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Conserved domains on  [gi|29789323|ref|NP_598501|]
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protein arginine N-methyltransferase 3 [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10382869)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; contains a C2H2-type zinc finger

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047|GO:0008270
SCOP:  3000118

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];
227-390 2.39e-35

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: 132.08  E-value: 2.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 227 HEEMLKDKVRTESYRDFIYQnpHIFKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDQSEILYQ-AMDIIRLNKLEDTIVL 305
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAvARRIIAANGLSDRITV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 306 IKGKIEEVSLPvEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTislVAVSDVSKHADRIAFWDD-VY 384
Cdd:COG4076  90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERIT---NAAQPVESPVDAEGFEDWqFD 165

                ....*.
gi 29789323 385 GFNMSC 390
Cdd:COG4076 166 GFDFRL 171
zf-C2H2_2 super family cl20464
C2H2 type zinc-finger (2 copies); This family contains two copies of a C2H2-like zinc finger ...
48-97 8.27e-03

C2H2 type zinc-finger (2 copies); This family contains two copies of a C2H2-like zinc finger domain.


The actual alignment was detected with superfamily member pfam12756:

Pssm-ID: 463690  Cd Length: 98  Bit Score: 36.11  E-value: 8.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 29789323    48 CLFCDRLFASAEETFSHCKLEHQFNI---DSMVHKhglefygyIKLINFIRLK 97
Cdd:pfam12756   1 CLFCGHTSSTVEENLEHMFKSHGFFIperEYLVDL--------EGLLNYLREK 45
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
227-390 2.39e-35

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 132.08  E-value: 2.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 227 HEEMLKDKVRTESYRDFIYQnpHIFKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDQSEILYQ-AMDIIRLNKLEDTIVL 305
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAvARRIIAANGLSDRITV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 306 IKGKIEEVSLPvEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTislVAVSDVSKHADRIAFWDD-VY 384
Cdd:COG4076  90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERIT---NAAQPVESPVDAEGFEDWqFD 165

                ....*.
gi 29789323 385 GFNMSC 390
Cdd:COG4076 166 GFDFRL 171
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
256-356 4.91e-15

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: 70.92  E-value: 4.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 256 VLDVGCGTGILSMFAAKVGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSL-PVEKVDVIISEWMGYFL-- 332
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLve 81
                        90       100
                ....*....|....*....|....
gi 29789323 333 LFESMLDSVLyaksKYLAKGGSVY 356
Cdd:cd02440  82 DLARFLEEAR----RLLKPGGVLV 101
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
249-324 4.13e-13

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 69.03  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323  249 HIFKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDqseILYQAMDI----IRLNKLEDTIVLIKGKieevslpvEKVDVII 324
Cdd:PRK00517 116 LVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVD---IDPQAVEAarenAELNGVELNVYLPQGD--------LKADVIV 184
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
252-324 1.11e-10

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: 62.67  E-value: 1.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789323   252 KDKVVLDVGCGTGILSMFAAKVGAKKVIAVDqseILYQAMDI----IRLNKLEDTIVLIKGKieevSLPVEKVDVII 324
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAakenAELNGVEARLEVYLPG----DLPKEKADVVV 230
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
252-324 5.61e-09

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


Pssm-ID: 273061  Cd Length: 288  Bit Score: 57.54  E-value: 5.61e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789323   252 KDKVVLDVGCGTGILSMFAAKVGAKKVIAVD-QSEILYQAMDIIRLNKLEDTIVLIKGKIEEvslPVE-KVDVII 324
Cdd:TIGR00406 159 KDKNVIDVGCGSGILSIAALKLGAAKVVGIDiDPLAVESARKNAELNQVSDRLQVKLIYLEQ---PIEgKADVIV 230
zf-C2H2_2 pfam12756
C2H2 type zinc-finger (2 copies); This family contains two copies of a C2H2-like zinc finger ...
48-97 8.27e-03

C2H2 type zinc-finger (2 copies); This family contains two copies of a C2H2-like zinc finger domain.


