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Conserved domains on  [gi|1625649062|ref|NP_001357018|]
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histone-arginine methyltransferase CARM1 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 39-103 4.28e-43

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


The actual alignment was detected with superfamily member pfam11531:

Pssm-ID: 473070  Cd Length: 105  Bit Score: 148.84  E-value: 4.28e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625649062  39 NEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFS 103
Cdd:pfam11531  41 GEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFASPADFCSFYNILKNCRGHKGERSVFS 105
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
124-311 2.82e-41

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 148.65  E-value: 2.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 124 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 202
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 203 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 281
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1625649062 282 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 311
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 ...
 39-103 4.28e-43

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: 148.84  E-value: 4.28e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625649062  39 NEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFS 103
Cdd:pfam11531  41 GEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFASPADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 34-104 2.47e-41

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: 144.47  E-value: 2.47e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625649062  34 DAGLRNEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFSE 104
Cdd:cd13330    37 LVLSTNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLLQFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
124-311 2.82e-41

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 148.65  E-value: 2.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 124 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 202
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 203 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 281
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1625649062 282 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 311
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 153-248 4.35e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 153 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 230
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1625649062 231 ERMLESYLH-AKKYLKPSG 248
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 153-248 4.90e-11

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 59.75  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 153 VLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 230
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|
gi 1625649062 231 --ERMLESylhAKKYLKPSG 248
Cdd:cd02440    82 dlARFLEE---ARRLLKPGG 98
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
134-178 2.62e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 2.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1625649062 134 TGTYQ------RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV 178
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 147-248 2.54e-07

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


Pssm-ID: 273061  Cd Length: 288  Bit Score: 52.53  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 147 DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEVSLPeqVDIIISEpm 224
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 1625649062 225 gymLFNERMLESYLHAKKYLKPSG 248
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
 
Name Accession Description Interval E-value
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 39-103 4.28e-43

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: 148.84  E-value: 4.28e-43
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1625649062  39 NEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFS 103
Cdd:pfam11531  41 GEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFASPADFCSFYNILKNCRGHKGERSVFS 105
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 34-104 2.47e-41

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: 144.47  E-value: 2.47e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625649062  34 DAGLRNEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFSE 104
Cdd:cd13330    37 LVLSTNEDVCVFKCSVNRETECSRVGKQSFLITLGCNSVLLQFATPSEFSSFYNALKNCRGQTNEKSVFSQ 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
124-311 2.82e-41

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 148.65  E-value: 2.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 124 QQNMMQDYVRTGTYQRAIlqNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVV 202
Cdd:COG4076    12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 203 IPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKK-YLKPSGNMFPTIGDVHLAPftdeqlyMEQFTKANFWYQP 281
Cdd:COG4076    90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKrLLKPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1625649062 282 SFHGVDLSALrgaAVDEYFRQPVVDTFDIR 311
Cdd:COG4076   163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
139-220 6.19e-12

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 66.35  E-value: 6.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 139 RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIY-------AVEAStmAQHAEVlvksNNLTDRIVVIPGKVEEvs 211
Cdd:COG2264   140 EALEKL--LKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA--RENAEL----NGVEDRIEVVLGDLLE-- 209


                  ....*....
gi 1625649062 212 lPEQVDIII 220
Cdd:COG2264   210 -DGPYDLVV 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 153-248 4.35e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 153 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQVDIIISePMGYMLFN 230
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 1625649062 231 ERMLESYLH-AKKYLKPSG 248
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 153-248 4.90e-11

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 59.75  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 153 VLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSL--PEQVDIIISEPMGYMLFN 230
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|
gi 1625649062 231 --ERMLESylhAKKYLKPSG 248
Cdd:cd02440    82 dlARFLEE---ARRLLKPGG 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 153-251 2.26e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 59.17  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 153 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMgYMLFNE 231
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                          90       100
                  ....*....|....*....|.
gi 1625649062 232 RMLESYL-HAKKYLKPSGNMF 251
Cdd:COG2230   134 ENYPAYFaKVARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 128-251 8.51e-10

