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Conserved domains on  [gi|340720716|ref|XP_003398778|]
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histone-arginine methyltransferase CARMER isoform X2 [Bombus terrestris]

Protein Classification

histone-arginine methyltransferase( domain architecture ID 10351171)

histone-arginine methyltransferase is a type I arginine methyltransferase belonging to the class I SAM-dependent methyltransferase superfamily, similar to Drosophila histone-arginine methyltransferase CARMER that methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins, using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110|2.30.29.30
EC:  2.1.1.319
Gene Ontology:  GO:1904047|GO:0035097|GO:0042054|GO:0018216
PubMed:  12504684|12826405|22728242|15493994
SCOP:  3000118|4002395

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
134-321 3.49e-39

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: 143.25  E-value: 3.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 134 QQNMMQDYIRTSTYQRAIlgNLSDFKDKVVLDVGAGSGILSFFAVQAGAKKVYAVEAS-NMANHAELLVAANNLSDKIIV 212
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 213 IAGKIEEIDLPERVDCIVSEPMGYMLYNERMLETYLHAKKWLV-PGGRMFPSRGDLHIAPfsdenlyMEQFNKANFWYQT 291
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLkPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 340720716 292 CFHGVDLSAMRNNAIKEyfrQPIVDTFDIR 321
Cdd:COG4076  163 QFDGFDFRLFGFLLYAE---PLLHLTRLVR 189
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 4-114 5.69e-06

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 cd13330:

Pssm-ID: 473070  Cd Length: 107  Bit Score: 45.47  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716   4 VFRAVTVSTLS--NNGQSTAKFNKPVTLNINYDpqglSVEFLagesTGRDKTTLLEFPVTPSTECSRVSSRSYVFTLDTD 81
Cdd:cd13330    2 VFPGVRLLSIGdaNGEIQRHAEQQPLRLEVKAG----SVLVL----STNEDVCVFKCSVNRETECSRVGKQSFLITLGCN 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 340720716  82 SLLITFVSETDFRNFHSQilkLKNGKGI----SAFNE 114
Cdd:cd13330   74 SVLLQFATPSEFSSFYNA---LKNCRGQtnekSVFSQ 107
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
134-321 3.49e-39

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 143.25  E-value: 3.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 134 QQNMMQDYIRTSTYQRAIlgNLSDFKDKVVLDVGAGSGILSFFAVQAGAKKVYAVEAS-NMANHAELLVAANNLSDKIIV 212
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 213 IAGKIEEIDLPERVDCIVSEPMGYMLYNERMLETYLHAKKWLV-PGGRMFPSRGDLHIAPfsdenlyMEQFNKANFWYQT 291
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLkPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 340720716 292 CFHGVDLSAMRNNAIKEyfrQPIVDTFDIR 321
Cdd:COG4076  163 QFDGFDFRLFGFLLYAE---PLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 163-264 2.86e-13

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 66.30  E-value: 2.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 163 VLDVGAGSGILSFFAVQAGAKKVYAVEASNMANHAELLVAANNLSDKIIVIAGKIEEIDL--PERVDCIVSEPMgYMLYN 240
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPP-LHHLV 80

                         90       100
                 ....*....|....*....|....
gi 340720716 241 ERMLETYLHAKKWLVPGGRMFPSR 264
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTL 104
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 163-258 1.93e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.57  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  163 VLDVGAGSGILSFFAVQAGAKKVYAVEAS-NMANHAELLVAANNLsdKIIVIAGKIEEIDLP-ERVDCIVSePMGYMLYN 240
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 340720716  241 ERMLETYLH-AKKWLVPGG 258
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
157-214 4.25e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 51.31  E-value: 4.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 157 DFKDKVVLDVGAGSGILSFFAVQAGAKKVY-------AVEAS--NMA-NHAEL------------LVAANNLSDKIIVIA 214
Cdd:PRK00517 117 VLPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAAreNAElNGVELnvylpqgdlkadVIVANILANPLLELA 196
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 4-114 5.69e-06