Pssm-ID: 463690  Cd Length: 98  Bit Score: 36.11  E-value: 8.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 29789323    48 CLFCDRLFASAEETFSHCKLEHQFNI---DSMVHKhglefygyIKLINFIRLK 97
Cdd:pfam12756   1 CLFCGHTSSTVEENLEHMFKSHGFFIperEYLVDL--------EGLLNYLREK 45
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
227-390 2.39e-35

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 132.08  E-value: 2.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 227 HEEMLKDKVRTESYRDFIYQnpHIFKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDQSEILYQ-AMDIIRLNKLEDTIVL 305
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAvARRIIAANGLSDRITV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 306 IKGKIEEVSLPvEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTislVAVSDVSKHADRIAFWDD-VY 384
Cdd:COG4076  90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERIT---NAAQPVESPVDAEGFEDWqFD 165

                ....*.
gi 29789323 385 GFNMSC 390
Cdd:COG4076 166 GFDFRL 171
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
249-324 1.25e-15

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 77.14  E-value: 1.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 249 HIFKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDQSEilyQAMDI----IRLNKLEDTIVLIKGKIeevsLPVEKVDVII 324
Cdd:COG2264 145 LLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDP---VAVEAarenAELNGVEDRIEVVLGDL----LEDGPYDLVV 217
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
256-356 4.91e-15

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: 70.92  E-value: 4.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 256 VLDVGCGTGILSMFAAKVGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSL-PVEKVDVIISEWMGYFL-- 332
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLve 81
                        90       100
                ....*....|....*....|....
gi 29789323 333 LFESMLDSVLyaksKYLAKGGSVY 356
Cdd:cd02440  82 DLARFLEEAR----RLLKPGGVLV 101
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
249-324 4.13e-13

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 69.03  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323  249 HIFKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDqseILYQAMDI----IRLNKLEDTIVLIKGKieevslpvEKVDVII 324
Cdd:PRK00517 116 LVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVD---IDPQAVEAarenAELNGVELNVYLPQGD--------LKADVIV 184
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
247-325 2.34e-11

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 61.19  E-value: 2.34e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789323 247 NPHIFKDKVVLDVGCGTGILSMFAAKVGAkKVIAVDQSEilyQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIIS 325
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISP---EALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVIC 93
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
252-324 1.11e-10

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: 62.67  E-value: 1.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789323   252 KDKVVLDVGCGTGILSMFAAKVGAKKVIAVDqseILYQAMDI----IRLNKLEDTIVLIKGKieevSLPVEKVDVII 324
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAakenAELNGVEARLEVYLPG----DLPKEKADVVV 230
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
251-325 1.79e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 60.30  E-value: 1.79e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789323 251 FKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDqseILYQAMDIIRLN--KLEDTIVLIKGKIEEVSLpVEKVDVIIS 325
Cdd:COG2263  44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVD---IDPEALEIARENaeRLGVRVDFIRADVTRIPL-GGSVDTVVM 116
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
256-325 1.87e-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: 1.87e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789323   256 VLDVGCGTGILSMFAAKVGAKKVIAVDQSEI-LYQAMDiiRLNKLEDTIVLIKGKIEEVSLPVEKVDVIIS 325
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEmLERARE--RAAEAGLNVEFVQGDAEDLPFPDGSFDLVVS 69
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
256-325 2.23e-10

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: 60.93  E-value: 2.23e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789323 256 VLDVGCGTGILS-MFAAKVGAKKVIAVDQSEILY-QAMDIIRLNKLEDTIVLIKGKIEEVS--LPVEKVDVIIS 325
Cdd:COG4123  41 VLDLGTGTGVIAlMLAQRSPGARITGVEIQPEAAeLARRNVALNGLEDRITVIHGDLKEFAaeLPPGSFDLVVS 114
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
252-324 5.61e-09

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


Pssm-ID: 273061  Cd Length: 288  Bit Score: 57.54  E-value: 5.61e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789323   252 KDKVVLDVGCGTGILSMFAAKVGAKKVIAVD-QSEILYQAMDIIRLNKLEDTIVLIKGKIEEvslPVE-KVDVII 324
Cdd:TIGR00406 159 KDKNVIDVGCGSGILSIAALKLGAAKVVGIDiDPLAVESARKNAELNQVSDRLQVKLIYLEQ---PIEgKADVIV 230
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
252-325 1.12e-08

