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Conserved domains on  [gi|2064978430|gb|KAG7491437|]
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hypothetical protein MATL_G00003560 [Megalops atlanticus]

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 1.04e-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: 1.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430   8 GVRLLSIGDANGEIQRHSEQQPLRLEVKSTPDAALINLSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLLQFSS 87
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 2064978430  88 PADFSSFYNILKNCRGHNAERSVFS 112
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
133-320 1.48e-42

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.50  E-value: 1.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 133 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLTDRVVV 211
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 212 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPSGNLFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 290
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 2064978430 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 1.04e-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: 1.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430   8 GVRLLSIGDANGEIQRHSEQQPLRLEVKSTPDAALINLSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLLQFSS 87
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 2064978430  88 PADFSSFYNILKNCRGHNAERSVFS 112
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 4-113 2.14e-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: 190.30  E-value: 2.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430   4 SVFPGVRLLSIGDANGEIQRHSEQQPLRLEVKSTPDAALinlSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLL 83
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVL---STNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2064978430  84 QFSSPADFSSFYNILKNCRGHNAERSVFSE 113
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
133-320 1.48e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.50  E-value: 1.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 133 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLTDRVVV 211
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 212 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPSGNLFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 290
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 2064978430 291 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 320
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 162-263 1.10e-11

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 61.68  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 162 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNGLTDRVVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 239
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 2064978430 240 --ERMLESYLHAkkfLKPSGNLFPTI 263
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 162-257 2.00e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 60.66  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 162 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLtdRVVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 239
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 2064978430 240 ERMLESYLH-AKKFLKPSG 257
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 156-259 4.13e-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: 57.92  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 156 DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNGLTDRVVVI-PGKVEEVSLPeqVDIIISEpm 233
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....*.
gi 2064978430 234 gymLFNERMLESYLHAKKFLKPSGNL 259
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGGWL 255
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
143-229 1.24e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.93  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 143 TGTYQ------RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNGLTDRV 209
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAA--RENAEL----NGVELNV 171

                          90       100
                  ....*....|....*....|
gi 2064978430 210 VVIPGKveevslpEQVDIII 229
Cdd:PRK00517  172 YLPQGD-------LKADVIV 184
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 8-112 1.04e-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: 1.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430   8 GVRLLSIGDANGEIQRHSEQQPLRLEVKSTPDAALINLSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLLQFSS 87
Cdd:pfam11531   1 GVRLLSIGDANGEIQRHSEQQPLRLEVKVGPDAALIILSNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFAS 80

                          90       100
                  ....*....|....*....|....*
gi 2064978430  88 PADFSSFYNILKNCRGHNAERSVFS 112
Cdd:pfam11531  81 PADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 4-113 2.14e-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: 190.30  E-value: 2.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430   4 SVFPGVRLLSIGDANGEIQRHSEQQPLRLEVKSTPDAALinlSNTEETCVFKCSLSRETECSRVGKQSFIITLGCNSVLL 83
Cdd:cd13330     1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSVLVL---STNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2064978430  84 QFSSPADFSSFYNILKNCRGHNAERSVFSE 113
Cdd:cd13330    78 QFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
133-320 1.48e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.50  E-value: 1.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 133 QQNMMQDYVRTGTYQRAIlqNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLTDRVVV 211
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 212 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-FLKPSGNLFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 290
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 2064978430 291 SFHGVDLSALrgaAVDEYFRQPIVDTFDIR 320
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
148-229 9.75e-13

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 68.66  E-value: 9.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 148 RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNGLTDRVVVIPGKVEEvs 220
Cdd:COG2264   140 EALEKL--LKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA--RENAEL----NGVEDRIEVVLGDLLE-- 209


                  ....*....
gi 2064978430 221 lPEQVDIII 229
Cdd:COG2264   210 -DGPYDLVV 217
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 162-260 9.27e-12

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 63.41  E-value: 9.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 162 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLTDRVVVIPGKVEEVSLPEQVDIIISEPMgYMLFNE 240
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                          90       100
                  ....*....|....*....|.
gi 2064978430 241 RMLESYL-HAKKFLKPSGNLF 260
Cdd:COG2230   134 ENYPAYFaKVARLLKPGGRLL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 162-263 1.10e-11