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: 45.47  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716   4 VFRAVTVSTLS--NNGQSTAKFNKPVTLNINYDpqglSVEFLagesTGRDKTTLLEFPVTPSTECSRVSSRSYVFTLDTD 81
Cdd:cd13330    2 VFPGVRLLSIGdaNGEIQRHAEQQPLRLEVKAG----SVLVL----STNEDVCVFKCSVNRETECSRVGKQSFLITLGCN 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 340720716  82 SLLITFVSETDFRNFHSQilkLKNGKGI----SAFNE 114
Cdd:cd13330   74 SVLLQFATPSEFSSFYNA---LKNCRGQtnekSVFSQ 107
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 48-102 3.06e-05

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: 43.29  E-value: 3.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 340720716   48 TGRDKTTLLEFPVTPSTECSRVSSRSYVFTLDTDSLLITFVSETDFRNFHSqILK 102
Cdd:pfam11531  39 SNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFASPADFCSFYN-ILK 92
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 162-208 8.44e-05

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: 43.07  E-value: 8.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 340720716  162 VVLDVGAGSGILSFFAVQAGAK-KVYAVEAS-NMANHAELLVAANNLSD 208
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLpDAYEILEENVKLNNLPN 49
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
134-321 3.49e-39

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 143.25  E-value: 3.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 134 QQNMMQDYIRTSTYQRAIlgNLSDFKDKVVLDVGAGSGILSFFAVQAGAKKVYAVEAS-NMANHAELLVAANNLSDKIIV 212
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 213 IAGKIEEIDLPERVDCIVSEPMGYMLYNERMLETYLHAKKWLV-PGGRMFPSRGDLHIAPfsdenlyMEQFNKANFWYQT 291
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLkPGGRIIPERITNAAQP-------VESPVDAEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 340720716 292 CFHGVDLSAMRNNAIKEyfrQPIVDTFDIR 321
Cdd:COG4076  163 QFDGFDFRLFGFLLYAE---PLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 163-264 2.86e-13

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 66.30  E-value: 2.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 163 VLDVGAGSGILSFFAVQAGAKKVYAVEASNMANHAELLVAANNLSDKIIVIAGKIEEIDL--PERVDCIVSEPMgYMLYN 240
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPP-LHHLV 80

                         90       100
                 ....*....|....*....|....
gi 340720716 241 ERMLETYLHAKKWLVPGGRMFPSR 264
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTL 104
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 163-261 4.57e-12

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 64.18  E-value: 4.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 163 VLDVGAGSGILSFFAVQAGAKKVYAVEAS-NMANHAELLVAANNLSDKIIVIAGKIEEIDLPERVDCIVSEPMgYMLYNE 241
Cdd:COG2230   55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                         90       100
                 ....*....|....*....|.
gi 340720716 242 RMLETYL-HAKKWLVPGGRMF 261
Cdd:COG2230  134 ENYPAYFaKVARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 138-261 7.08e-12

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 62.73  E-value: 7.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 138 MQDYIRTSTYQRAILGNLSDF--KDKVVLDVGAGSGILSFFAVQAGAkKVYAVEAS-NMANHAELLVAANNLSdkiiVIA 214
Cdd:COG2227    1 MSDPDARDFWDRRLAALLARLlpAGGRVLDVGCGTGRLALALARRGA-DVTGVDISpEALEIARERAAELNVD----FVQ 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 340720716 215 GKIEEIDLP-ERVDCIVSepMGYMLYNERMLETYLHAKKWLVPGGRMF 261
Cdd:COG2227   76 GDLEDLPLEdGSFDLVIC--SEVLEHLPDPAALLRELARLLKPGGLLL 121
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
157-230 7.79e-11

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 63.27  E-value: 7.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 157 DFKDKVVLDVGAGSGILSFFAVQAGAKKVY-------AVEASnMANhaellVAANNLSDKIIVIAGKIEEidlPERVDCI 229
Cdd:COG2264  146 LKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEAA-REN-----AELNGVEDRIEVVLGDLLE---DGPYDLV 216


