFKDKVVLDVGCGSGI--LSFFAAQAGARkVYAVEASTMA-QHAEVLVNSNGLKDRVEVIPGKV-EEVSLPE 251
Cdd:COG2890   102 ELALALLPAGAPPRVLDLGTGSGAiaLALAKERPDAR-VTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDG 180


                  ....*....
gi 1865689338 252 QVDIIISEP 260
Cdd:COG2890   181 RFDLIVSNP 189
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
188-292 8.70e-06

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 47.98  E-value: 8.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 188 KVVLDVGCGSGILSFFAAQAGARKVYAVEAStmaqhAEVL----VN--SNGLKD-RVEVIPGKVEEV--SLP-EQVDIII 257
Cdd:COG2521   134 DRVLDTCTGLGYTAIEALKRGAREVITVEKD-----PNVLelaeLNpwSRELANeRIKIILGDASEVikTFPdESFDAII 208

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1865689338 258 SEPmgyMLFNermLESYLHAKKF-------LKPNGNLFPTIG 292
Cdd:COG2521   209 HDP---PRFS---LAGELYSLEFyrelyrvLKPGGRLFHYTG 244
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
178-258 9.66e-06

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 47.59  E-value: 9.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 178 ILQNHTDFKDKVVLDVGCGSGILSFFAAQAgARKVYAVEA-STMAQHAEVLVNSNGlkdRVEVIPGKVEEVSLPEqVDII 256
Cdd:PRK14896   21 IVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIAAG---NVEIIEGDALKVDLPE-FNKV 95


                  ..
gi 1865689338 257 IS 258
Cdd:PRK14896   96 VS 97
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 176-328 1.29e-05

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: 47.35  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 176 RAILQNHTDFKdkvVLDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNGLKDRVEVIPGKVEEVSLPEQV 253
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 254 DIIISEPmGYMLFNE--RMLESYLH----------------------AKKFLKPNGNLFPTIGDVHLApftdeqLYMEQF 309
Cdd:TIGR00536 184 DIIVSNP-PYIDEEDlaDLPNVVRFepllalvggddglnilrqiielAPDYLKPNGFLVCEIGNWQQK------SLKELL 256

                         170
                  ....*....|....*....
gi 1865689338 310 TKANFWYQPSFHGvDLSAL 328
Cdd:TIGR00536 257 RIKFTWYDVENGR-DLNGK 274
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 186-257 2.16e-05

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: 47.09  E-value: 2.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1865689338 186 KDKVVLDVGCGSGILSFFAAQAgARKVYAVEAS-TMAQHAEVLVNSNGLkDRVEVIPGKVEEVsLPEQV-----DIII 257
Cdd:COG2265   233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDARENARLNGL-KNVEFVAGDLEEV-LPELLwggrpDVVV 307
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
167-258 4.72e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.22  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 167 DYVRTGTYQRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNGLKDRVEVipGKVE 245
Cdd:COG4976    27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSeEMLAKAR----EKGVYDRLLV--ADLA 99

                          90
                  ....*....|....
gi 1865689338 246 EVS-LPEQVDIIIS 258
Cdd:COG4976   100 DLAePDGRFDLIVA 113
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 174-319 2.03e-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: 43.93  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 174 YQRaILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTM--AQHaEVLVNSNGLKDRVEVIPGKVEEVSLPE 251
Cdd:pfam08003 104 WDR-VLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELflCQF-EAVRKLLGNDQRAHLLPLGIEQLPALA 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1865689338 252 QVDIIISepMGYMLFNERMLESYLHAKKFLKPNGNL-FPTI---GDVHLAPFTDEQlYMEQftkANFWYQPS 319
Cdd:pfam08003 182 AFDTVFS--MGVLYHRRSPLDHLLQLKDQLVKGGELvLETLvidGDENTVLVPGDR-YAQM---RNVYFIPS 247
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
174-288 2.93e-04