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 61.68  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 162 VLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHAEVLVNSNGLTDRVVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 239
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*.
gi 2064978430 240 --ERMLESYLHAkkfLKPSGNLFPTI 263
Cdd:cd02440    82 dlARFLEEARRL---LKPGGVLVLTL 104
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
149-232 1.31e-11

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 63.77  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 149 AILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAStmAQHAEVLV-NSNGLTDRVVVIPGKVEEVSLPEQVDI 227
Cdd:COG2263    38 AYLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIAReNAERLGVRVDFIRADVTRIPLGGSVDT 113


                  ....*
gi 2064978430 228 IISEP 232
Cdd:COG2263   114 VVMNP 118
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 162-257 2.00e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 60.66  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 162 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLtdRVVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 239
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 2064978430 240 ERMLESYLH-AKKFLKPSG 257
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 137-260 7.66e-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: 59.65  E-value: 7.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 137 MQDYVRTGTYQRAILQ--NHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNGLTDRVVVIP 213
Cdd:COG2227     1 MSDPDARDFWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISpEALEIAR----ERAAELNVDFVQ 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2064978430 214 GKVEEVSLP-EQVDIIIS-EPMGYMLFNERMLEsylHAKKFLKPSGNLF 260
Cdd:COG2227    76 GDLEDLPLEdGSFDLVICsEVLEHLPDPAALLR---ELARLLKPGGLLL 121
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 148-274 4.57e-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: 59.90  E-value: 4.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 148 RAILQnHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMAQHA-EVLVNSNGLTdrVVVIPGKVEEVSLPEQVD 226
Cdd:COG3897    61 RYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAAlRLNAALNGVA--ITTRLGDWRDPPAAGGFD 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2064978430 227 IIIsepMGYMLFNERMLEsYLHA--KKFLKPSGNLFptIGD---VHLAPFTDE 274
Cdd:COG3897   138 LIL---GGDVLYERDLAE-PLLPflDRLAAPGGEVL--IGDpgrGYLPAFRER 184
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 156-259 4.13e-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: 57.92  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 156 DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNGLTDRVVVI-PGKVEEVSLPeqVDIIISEpm 233
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....*.
gi 2064978430 234 gymLFNERMLESYLHAKKFLKPSGNL 259
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGGWL 255
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 138-257 5.25e-09

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


Pssm-ID: 428356  Cd Length: 171  Bit Score: 55.67  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 138 QDYVRTGTYQRAI---LQNHTDFKDK-----VVLDVGCGSGIL---SFFAAQAGAR--KVYAVEASTMA----QHaevLV 200
Cdd:pfam05185  35 KDPVKYDLYERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEETGTkvKIYAVEKNPNAyvtlQK---RI 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2064978430 201 NSNGLTDRVVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKFLKPSG 257
Cdd:pfam05185 112 NFEKWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
143-229 1.24e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.93  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 143 TGTYQ------RAILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVY-------AVEAStmAQHAEVlvnsNGLTDRV 209
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAA--RENAEL----NGVELNV 171

                          90       100
                  ....*....|....*....|
gi 2064978430 210 VVIPGKveevslpEQVDIII 229
Cdd:PRK00517  172 YLPQGD-------LKADVIV 184
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 148-257 1.59e-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: 53.46  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 148 RAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNGLtdRVVVIPGKVEEVSLP-EQV 225
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISpEMLELARERAAEAGL--NVEFVVGDAEDLPFPdGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2064978430 226 DIIISePMGYMLFN--ERMLEsylHAKKFLKPSG 257
Cdd:COG2226    89 DLVIS-SFVLHHLPdpERALA---EIARVLKPGG 118
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 148-260 1.73e-08

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 54.13  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 148 RAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNGLtDRVVVIPGKVEEVSLPEQV 225
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2064978430 226 DIIISEP-------MGYMLfNERMLEsylHAKKFLKPSGNLF 260
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 158-257 6.10e-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: 54.58  E-value: 6.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 158 KDKVVLDVGCGSGILSFFAAQAGARKVYAVE----ASTMAQH-AEVlvnsNGLTDRVVVI-PGKVEEvslpEQVDI---- 227
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDidpvAVRAAKEnAEL----NGVEARLEVYlPGDLPK----EKADVvvan 232