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 53.84  E-value: 1.12e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789323 252 KDKVVLDVGCGTGILSMFAAKVGAkKVIAVDQS-EILYQAMDiiRLNKLEDTIVLIKGKIEEVSLPVEKVDVIIS 325
Cdd:COG2226  22 PGARVLDLGCGTGRLALALAERGA-RVTGVDISpEMLELARE--RAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS 93
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
257-328 1.75e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.20  E-value: 1.75e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789323   257 LDVGCGTGILSMFAAKVGAkKVIAVDQSEilyQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISEWM 328
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISP---EMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEV 68
PRK14968 PRK14968
putative methyltransferase; Provisional
252-356 2.45e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 51.05  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323  252 KDKVVLDVGCGTGILSMFAAKVGaKKVIAVDQSEI-LYQAMDIIRLNKLEDTIVL---------IKGKIEEVS------L 315
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYaVECAKCNAKLNNIRNNGVEvirsdlfepFRGDKFDVIlfnppyL 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 29789323  316 PVEKvDVIISEWMGYFL--------LFESMLDSVlyakSKYLAKGGSVY 356
Cdd:PRK14968 102 PTEE-EEEWDDWLNYALsggkdgreVIDRFLDEV----GRYLKPGGRIL 145
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
250-365 4.16e-07

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 50.57  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323  250 IFKDKVVLDVGCGTGILSMFAAK-VGAK-KVIAVDQSEilyQAMDIIRLN----KLEDTIVLIKGKIEEVslpvekVDVI 323
Cdd:PRK00377  38 LRKGDMILDIGCGTGSVTVEASLlVGETgKVYAVDKDE---KAINLTRRNaekfGVLNNIVLIKGEAPEI------LFTI 108
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 29789323  324 ISEWMGYFLLFESM-LDSVLYAKSKYLAKGGSVYPDICTISLV 365
Cdd:PRK00377 109 NEKFDRIFIGGGSEkLKEIISASWEIIKKGGRIVIDAILLETV 151
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
248-343 4.72e-07

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 51.78  E-value: 4.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323  248 PHIF--KDKVVLDVGCGTG--ILSMFAAkvGAKKVIAVDQSEI-LYQAMDIIRLNKLEDTIVLIKGKIEEVSlPVEKVDV 322
Cdd:PRK15068 116 PHLSplKGRTVLDVGCGNGyhMWRMLGA--GAKLVVGIDPSQLfLCQFEAVRKLLGNDQRAHLLPLGIEQLP-ALKAFDT 192
                         90       100
                 ....*....|....*....|.
gi 29789323  323 IISewMGyfllfesmldsVLY 343
Cdd:PRK15068 193 VFS--MG-----------VLY 200
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
242-297 8.16e-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: 49.88  E-value: 8.16e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 29789323 242 DFIYQNPHIfKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDqseILYQAMDIIRLN 297
Cdd:COG3897  61 RYLLDHPEV-AGKRVLELGCGLGLVGIAAAKAGAADVTATD---YDPEALAALRLN 112
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
246-325 1.36e-06

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: 49.59  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323   246 QNPHIFKDKVVLDVGCGTGILS-MFAAKVGAKKVIAVDQSEI-LYQAMDIIRLNkledtIVLIKGKIEEVSLPVEKVDVI 323
Cdd:TIGR02072  28 KEKGIFIPASVLDIGCGTGYLTrALLKRFPQAEFIALDISAGmLAQAKTKLSEN-----VQFICGDAEKLPLEDSSFDLI 102

                  ..
gi 29789323   324 IS 325
Cdd:TIGR02072 103 VS 104
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
256-353 2.80e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 47.23  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 256 VLDVGCGTGILSMFAAKVGAKKVIAVDQSEILYQ-AMDIIRLNKLEDTIVLIKGKIEEVSLPvEKVDVIIS----EWMG- 329
Cdd:COG2230  55 VLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEyARERAAEAGLADRVEVRLADYRDLPAD-GQFDAIVSigmfEHVGp 133
                        90       100
                ....*....|....*....|....*.
gi 29789323 330 --YFLLFESMLDSvlyakskyLAKGG 353
Cdd:COG2230 134 enYPAYFAKVARL--------LKPGG 151
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
221-355 3.91e-06