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 43.31  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 174 YQRaiLQNHT-DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS--TMAQHaEVLVNSNGLKDRVEVIPGKVEEVSLP 250
Cdd:PRK15068  111 WDR--VLPHLsPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSqlFLCQF-EAVRKLLGNDQRAHLLPLGIEQLPAL 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1865689338 251 EQVDIIISepMGyMLFNER----MLesyLHAKKFLKPNGNLF 288
Cdd:PRK15068  188 KAFDTVFS--MG-VLYHRRspldHL---KQLKDQLVPGGELV 223
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 186-285 4.68e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.86  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 186 KDKVVLDVGCGSGILSFFAAQ--AGARKVYAVEAS-TMAQHAEVLVNSNGLkDRVEVIPGKVEEvsLPEQV-----DIII 257
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISeEAIEKARENAQKLGF-DNVEFEQGDIEE--LPELLeddkfDVVI 79

                          90       100
                  ....*....|....*....|....*....
gi 1865689338 258 S-EPMGYMLFNERMLESylhAKKFLKPNG 285
Cdd:pfam13847  80 SnCVLNHIPDPDKVLQE---ILRVLKPGG 105
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 177-258 4.81e-04

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 42.27  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 177 AILQNHTDFKDKVVLDVGCGSGILSF-FAAQAGARKVYAVEAS-TMAQHAEVLVNSNglkdrVEVIPGKVEEVSLPE-QV 253
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISaGMLAQAKTKLSEN-----VQFICGDAEKLPLEDsSF 99


                  ....*
gi 1865689338 254 DIIIS 258
Cdd:TIGR02072 100 DLIVS 104
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 189-241 5.05e-04

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: 40.76  E-value: 5.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1865689338 189 VVLDVGCGSGILSFFAAQAGAR-KVYAVEAST-MAQHAEVLVNSNGLKDrVEVIP 241
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNLPN-VVLLN 54
PRK14968 PRK14968
putative methyltransferase; Provisional
 171-314 5.69e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 171 TGTYQRA-----ILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKV------YAVEAstmaqhAEVLVNSNGLKDR-VE 238
Cdd:PRK14968    3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC------AKCNAKLNNIRNNgVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 239 VIPGK-VEEVS-------------LPEQVDIIISEPMGYMLF----NERMLESYL-HAKKFLKPNGNLFPTIGDvhlapF 299
Cdd:PRK14968   77 VIRSDlFEPFRgdkfdvilfnppyLPTEEEEEWDDWLNYALSggkdGREVIDRFLdEVGRYLKPGGRILLLQSS-----L 151

                         170
                  ....*....|....*
gi 1865689338 300 TDEQLYMEQFTKANF 314
Cdd:PRK14968  152 TGEDEVLEYLEKLGF 166
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
183-288 5.89e-04

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 42.24  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 183 TDFKDKVVLDVGCGSGILSFFAAQAGARKV--YAVEA-STMAQHAEVLVNSNGLKdrVEVIPGKVEEVSLPEQVDIIISE 259
Cdd:COG0827   112 TKKEGLRILDPAVGTGNLLTTVLNQLKKKVnaYGVEVdDLLIRLAAVLANLQGHP--VELFHQDALQPLLIDPVDVVISD 189

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1865689338 260 -PMGY-----------MLFNERMleSYLH------AKKFLKPNGNLF 288
Cdd:COG0827   190 lPVGYypnderakrfkLKADEGH--SYAHhlfieqSLNYLKPGGYLF 234
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
178-285 7.93e-04

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 40.69  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 178 ILQNHtdFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAeVLVNSNGLKDRVEVIPGKVEE-----VSLPEQ 252
Cdd:pfam03602  35 WLAPY--IEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQI-LKENLQLLGLPGAVLVMDALLallrlAGKGPV 111

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1865689338 253 VDIIISEPmGYM--LFNERMleSYLHAKKFLKPNG 285
Cdd:pfam03602 112 FDIVFLDP-PYAkgLIEEVL--DLLAEKGWLKPNA 143
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 191-287 8.14e-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: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 191 LDVGCGSGILSFFAAQAGAR-KVYAVEAS-TMAQHAEVLVNSNGLKDRVEV-IPGKVEEVSLPEQVDIIISEpmGYMLFN 267
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISpAALEAARERLAALGLLNAVRVeLFQLDLGELDPGSFDVVVAS--NVLHHL 78