                          90       100       110
                  ....*....|....*....|....*....|
gi 2064978430 228 IISEPMgymlfnERMLEsylHAKKFLKPSG 257
Cdd:pfam06325 233 ILADPL------IELAP---DIYALVKPGG 253
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 162-232 9.44e-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: 53.22  E-value: 9.44e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064978430 162 VLDVGCGSGILSFFAAQ-AGARKVYAVE----ASTMAQHAevlVNSNGLTDRVVVIPGKVEEVS---LPEQVDIIISEP 232
Cdd:COG4123    41 VLDLGTGTGVIALMLAQrSPGARITGVEiqpeAAELARRN---VALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP 116
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 163-260 5.72e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 47.66  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 163 LDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEVLVNSNGLTDRVvvipGKVEEVSLP-EQVDIIISEpmgYMLFNE 240
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISpEMLELAREKAPREGLTFVV----GDAEDLPFPdNSFDLVLSS---EVLHHV 72

                          90       100
                  ....*....|....*....|.
gi 2064978430 241 RMLESYLH-AKKFLKPSGNLF 260
Cdd:pfam08241  73 EDPERALReIARVLKPGGILI 93
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 151-220 2.01e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 49.07  E-value: 2.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064978430 151 LQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVE-ASTMAQHAEVLVNSNGLTDRVVVIPGKVEEVS 220
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL 125
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
162-230 3.29e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 45.97  E-value: 3.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064978430 162 VLDVGCGSGILS-FFAAQAGARKVYAVEAS-TMAQHAevlvnsNGLTDRVVVIPGKVEEVSLPEQVDIIIS 230
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVDLSpEMLARA------RARLPNVRFVVADLRDLDPPEPFDLVVS 69
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 150-228 1.06e-05

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


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 46.23  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 150 ILQNhtDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVE-----ASTMAQHAEVLvnsnGLTDRVVVIPGKVEEV---SL 221
Cdd:COG0742    35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEkdrkaAAVIRKNLEKL----GLEDRARVIRGDALRFlkrLA 108


                  ....*..
gi 2064978430 222 PEQVDII 228
Cdd:COG0742   109 GEPFDLV 115
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 139-260 1.42e-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: 45.95  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 139 DYVRTGTyqRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGA-RKVYAVEASTMA-QHAEVLVNSNGLTDrVVVIPGKV 216
Cdd:COG2813    32 DRLDIGT--RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGLEN-VEVLWSDG 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2064978430 217 EEVSLPEQVDIIISEP-----------MGYMLFNErmlesylhAKKFLKPSGNLF 260
Cdd:COG2813   109 LSGVPDGSFDLILSNPpfhagravdkeVAHALIAD--------AARHLRPGGELW 155
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
150-230 3.06e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 45.66  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 150 ILQNHTDFKDKVVLDVGCGSGILSFFAAQAgARKVYAVEA-STMAQHAEVLVNSNGltdRVVVIPGKVEEVSLPEqVDII 228
Cdd:PRK14896   21 IVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIAAG---NVEIIEGDALKVDLPE-FNKV 95


                  ..
gi 2064978430 229 IS 230
Cdd:PRK14896   96 VS 97
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 148-232 3.41e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 45.91  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 148 RAILQNHTDFKDKVVLDVGCGSGI--LSFFAAQAGARkVYAVEASTMA-QHAEVLVNSNGLTDRVVVIPGKV-EEVSLPE 223
Cdd:COG2890   102 ELALALLPAGAPPRVLDLGTGSGAiaLALAKERPDAR-VTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDG 180


                  ....*....
gi 2064978430 224 QVDIIISEP 232
Cdd:COG2890   181 RFDLIVSNP 189
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
139-230 4.90e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.22  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 139 DYVRTGTYQRAILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARkVYAVEAS-TMAQHAEvlvnSNGLTDRVVVipGKVE 217
Cdd:COG4976    27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSeEMLAKAR----EKGVYDRLLV--ADLA 99