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 56.56  E-value: 8.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 128 MQDYVRTGTYQRAILQ--NHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLTdrivVIP 204
Cdd:COG2227     1 MSDPDARDFWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISpEALEIARERAAELNVD----FVQ 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1625649062 205 GKVEEVSLP-EQVDIIIS-EPMGYMLFNERMLEsylHAKKYLKPSGNMF 251
Cdd:COG2227    76 GDLEDLPLEdGSFDLVICsEVLEHLPDPAALLR---ELARLLKPGGLLL 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
140-223 9.35e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 58.38  E-value: 9.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 140 AILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAStmAQHAEVLvKSN--NLTDRIVVIPGKVEEVSLPEQVD 217
Cdd:COG2263    38 AYLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIA-RENaeRLGVRVDFIRADVTRIPLGGSVD 112


                  ....*.
gi 1625649062 218 IIISEP 223
Cdd:COG2263   113 TVVMNP 118
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 139-220 1.08e-08

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


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 55.66  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 139 RAILQnHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHA-EVLVKSNNLTdrIVVIPGKVEEVSLPEQVD 217
Cdd:COG3897    61 RYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAAlRLNAALNGVA--ITTRLGDWRDPPAAGGFD 137


                  ...
gi 1625649062 218 III 220
Cdd:COG3897   138 LIL 140
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 153-223 1.29e-08

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


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 55.54  E-value: 1.29e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1625649062 153 VLDVGCGSGILSFFAAQ-AGARKIYAVE----ASTMAQHAevlVKSNNLTDRIVVIPGKVEEVS---LPEQVDIIISEP 223
Cdd:COG4123    41 VLDLGTGTGVIALMLAQrSPGARITGVEiqpeAAELARRN---VALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNP 116
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 149-248 1.94e-08

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


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 55.73  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 149 KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEvslpEQVDI----IISE 222
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAvRAAKENAELNGVEARLEVYlPGDLPK----EKADVvvanILAD 236

                          90       100
                  ....*....|....*....|....*.
gi 1625649062 223 PMgymlfnERMLEsylHAKKYLKPSG 248
Cdd:pfam06325 237 PL------IELAP---DIYALVKPGG 253
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
134-178 2.62e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 2.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1625649062 134 TGTYQ------RAILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAV 178
Cdd:PRK00517  100 TGTHPttrlclEALEKL--VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV 148
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 139-251 2.87e-08

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 53.36  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 139 RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGAR-KIYAVEASTMA-QHAEVLVKSNNLtDRIVVIPGKVEEVSLPEQV 216
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1625649062 217 DIIISEP-------MGYMLfNERMLEsylHAKKYLKPSGNMF 251
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 139-248 2.27e-07

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 50.38  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 139 RAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLtdRIVVIPGKVEEVSLP-EQV 216
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISpEMLELARERAAEAGL--NVEFVVGDAEDLPFPdGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1625649062 217 DIIISePMGYMLFN--ERMLEsylHAKKYLKPSG 248
Cdd:COG2226    89 DLVIS-SFVLHHLPdpERALA---EIARVLKPGG 118
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 147-248 2.54e-07

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


Pssm-ID: 273061  Cd Length: 288  Bit Score: 52.53  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 147 DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMA-QHAEVLVKSNNLTDRIVVI-PGKVEEVSLPeqVDIIISEpm 224
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAvESARKNAELNQVSDRLQVKlIYLEQPIEGK--ADVIVAN-- 232

                          90       100
                  ....*....|....*....|....
gi 1625649062 225 gymLFNERMLESYLHAKKYLKPSG 248
Cdd:TIGR00406 233 ---ILAEVIKELYPQFSRLVKPGG 253
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 129-248 4.52e-07

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


Pssm-ID: 428356  Cd Length: 171  Bit Score: 49.90  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 129 QDYVRTGTYQRAI---LQNHTDFKDK-----IVLDVGCGSGIL---SFFAAQAGAR--KIYAVEASTMA----QHaevLV 191
Cdd:pfam05185  35 KDPVKYDLYERAIekaLSDRVPEKKKtskllVILVVGAGRGPLvdrALRAAEETGTkvKIYAVEKNPNAyvtlQK---RI 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1625649062 192 KSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG 248
Cdd:pfam05185 112 NFEKWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 154-248 5.34e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.96  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 154 LDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAEVLVKSNNLTdrivVIPGKVEEVSLP-EQVDIIISEpmgYMLFNE 231
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISpEMLELAREKAPREGLT----FVVGDAEDLPFPdNSFDLVLSS---EVLHHV 72