                 .
gi 340720716 230 V 230
Cdd:COG2264  217 V 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 163-258 1.93e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.57  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  163 VLDVGAGSGILSFFAVQAGAKKVYAVEAS-NMANHAELLVAANNLsdKIIVIAGKIEEIDLP-ERVDCIVSePMGYMLYN 240
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 340720716  241 ERMLETYLH-AKKWLVPGG 258
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
157-233 1.33e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 57.99  E-value: 1.33e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 340720716 157 DFKDKVVLDVGAGSGILSFFAVQAGAKKVYAVEASnmANHAELLV-AANNLSDKIIVIAGKIEEIDLPERVDCIVSEP 233
Cdd:COG2263   43 DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDID--PEALEIAReNAERLGVRVDFIRADVTRIPLGGSVDTVVMNP 118
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 149-268 6.70e-09

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: 54.61  E-value: 6.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 149 RAILGNLSDFKDKVVLDVGAGSGILSFFAVQAGAkKVYAVEAS-NMANHAELLVAANNLsdKIIVIAGKIEEIDLP-ERV 226
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAERGA-RVTGVDISpEMLELARERAAEAGL--NVEFVVGDAEDLPFPdGSF 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 340720716 227 DCIVSepmGYMLYN----ERMLEtylHAKKWLVPGGRMF------PSRGDLH 268
Cdd:COG2226   89 DLVIS---SFVLHHlpdpERALA---EIARVLKPGGRLVvvdfspPDLAELE 134
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 151-261 1.43e-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: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 151 ILGNLSDFKD-KVVLDVGAGSGILSFFAVQ-AGAKKVYAVEA-SNMANHAELLVAANNLSDKIIVIAGKIEEI---DLPE 224
Cdd:COG4123   28 LLAAFAPVKKgGRVLDLGTGTGVIALMLAQrSPGARITGVEIqPEAAELARRNVALNGLEDRITVIHGDLKEFaaeLPPG 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 340720716 225 RVDCIVSEPmGYMLYNE------------RM-----LETYLH-AKKWLVPGGRMF 261
Cdd:COG4123  108 SFDLVVSNP-PYFKAGSgrkspdearaiaRHedaltLEDLIRaAARLLKPGGRFA 161
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 149-245 1.63e-07

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: 52.19  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 149 RAILGNlSDFKDKVVLDVGAGSGILSFFAVQAGAKKVYAVEASNMA-NHAELLVAANNLsdKIIVIAGKIEEIDLPERVD 227
Cdd:COG3897   61 RYLLDH-PEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEAlAALRLNAALNGV--AITTRLGDWRDPPAAGGFD 137

                         90
                 ....*....|....*...
gi 340720716 228 CIVsepMGYMLYNERMLE 245
Cdd:COG3897  138 LIL---GGDVLYERDLAE 152
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 159-259 3.85e-07

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: 51.88  E-value: 3.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  159 KDKVVLDVGAGSGILSFFAVQAGAKKVYAVEASNMA-NHAELLVAANNLSDKIIVIAGKieeiDLPER-VDCIV----SE 232
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAvRAAKENAELNGVEARLEVYLPG----DLPKEkADVVVanilAD 236

                          90       100
                  ....*....|....*....|....*..
gi 340720716  233 PMgymlynERMLEtylHAKKWLVPGGR 259
Cdd:pfam06325 237 PL------IELAP---DIYALVKPGGY 254
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
157-214 4.25e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 51.31  E-value: 4.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 157 DFKDKVVLDVGAGSGILSFFAVQAGAKKVY-------AVEAS--NMA-NHAEL------------LVAANNLSDKIIVIA 214
Cdd:PRK00517 117 VLPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAAreNAElNGVELnvylpqgdlkadVIVANILANPLLELA 196
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
163-261 1.75e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 46.74  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 163 VLDVGAGSGILS-FFAVQAGAKKVYAVEASnmanhAELLVAANNLSDKIIVIAGKIEEIDLPERVDCIVSepmGYML-YN 240
Cdd:COG4106    5 VLDLGCGTGRLTaLLAERFPGARVTGVDLS-----PEMLARARARLPNVRFVVADLRDLDPPEPFDLVVS---NAALhWL 76