                          90
                  ....*....|....
gi 2064978430 218 EVS-LPEQVDIIIS 230
Cdd:COG4976   100 DLAePDGRFDLIVA 113
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 146-291 5.93e-05

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: 45.47  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 146 YQRaILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEASTM--AQHaEVLVNSNGLTDRVVVIPGKVEEVSLPE 223
Cdd:pfam08003 104 WDR-VLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELflCQF-EAVRKLLGNDQRAHLLPLGIEQLPALA 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064978430 224 QVDIIISepMGYMLFNERMLESYLHAKKFLKPSGNL-FPTI---GDVHLAPFTDEQlYMEQftkANFWYQPS 291
Cdd:pfam08003 182 AFDTVFS--MGVLYHRRSPLDHLLQLKDQLVKGGELvLETLvidGDENTVLVPGDR-YAQM---RNVYFIPS 247
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
160-264 6.47e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.90  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 160 KVVLDVGCGSGILSFFAAQAGARKVYAVEAStmaqhAEVL----VN--SNGLTD-RVVVIPGKVEEV--SLP-EQVDIII 229
Cdd:COG2521   134 DRVLDTCTGLGYTAIEALKRGAREVITVEKD-----PNVLelaeLNpwSRELANeRIKIILGDASEVikTFPdESFDAII 208

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2064978430 230 SEPmgyMLFNermLESYLHAKKF-------LKPSGNLFPTIG 264
Cdd:COG2521   209 HDP---PRFS---LAGELYSLEFyrelyrvLKPGGRLFHYTG 244
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 158-229 1.39e-04

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 44.40  E-value: 1.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064978430 158 KDKVVLDVGCGSGILSFFAAQAgARKVYAVEAS-TMAQHAEVLVNSNGLtDRVVVIPGKVEEVsLPEQV-----DIII 229
Cdd:COG2265   233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDARENARLNGL-KNVEFVAGDLEEV-LPELLwggrpDVVV 307
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 162-260 1.74e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.98  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 162 VLDVGCGSGILSFFAAQAGARKVYAVEAS-TMAQHAEVLVNSNGLTD-RVVVIPGKVEEVSLPEQVDIIISepMGYM-LF 238
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVA--FGVLhHL 107

                          90       100
                  ....*....|....*....|...
gi 2064978430 239 NERMLESYLH-AKKFLKPSGNLF 260
Cdd:COG0500   108 PPEEREALLReLARALKPGGVLL 130
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
146-260 4.71e-04

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.54  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 146 YQRaiLQNHT-DFKDKVVLDVGCGSGILSFFAAQAGARKVYAVEAS--TMAQ-HA-EVLVNSNgltDRVVVIPGKVEEVS 220
Cdd:PRK15068  111 WDR--VLPHLsPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSqlFLCQfEAvRKLLGND---QRAHLLPLGIEQLP 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2064978430 221 LPEQVDIIISepMGyMLFNER----MLesyLHAKKFLKPSGNLF 260
Cdd:PRK15068  186 ALKAFDTVFS--MG-VLYHRRspldHL---KQLKDQLVPGGELV 223
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 149-230 1.18e-03

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 40.73  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 149 AILQNHTDFKDKVVLDVGCGSGILSF-FAAQAGARKVYAVEAS-TMAQHAEVLVNSNgltdrVVVIPGKVEEVSLPE-QV 225
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISaGMLAQAKTKLSEN-----VQFICGDAEKLPLEDsSF 99


                  ....*
gi 2064978430 226 DIIIS 230
Cdd:TIGR02072 100 DLIVS 104
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 148-300 1.21e-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: 41.18  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 148 RAILQNHTDFKdkvVLDVGCGSGILSFFAAQAGAR-KVYAVEASTMA-QHAEVLVNSNGLTDRVVVIPGKVEEVSLPEQV 225
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 226 DIIISEPmGYMLFNE--RMLESYLH----------------------AKKFLKPSGNLFPTIGDVHLApftdeqLYMEQF 281
Cdd:TIGR00536 184 DIIVSNP-PYIDEEDlaDLPNVVRFepllalvggddglnilrqiielAPDYLKPNGFLVCEIGNWQQK------SLKELL 256