                          90
                  ....*....|....*...
gi 1625649062 232 RMLESYLH-AKKYLKPSG 248
Cdd:pfam08241  73 EDPERALReIARVLKPGG 90
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
153-221 5.50e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 45.20  E-value: 5.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 153 VLDVGCGSGILS-FFAAQAGARKIYAVEAStmaqhAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIIS 221
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVDLS-----PEMLARARARLPNVRFVVADLRDLDPPEPFDLVVS 69
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 130-248 3.06e-05

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 44.80  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 130 DYVRTGTyqRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGA-RKIYAVEASTMA-QHAEVLVKSNNLTDrIVVIPGKV 207
Cdd:COG2813    32 DRLDIGT--RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGLEN-VEVLWSDG 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1625649062 208 EEVSLPEQVDIIISEP-----------MGYMLFNErmlesylhAKKYLKPSG 248
Cdd:COG2813   109 LSGVPDGSFDLILSNPpfhagravdkeVAHALIAD--------AARHLRPGG 152
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 141-219 4.42e-05

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


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 44.30  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 141 ILQNhtDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAStmAQHAEVLvKSN----NLTDRIVVIPGKVEEV---SLP 213
Cdd:COG0742    35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEKD--RKAAAVI-RKNleklGLEDRARVIRGDALRFlkrLAG 109


                  ....*.
gi 1625649062 214 EQVDII 219
Cdd:COG0742   110 EPFDLV 115
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 142-211 4.53e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 44.83  E-value: 4.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1625649062 142 LQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVE-ASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVS 211
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL 125
PRK14968 PRK14968
putative methyltransferase; Provisional
 134-277 1.79e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.58  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 134 TGTYQRA-----ILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKI------YAVEAstmaqhAEVLVKSNNLTDR-IV 201
Cdd:PRK14968    3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC------AKCNAKLNNIRNNgVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 202 VIPGK-VEEVS-------------LPEQVDIIISEPMGYMLF----NERMLESYL-HAKKYLKPSGNMFPTIGDvhlapF 262
Cdd:PRK14968   77 VIRSDlFEPFRgdkfdvilfnppyLPTEEEEEWDDWLNYALSggkdGREVIDRFLdEVGRYLKPGGRILLLQSS-----L 151

                         170
                  ....*....|....*
gi 1625649062 263 TDEQLYMEQFTKANF 277
Cdd:PRK14968  152 TGEDEVLEYLEKLGF 166
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
141-221 2.02e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 43.35  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 141 ILQNHTDFKDKIVLDVGCGSGILSFFAAQAgARKIYAVEA-STMAQHA-EVLVKSNNLTdrivVIPGKVEEVSLPEqVDI 218
Cdd:PRK14896   21 IVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLrDDEIAAGNVE----IIEGDALKVDLPE-FNK 94


                  ...
gi 1625649062 219 IIS 221
Cdd:PRK14896   95 VVS 97
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
130-221 2.59e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.91  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 130 DYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARkIYAVEAS-TMAQHAevlvKSNNLTDRIVVipGKVE 208
Cdd:COG4976    27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSeEMLAKA----REKGVYDRLLV--ADLA 99

                          90
                  ....*....|....
gi 1625649062 209 EVS-LPEQVDIIIS 221
Cdd:COG4976   100 DLAePDGRFDLIVA 113
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 139-223 3.36e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.83  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 139 RAILQNHTDFKDKIVLDVGCGSGI--LSFFAAQAGARkIYAVEASTMA-QHAEVLVKSNNLTDRIVVIPGKV-EEVSLPE 214
Cdd:COG2890   102 ELALALLPAGAPPRVLDLGTGSGAiaLALAKERPDAR-VTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDG 180


                  ....*....
gi 1625649062 215 QVDIIISEP 223
Cdd:COG2890   181 RFDLIVSNP 189
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
137-225 6.01e-04

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.15  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 137 YQRaiLQNHT-DFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEAS--TMAQ-HA-EVLVKSNNltdRIVVIPGKVEEVS 211
Cdd:PRK15068  111 WDR--VLPHLsPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSqlFLCQfEAvRKLLGNDQ---RAHLLPLGIEQLP 185