                         90       100
                 ....*....|....*....|.
gi 340720716 241 ERMLETYLHAKKWLVPGGRMF 261
Cdd:COG4106   77 PDHAALLARLAAALAPGGVLA 97
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 149-261 1.91e-06

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: 48.36  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  149 RAILGNLSDFKDKVVLDVGAGSGILSFFAVQAGAK-KVYAVEASNMA-NHAELLVAANNLSDKIIVIAGKIEEIDlPERV 226
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGLENGEVVASDVYSGVE-DGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 340720716  227 DCIVSEP-------MGYMLyNERMLEtylHAKKWLVPGGRMF 261
Cdd:pfam05175 100 DLIISNPpfhaglaTTYNV-AQRFIA---DAKRHLRPGGELW 137
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 150-259 3.07e-06

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 49.00  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 150 AILGNLSDFKDKVVLDVGAGSGILS-FFAVQAGAK-KVYAVEA-SNMANHAELLVAANNLSDKIIVIAGKIEEIDLPERV 226
Cdd:COG2519   82 YIIARLDIFPGARVLEAGTGSGALTlALARAVGPEgKVYSYERrEDFAEIARKNLERFGLPDNVELKLGDIREGIDEGDV 161

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 340720716 227 DCIV---SEPmgymlynERMLEtylHAKKWLVPGGR 259
Cdd:COG2519  162 DAVFldmPDP-------WEALE---AVAKALKPGGV 187
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
151-231 5.27e-06

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 48.36  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 151 ILGNLSDFKDKVVLDVGAGSGILSFFaVQAGAKKVYAVEA-SNMANHA-ELLVAANNLSdkiiVIAGKIEEIDLPErVDC 228
Cdd:PRK14896  21 IVEYAEDTDGDPVLEIGPGKGALTDE-LAKRAKKVYAIELdPRLAEFLrDDEIAAGNVE----IIEGDALKVDLPE-FNK 94


                 ...
gi 340720716 229 IVS 231
Cdd:PRK14896  95 VVS 97
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 4-114 5.69e-06

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: 45.47  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716   4 VFRAVTVSTLS--NNGQSTAKFNKPVTLNINYDpqglSVEFLagesTGRDKTTLLEFPVTPSTECSRVSSRSYVFTLDTD 81
Cdd:cd13330    2 VFPGVRLLSIGdaNGEIQRHAEQQPLRLEVKAG----SVLVL----STNEDVCVFKCSVNRETECSRVGKQSFLITLGCN 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 340720716  82 SLLITFVSETDFRNFHSQilkLKNGKGI----SAFNE 114
Cdd:cd13330   74 SVLLQFATPSEFSSFYNA---LKNCRGQtnekSVFSQ 107
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 149-261 6.64e-06

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 47.11  E-value: 6.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 149 RAILGNLSDFKDKVVLDVGAGSGILS-FFAVQAGAKKVYAVEASNMA-NHAELLVAANNLSDkIIVIAGKIEEIDLPERV 226
Cdd:COG2813   39 RLLLEHLPEPLGGRVLDLGCGYGVIGlALAKRNPEARVTLVDVNARAvELARANAAANGLEN-VEVLWSDGLSGVPDGSF 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 340720716 227 DCIVSEP-------MGYMLYnERMLETylhAKKWLVPGGRMF 261
Cdd:COG2813  118 DLILSNPpfhagraVDKEVA-HALIAD---AARHLRPGGELW 155
CARM1 pfam11531
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ...
 48-102 3.06e-05

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: 43.29  E-value: 3.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 340720716   48 TGRDKTTLLEFPVTPSTECSRVSSRSYVFTLDTDSLLITFVSETDFRNFHSqILK 102
Cdd:pfam11531  39 SNGEEVCVFKCSVSRDTECSRVGKQSFIITLGCNSVLLQFASPADFCSFYN-ILK 92
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-261 5.78e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 42.27  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  164 LDVGAGSGILSFFAVQAGAkKVYAVEAS-NMANHAELLVAANNLSdkiiVIAGKIEEIDLP-ERVDCIVSEpmgYMLYNE 241
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISpEMLELAREKAPREGLT----FVVGDAEDLPFPdNSFDLVLSS---EVLHHV 72