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: 48.94  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323   221 YGHYGIHeemlkdkVRTESYRDFIYQN--PHI--FKDKVVLDVGCGTG--ILSMFAAkvGAKKVIAVDQSEI-LYQAMDI 293
Cdd:pfam08003  87 FHLFGVH-------IDTEWRSDWKWDRvlPHLspLKGRTILDVGCGNGyhMWRMLGE--GAAMVVGIDPSELfLCQFEAV 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789323   294 IRLNKLEDTIVLIKGKIEEVSlPVEKVDVIISewMGYFLLFESMLDSVLYAKSKyLAKGGSV 355
Cdd:pfam08003 158 RKLLGNDQRAHLLPLGIEQLP-ALAAFDTVFS--MGVLYHRRSPLDHLLQLKDQ-LVKGGEL 215
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
250-325 7.73e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.87  E-value: 7.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323   250 IFKDKVVLDVGCGTGILSMFAA-KVGAK-KVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEE--VSLPVEKVDVIIS 325
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAeELGPNaEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEElpELLEDDKFDVVIS 80
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
231-325 1.62e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 46.43  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323  231 LKDKvrteSYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKVgAKKVIAVDQSEILyqamdIIRLNKL---EDTIVLIK 307
Cdd:PRK14896  12 LIDD----RVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELDPRL-----AEFLRDDeiaAGNVEIIE 81
                         90
                 ....*....|....*...
gi 29789323  308 GKIEEVSLPveKVDVIIS 325
Cdd:PRK14896  82 GDALKVDLP--EFNKVVS 97
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
252-308 2.32e-05

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 46.71  E-value: 2.32e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 29789323 252 KDKVVLDVGCGTGILSMFAAKVGAKKVIAVDQSE-ILYQAMDIIRLNKLEDTIVLIKG 308
Cdd:COG1092 216 KGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSAtALEWAKENAALNGLDDRHEFVQA 273
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
256-325 2.70e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.89  E-value: 2.70e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789323 256 VLDVGCGTGILS-MFAAKVGAKKVIAVDQSEilyqAMdIIRLNKLEDTIVLIKGKIEEVSLPvEKVDVIIS 325
Cdd:COG4106   5 VLDLGCGTGRLTaLLAERFPGARVTGVDLSP----EM-LARARARLPNVRFVVADLRDLDPP-EPFDLVVS 69
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
252-326 2.98e-05

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 44.55  E-value: 2.98e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789323 252 KDKVVLDVGCGTGILSMFAAKVGAkKVIAVD-QSEILYQAMDIIRLNKLEDtIVLIKGKIEEVSLPVEKVDVIISE 326
Cdd:COG1041  26 EGDTVLDPFCGTGTILIEAGLLGR-RVIGSDiDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADESVDAIVTD 99
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
236-380 3.78e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 43.96  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323   236 RTESYRDFI-YQNPHIFKDKVVLDVGCGTGILSMFAAKVGAkKVIAVDQSEILYQAMDIIRLNKLEDtivlikgkIEEVS 314
Cdd:pfam13489   5 RERLLADLLlRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF-SVTGVDPSPIAIERALLNVRFDQFD--------EQEAA 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789323   315 LPVEKVDVIISewmgyFLLFESMLDSVLYAKS--KYLAKGGSVYpdictISLVAVSDvsKHADRIAFW 380
Cdd:pfam13489  76 VPAGKFDVIVA-----REVLEHVPDPPALLRQiaALLKPGGLLL-----LSTPLASD--EADRLLLEW 131
arsM PRK11873
arsenite methyltransferase;
255-325 4.86e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 45.32  E-value: 4.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789323  255 VVLDVGCGTGILSMFAA-KVGAK-KVIAVDQSEilyqAM-DIIRLN--KLEDTIV-LIKGKIEEVSLPVEKVDVIIS 325
Cdd:PRK11873  80 TVLDLGSGGGFDCFLAArRVGPTgKVIGVDMTP----EMlAKARANarKAGYTNVeFRLGEIEALPVADNSVDVIIS 152
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
252-355 5.66e-05