                          90
                  ....*....|....
gi 1625649062 212 LPEQVDIIISepMG 225
Cdd:PRK15068  186 ALKAFDTVFS--MG 197
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 140-221 8.49e-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: 41.12  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 140 AILQNHTDFKDKIVLDVGCGSGILSF-FAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTdrivvIPGKVEEVSLPE-QV 216
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISaGMLAQAKTKLSENVQF-----ICGDAEKLPLEDsSF 99


                  ....*
gi 1625649062 217 DIIIS 221
Cdd:TIGR02072 100 DLIVS 104
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 152-196 1.35e-03

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


Pssm-ID: 273628  Cd Length: 143  Bit Score: 39.22  E-value: 1.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1625649062 152 IVLDVGCGSGILSFFAAQAGAR-KIYAVEAST-MAQHAEVLVKSNNL 196
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLPdAYEILEENVKLNNL 47
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 137-282 1.63e-03

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


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 40.85  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 137 YQRaILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTM--AQHaEVLVKSNNLTDRIVVIPGKVEEVSLPE 214
Cdd:pfam08003 104 WDR-VLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELflCQF-EAVRKLLGNDQRAHLLPLGIEQLPALA 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1625649062 215 QVDIIISepMGYMLFNERMLESYLHAKKYLKPSGNM-FPTI---GDVHLAPFTDEQlYMEQftkANFWYQPS 282
Cdd:pfam08003 182 AFDTVFS--MGVLYHRRSPLDHLLQLKDQLVKGGELvLETLvidGDENTVLVPGDR-YAQM---RNVYFIPS 247
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 139-291 1.65e-03

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


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 139 RAILQNHTDFKdkiVLDVGCGSGILSFFAAQAGAR-KIYAVEASTMA-QHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQV 216
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKI 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 217 DIIISEPmGYMLFNE--RMLESYLH----------------------AKKYLKPSGNMFPTIGDVHLApftdeqLYMEQF 272
Cdd:TIGR00536 184 DIIVSNP-PYIDEEDlaDLPNVVRFepllalvggddglnilrqiielAPDYLKPNGFLVCEIGNWQQK------SLKELL 256

                         170
                  ....*....|....*....
gi 1625649062 273 TKANFWYQPSFHGvDLSAL 291
Cdd:TIGR00536 257 RIKFTWYDVENGR-DLNGK 274
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 149-220 2.40e-03

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 40.54  E-value: 2.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1625649062 149 KDKIVLDVGCGSGILSFFAAQAgARKIYAVEAS-TMAQHAEVLVKSNNLtDRIVVIPGKVEEVsLPEQV-----DIII 220
Cdd:COG2265   233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDARENARLNGL-KNVEFVAGDLEEV-LPELLwggrpDVVV 307
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
151-223 2.95e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 39.89  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 151 KIVLDVGCGSGILSFFAAQAGARKIYAVEAStmaqhAEVLVK------SNNLTD-RIVVIPGKVEEV--SLP-EQVDIII 220
Cdd:COG2521   134 DRVLDTCTGLGYTAIEALKRGAREVITVEKD-----PNVLELaelnpwSRELANeRIKIILGDASEVikTFPdESFDAII 208


                  ...
gi 1625649062 221 SEP 223
Cdd:COG2521   209 HDP 211
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 153-248 4.23e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.74  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 153 VLDVGCGSGILSFFAAQAGARKIYAVEAS-TMAQHAEVLVKSNNLTD-RIVVIPGKVEEVSLPEQVDIIISepMGYM-LF 229
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVA--FGVLhHL 107

                          90       100
                  ....*....|....*....|
gi 1625649062 230 NERMLESYLH-AKKYLKPSG 248
Cdd:COG0500   108 PPEEREALLReLARALKPGG 127
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
146-248 5.94e-03

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 39.16  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1625649062 146 TDFKDKIVLDVGCGSGILSFFAAQAGARKI--YAVEA-STMAQhaeVLVKSNNLTDR-IVVIPGKVEEVSLPEQVDIIIS 221
Cdd:COG0827   112 TKKEGLRILDPAVGTGNLLTTVLNQLKKKVnaYGVEVdDLLIR---LAAVLANLQGHpVELFHQDALQPLLIDPVDVVIS 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1625649062 222 E-PMGY-----------MLFNERMleSYLH------AKKYLKPSG 248
Cdd:COG0827   189 DlPVGYypnderakrfkLKADEGH--SYAHhlfieqSLNYLKPGG 231
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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