                          90       100
                  ....*....|....*....|.
gi 340720716  242 RMLETYLH-AKKWLVPGGRMF 261
Cdd:pfam08241  73 EDPERALReIARVLKPGGILI 93
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 162-208 8.44e-05

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: 43.07  E-value: 8.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 340720716  162 VVLDVGAGSGILSFFAVQAGAK-KVYAVEAS-NMANHAELLVAANNLSD 208
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLpDAYEILEENVKLNNLPN 49
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 149-261 1.25e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 44.37  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 149 RAILGNLSDFKDKVVLDVGAGSGILsffAVqAGAK-----KVYAVEASNMA-NHAELLVAANNLSDKIIVIAGKI-EEID 221
Cdd:COG2890  102 ELALALLPAGAPPRVLDLGTGSGAI---AL-ALAKerpdaRVTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLP 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 340720716 222 LPERVDCIVS--------------------EPM--------GYMLYnERMLEtylHAKKWLVPGGRMF 261
Cdd:COG2890  178 GDGRFDLIVSnppyipedeiallppevrdhEPRlaldggedGLDFY-RRIIA---QAPRLLKPGGWLL 241
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 151-258 1.28e-04

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: 43.15  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 151 ILGNlsDFKDKVVLDVGAGSGILSFFAVQAGAKKVYAVEASnmANHAELL---VAANNLSDKIIVIAGKIE---EIDLPE 224
Cdd:COG0742   35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEKD--RKAAAVIrknLEKLGLEDRARVIRGDALrflKRLAGE 110

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 340720716 225 RVDCIVSEP---MGYMlynERMLETyLHAKKWLVPGG 258
Cdd:COG0742  111 PFDLVFLDPpyaKGLL---EKALEL-LAENGLLAPGG 143
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 139-241 1.48e-04

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: 42.58  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  139 QDYIRTSTYQRAILGNLSDFKDK--------VVLDVGAGSGIL---SFFAVQ-AGAK-KVYAVEA-SNMANHAELLVAAN 204
Cdd:pfam05185  35 KDPVKYDLYERAIEKALSDRVPEkkktskllVILVVGAGRGPLvdrALRAAEeTGTKvKIYAVEKnPNAYVTLQKRINFE 114

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 340720716  205 NLSDKIIVIAGKIEEIDLPERVDCIVSEPMGYMLYNE 241
Cdd:pfam05185 115 KWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNE 151
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 147-258 1.84e-04

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


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 43.93  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  147 YQRaILGNLSDFKDKVVLDVGAGSGILSFFAVQAGAKKVYAVEASNM-ANHAELLVAANNLSDKIIVIAGKIEEIDLPER 225
Cdd:pfam08003 104 WDR-VLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELfLCQFEAVRKLLGNDQRAHLLPLGIEQLPALAA 182

                          90       100       110
                  ....*....|....*....|....*....|....
gi 340720716  226 VDCIVSepMGyMLYNERM-LETYLHAKKWLVPGG 258
Cdd:pfam08003 183 FDTVFS--MG-VLYHRRSpLDHLLQLKDQLVKGG 213
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
147-258 4.09e-04

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.92  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 147 YQRaILGNLSDFKDKVVLDVGAGSGILSFFAVQAGAKKVYAVEASnmanhaELLV----AANNLSDK---IIVIAGKIEE 219
Cdd:PRK15068 111 WDR-VLPHLSPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPS------QLFLcqfeAVRKLLGNdqrAHLLPLGIEQ 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 340720716 220 IDLPERVDCIVSepMGyMLYNERM-LETYLHAKKWLVPGG 258
Cdd:PRK15068 184 LPALKAFDTVFS--MG-VLYHRRSpLDHLKQLKDQLVPGG 220
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 150-231 4.74e-04