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


Pssm-ID: 426399  Cd Length: 179  Bit Score: 43.73  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323   252 KDKVVLDVGCGTGILSMFAAKVGAKKVIAVDqseILYQAMDIIRLNkleDTIVLIKGKIEEVS-------LPVEKVDVII 324
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGKVVGVD---LGPMQLWKPRND---PGVTFIQGDIRDPEtldlleeLLGRKVDLVL 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 29789323   325 SEwMGYFLLFESMLD---------SVLYAKSKYLAKGGSV 355
Cdd:pfam01728  95 SD-GSPFISGNKVLDhlrsldlvkAALEVALELLRKGGNF 133
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
238-325 6.00e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 43.83  E-value: 6.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 238 ESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKVGaKKVIAVDQSEilyqAM-DIIRLNKLEDTivLIKGKIEEVSLP 316
Cdd:COG4976  32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSE----EMlAKAREKGVYDR--LLVADLADLAEP 104

                ....*....
gi 29789323 317 VEKVDVIIS 325
Cdd:COG4976 105 DGRFDLIVA 113
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
256-356 6.00e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.14  E-value: 6.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 256 VLDVGCGTGILSMFAAKVGAKKVIAVDQS-EILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISewMGYF-LL 333
Cdd:COG0500  30 VLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNVEFLVADLAELDPLPAESFDLVVA--FGVLhHL 107
                        90       100
                ....*....|....*....|...
gi 29789323 334 FESMLDSVLYAKSKYLAKGGSVY 356
Cdd:COG0500 108 PPEEREALLRELARALKPGGVLL 130
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
249-356 6.11e-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: 43.92  E-value: 6.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 249 HIFKDKVVLDVGCGTGILSMFAAKVGAKKVIAVDQSeilYQAMDIIRLN----KLEDTIVLIKGKIEEV--SLPVEKVDV 322
Cdd:COG0742  38 PDIEGARVLDLFAGSGALGLEALSRGAASVVFVEKD---RKAAAVIRKNleklGLEDRARVIRGDALRFlkRLAGEPFDL 114
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 29789323 323 IisewmgyFL-------LFESMLDSVlyAKSKYLAKGGSVY 356
Cdd:COG0742 115 V-------FLdppyakgLLEKALELL--AENGLLAPGGLIV 146
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
250-324 2.62e-04

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: 42.84  E-value: 2.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 250 IFKDKVVLDVGCGTGILSMFAAK-VGAK-KVIAVDQSEilyQAMDIIRLN----KLEDTIVLIKGKIEEVsLPVEKVDVI 323
Cdd:COG2519  89 IFPGARVLEAGTGSGALTLALARaVGPEgKVYSYERRE---DFAEIARKNlerfGLPDNVELKLGDIREG-IDEGDVDAV 164

                .
gi 29789323 324 I 324
Cdd:COG2519 165 F 165
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
252-325 2.63e-04

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: 41.81  E-value: 2.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789323   252 KDKVVLDVGCGTGILSMFAAKVGAKkvIAVDQSEILYQAMDI----IRLNKLEDTIVLIKGKIEEVslPVEKVDVIIS 325
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPD--AELTMVDINARALESarenLAANGLENGEVVASDVYSGV--EDGKFDLIIS 104
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
255-342 3.43e-04

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 41.95  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323   255 VVLDVGCGTGILSMFAAKVG-AKKVIAVDQSEILYQAM-DIIRLNKLEDTIVLIKGKIEEVsLPVEKVDVIIsewMGYFL 332
Cdd:pfam02475 102 VVVDMFAGIGPFSIPIAKHSkARRVYAIELNPESYKYLkENIKLNKVEDVVKPILGDVREV-ILEDVADRVV---MNLPG 177
                          90
                  ....*....|
gi 29789323   333 LFESMLDSVL 342
Cdd:pfam02475 178 SAHEFLDKAF 187
PRK08317 PRK08317
hypothetical protein; Provisional
238-326 4.12e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 42.23  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323  238 ESYRDFIYQNPHIFKDKVVLDVGCGTGILSM-FAAKVGAK-KVIAVDQSEILYqAMDIIRLNKLEDTIVLIKGKIEEVSL 315
Cdd:PRK08317   5 RRYRARTFELLAVQPGDRVLDVGCGPGNDAReLARRVGPEgRVVGIDRSEAML-ALAKERAAGLGPNVEFVRGDADGLPF 83
                         90
                 ....*....|.
gi 29789323  316 PVEKVDVIISE 326
Cdd:PRK08317  84 PDGSFDAVRSD 94
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
252-285 4.49e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 41.75  E-value: 4.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 29789323  252 KDKVVLDVGCGTGILSMFAAKVGAkKVIAVDQSE 285
Cdd:PRK07580  63 TGLRILDAGCGVGSLSIPLARRGA-KVVASDISP 95
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
252-325 5.32e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.07  E-value: 5.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789323  252 KDKVVLDVGCGTGILS-MFAAKVGAKKVIAVDQSEilyQAMDIIRLN---KLEDTIVLIKGKIEEvSLPVEKVDVIIS 325
Cdd:PRK09328 108 EPLRVLDLGTGSGAIAlALAKERPDAEVTAVDISP---EALAVARRNakhGLGARVEFLQGDWFE-PLPGGRFDLIVS 181
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
256-325 5.37e-04