                         170
                  ....*....|....*....
gi 2064978430 282 TKANFWYQPSFHGvDLSAL 300
Cdd:TIGR00536 257 RIKFTWYDVENGR-DLNGK 274
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 161-205 1.23e-03

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 39.60  E-value: 1.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2064978430 161 VVLDVGCGSGILSFFAAQAGAR-KVYAVEAST-MAQHAEVLVNSNGL 205
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNL 47
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 163-229 2.34e-03

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 37.67  E-value: 2.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064978430 163 LDVGCGSGILSFFAAQA----GARKVYAVEASTMAQHAEVLVNSNGLTDRVVVIPGKVEEVS---LPEQVDIII 229
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAAlrdnGLGRLTAVDPDPGAEEAGALLRKAGLDDRVRLIVGDSREALpslADGPIDLLF 74
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 156-228 2.70e-03

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


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 39.66  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 156 DFKDKVVLDVGCGSG-----ILsffaaQAGARKVYAVEastmaqhaevlVNSNGL-----TD-RVVVIPG----KVEEVS 220
Cdd:COG1189    75 DVAGKVCLDIGASTGgftdcLL-----QRGAAKVYAVD-----------VGYGQLawklrQDpRVVVLERtnarYLTPED 138


                  ....*...
gi 2064978430 221 LPEQVDII 228
Cdd:COG1189   139 LPEPPDLV 146
PRK14968 PRK14968
putative methyltransferase; Provisional
 143-210 3.50e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.73  E-value: 3.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064978430 143 TGTYQRA-----ILQNHTDFKDKVVLDVGCGSGILSFFAAQAGARKV------YAVEAstmaqhAEVLVNSNGLTDRVV 210
Cdd:PRK14968    3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC------AKCNAKLNNIRNNGV 75
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 158-259 3.78e-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: 38.72  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 158 KDKVVLDVGCGSGilSF--FAAQAGARKVYAVEastmaqhaevlVNSNGL-----TDRVVVIPG---------KVEEVsL 221
Cdd:pfam01728  21 PGKTVLDLGAAPG--GWsqVALQRGAGKVVGVD-----------LGPMQLwkprnDPGVTFIQGdirdpetldLLEEL-L 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2064978430 222 PEQVDIII---SEPMGYMLFNERMLESYLH------AKKFLKPSGNL 259
Cdd:pfam01728  87 GRKVDLVLsdgSPFISGNKVLDHLRSLDLVkaalevALELLRKGGNF 133
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 157-228 5.90e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 38.24  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 157 FKDKVVLDVGCGSGILSFFAA--QAGARKVYAVEASTMA-----QHAEVLvnsnGLTDRVVVIPGKVEEV--SLPEQVDI 227
Cdd:PRK00377   39 RKGDMILDIGCGTGSVTVEASllVGETGKVYAVDKDEKAinltrRNAEKF----GVLNNIVLIKGEAPEIlfTINEKFDR 114


                  .
gi 2064978430 228 I 228
Cdd:PRK00377  115 I 115
PRK14967 PRK14967
putative methyltransferase; Provisional
 162-232 6.07e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 38.50  E-value: 6.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064978430 162 VLDVGCGSGILSFFAAQAGARKVYAVEASTMA-QHAEVLVNSNGLtdRVVVIPGKVEEVSLPEQVDIIISEP 232
Cdd:PRK14967   40 VLDLCTGSGALAVAAAAAGAGSVTAVDISRRAvRSARLNALLAGV--DVDVRRGDWARAVEFRPFDVVVSNP 109
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 149-232 6.99e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.60  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064978430 149 AILQNHTDFKDKVVLDVGCGSGILSffAAQAGAR---KVYAVEAS----TMAQH-AEvlvnsNGLTDRVVVIPGKVEEVS 220
Cdd:PRK09328   99 WALEALLLKEPLRVLDLGTGSGAIA--LALAKERpdaEVTAVDISpealAVARRnAK-----HGLGARVEFLQGDWFEPL 171

                          90
                  ....*....|..
gi 2064978430 221 LPEQVDIIISEP 232
Cdd:PRK09328  172 PGGRFDLIVSNP 183
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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