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 42.27  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  150 AILGNLSDFKDKVVLDVGAGSGILS-----FFAVQagakKVYAVEAS-NManhaeLLVAANNLSDKIIVIAGKIEEIDLP 223
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTrallkRFPQA----EFIALDISaGM-----LAQAKTKLSENVQFICGDAEKLPLE 95


                  ....*....
gi 340720716  224 ER-VDCIVS 231
Cdd:TIGR02072  96 DSsFDLIVS 104
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
140-259 1.78e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 39.60  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 140 DYIRTSTYQRAILGNLSDFKDKVVLDVGAGSGILSFFAVQAGaKKVYAVEAS-NMANHAellvAANNLSDKIIViaGKIE 218
Cdd:COG4976   27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSeEMLAKA----REKGVYDRLLV--ADLA 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 340720716 219 EID-LPERVDCIVSepMGYMLYNERMLETYLHAKKWLVPGGR 259
Cdd:COG4976  100 DLAePDGRFDLIVA--ADVLTYLGDLAAVFAGVARALKPGGL 139
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-259 2.72e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.35  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  164 LDVGAGSGILSFFAVQAGA-KKVYAVEAS-NMANHAELLVAANNLSDKIIVIAGKIEEIDL-PERVDCIVSEpmGYMLYN 240
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPgLEYTGLDISpAALEAARERLAALGLLNAVRVELFQLDLGELdPGSFDVVVAS--NVLHHL 78

                          90
                  ....*....|....*....
gi 340720716  241 ERMLETYLHAKKWLVPGGR 259
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGV 97
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 157-231 2.90e-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: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 157 DFKDKVVLDVGAGSGilSF--FAVQAGAKKVYAVEasnmanhaellVAANNLSDKI------IVIAG----KIEEIDLPE 224
Cdd:COG1189   75 DVAGKVCLDIGASTG--GFtdCLLQRGAAKVYAVD-----------VGYGQLAWKLrqdprvVVLERtnarYLTPEDLPE 141


                 ....*..
gi 340720716 225 RVDCIVS 231
Cdd:COG1189  142 PPDLVVI 148
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 159-260 4.18e-03

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


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 37.69  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  159 KDKVVLDVGAGSGILSF-FAVQAGAKKVYAVEAS-NMANHAELLVAANNLSDKIIVIAGKIEE-IDLPERVDCIVSEPMG 235
Cdd:TIGR02469  19 PGDVLWDIGAGTGSVTIeAARLVPNGRVYAIERNpEALDLIERNLRRFGVSNIVIVEGDAPEApEALLPDPDAVFVGGSG 98

                          90       100
                  ....*....|....*....|....*.
gi 340720716  236 ymlyneRMLETYLHA-KKWLVPGGRM 260
Cdd:TIGR02469  99 ------GLLQEILEAvERRLRPGGRI 118
PRK14968 PRK14968
putative methyltransferase; Provisional
 142-190 5.70e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 5.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 142 IRTSTYQRA-----ILGNLSDFKDKVVLDVGAGSGILSFFAVQAGAKKV------YAVEA 190
Cdd:PRK14968   1 LNDEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC 60
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 163-260 6.49e-03

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 38.85  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716  163 VLDVGAGSGILSFFAVQ-AGAKKVYAVEASNMANHAELLVAANNLSDKIIVIAGKIEeiDLPERVDCIVS----EPMGYm 237
Cdd:pfam02353  65 LLDIGCGWGGLMRRAAErYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYR--DFDEPFDRIVSvgmfEHVGH- 141

                          90       100
                  ....*....|....*....|....
gi 340720716  238 lynERmLETYLH-AKKWLVPGGRM 260
Cdd:pfam02353 142 ---EN-YDTFFKkLYNLLPPGGLM 161
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 152-220 7.82e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.28  E-value: 7.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340720716 152 LGNLSDFKDKVVLDVGAGSGILSFFAVQAGAkKVYAVE-ASNMANHAELLVAANNLSDKIIVIAGKIEEI 220
Cdd:PRK07580  56 LPADGDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESL 124
 
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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