                          90       100
                  ....*....|....*....|
gi 1865689338 268 ERMLESYLHAKKFLKPNGNL 287
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 191-257 9.05e-04

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 39.21  E-value: 9.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1865689338 191 LDVGCGSGILSFFAAQA----GARKVYAVEASTMAQHAEVLVNSNGLKDRVEVIPGKVEEVS---LPEQVDIII 257
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAAlrdnGLGRLTAVDPDPGAEEAGALLRKAGLDDRVRLIVGDSREALpslADGPIDLLF 74
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 177-260 9.84e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 41.30  E-value: 9.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 177 AILQNHTDFKDKVVLDVGCGSGILSffAAQAGAR---KVYAVEAS----TMAQH-AEvlvnsNGLKDRVEVIPGKVEEVS 248
Cdd:PRK09328   99 WALEALLLKEPLRVLDLGTGSGAIA--LALAKERpdaEVTAVDISpealAVARRnAK-----HGLGARVEFLQGDWFEPL 171

                          90
                  ....*....|..
gi 1865689338 249 LPEQVDIIISEP 260
Cdd:PRK09328  172 PGGRFDLIVSNP 183
PRK14967 PRK14967
putative methyltransferase; Provisional
 190-260 1.11e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 40.81  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1865689338 190 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQhAEVLVNSNGLKDRVEVIPGKVEEVSLPEQVDIIISEP 260
Cdd:PRK14967   40 VLDLCTGSGALAVAAAAAGAGSVTAVDISRRAV-RSARLNALLAGVDVDVRRGDWARAVEFRPFDVVVSNP 109
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 186-287 1.41e-03

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


Pssm-ID: 426399  Cd Length: 179  Bit Score: 39.88  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 186 KDKVVLDVGCGSGilSF--FAAQAGARKVYAVEastmaqhaevlVNSNGLKD-----RVEVIPG---------KVEEVsL 249
Cdd:pfam01728  21 PGKTVLDLGAAPG--GWsqVALQRGAGKVVGVD-----------LGPMQLWKprndpGVTFIQGdirdpetldLLEEL-L 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1865689338 250 PEQVDIII---SEPMGYMLFNERMLESYLH------AKKFLKPNGNL 287
Cdd:pfam01728  87 GRKVDLVLsdgSPFISGNKVLDHLRSLDLVkaalevALELLRKGGNF 133
arsM PRK11873
arsenite methyltransferase;
189-258 4.48e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 39.16  E-value: 4.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1865689338 189 VVLDVGCGSGILSFFAAQA-GAR-KVYAVEastMAQHAEVLVNSNGLK---DRVEVIPGKVEEVSLP-EQVDIIIS 258
Cdd:PRK11873   80 TVLDLGSGGGFDCFLAARRvGPTgKVIGVD---MTPEMLAKARANARKagyTNVEFRLGEIEALPVAdNSVDVIIS 152
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 190-258 6.54e-03

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 38.85  E-value: 6.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1865689338 190 VLDVGCGSGILSFFAAQ-AGARKVYAVEASTMAQHAEVLVNSNGLKDRVEVIPGKVEEvsLPEQVDIIIS 258
Cdd:pfam02353  65 LLDIGCGWGGLMRRAAErYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRD--FDEPFDRIVS 132
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 186-251 7.14e-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: 38.99  E-value: 7.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1865689338 186 KDKVVLDVGCGSGILSFFAAQAGAR-KVYAVE-----ASTMAQHAEVLvnsnGLkDRVEVIPGKVEEV--SLPE 251
Cdd:COG2242   247 PGDVLWDIGAGSGSVSIEAARLAPGgRVYAIErdperAALIRANARRF----GV-PNVEVVEGEAPEAlaDLPD 315
 
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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