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: 41.33  E-value: 5.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 256 VLDVGCGTGILSMFAAKVGAK-KVIAVDQSEilyQAMDI----IRLNKLEDTIVLikgkieeVS-----LPVEKVDVIIS 325
Cdd:COG2813  53 VLDLGCGYGVIGLALAKRNPEaRVTLVDVNA---RAVELaranAAANGLENVEVL-------WSdglsgVPDGSFDLILS 122
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
252-308 6.01e-04

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


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 40.01  E-value: 6.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789323   252 KDKVVLDVGCGTGILSMFAAK-VGAKKVIAVDQSEilyQAMDIIRLNK---LEDTIVLIKG 308
Cdd:TIGR02469  19 PGDVLWDIGAGTGSVTIEAARlVPNGRVYAIERNP---EALDLIERNLrrfGVSNIVIVEG 76
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
244-325 9.87e-04

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


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 9.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323   244 IYQNPHIFKdkvVLDVGCGTGILSM-FAAKVGAKKVIAVDQS-EILYQAMDIIRLNKLEDTIVLIKGKIEEvSLPVEKVD 321
Cdd:TIGR00536 109 LISQPPILH---ILDLGTGSGCIALaLAYEFPNAEVIAVDISpDALAVAEENAEKNQLEHRVEFIQSNLFE-PLAGQKID 184

                  ....
gi 29789323   322 VIIS 325
Cdd:TIGR00536 185 IIVS 188
PRK14967 PRK14967
putative methyltransferase; Provisional
256-325 1.13e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 40.42  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789323  256 VLDVGCGTGILSMFAAKVGAKKVIAVDQSEilyQAMDIIRLNKLED--TIVLIKGKIEEVsLPVEKVDVIIS 325
Cdd:PRK14967  40 VLDLCTGSGALAVAAAAAGAGSVTAVDISR---RAVRSARLNALLAgvDVDVRRGDWARA-VEFRPFDVVVS 107
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
255-325 1.50e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.52  E-value: 1.50e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789323 255 VVLDVGCGTGILS-MFAAKVGAKKVIAVDQSEilyQAMDI----IRLNKLEDTIVLIKGKIEEVSLPVEKVDVIIS 325
Cdd:COG2890 115 RVLDLGTGSGAIAlALAKERPDARVTAVDISP---DALAVarrnAERLGLEDRVRFLQGDLFEPLPGDGRFDLIVS 187
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
257-353 2.10e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.73  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323   257 LDVGCGTG-ILSMFAAKVGAKKVIAVDQSEI-LYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIIsewMGYFLLF 334
Cdd:pfam08242   1 LEIGCGTGtLLRALLEALPGLEYTGLDISPAaLEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVV---ASNVLHH 77
                          90
                  ....*....|....*....
gi 29789323   335 ESMLDSVLYAKSKYLAKGG 353
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGG 96
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
253-353 3.00e-03

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 39.85  E-value: 3.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789323 253 DKVVLDVGCGTGILSMFAAKVGAKKVIAVDQSEILYQAMDI-IRLNKLEDTIVLIKGKIEEV-SLPVEKVDVIIsewMGY 330
Cdd:COG2520 181 GERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKEnIRLNKVEDRVTPILGDAREVaPELEGKADRII---MNL 257
                        90       100
                ....*....|....*....|...
gi 29789323 331 FLLFESMLDSVLYAkskyLAKGG 353
Cdd:COG2520 258 PHSADEFLDAALRA----LKPGG 276
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
254-324 4.17e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 39.12  E-value: 4.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789323 254 KVVLDVGCGTGILSMFAAKVGAKKVIAVDQSEIlyqAMDIIRLN----KLEDT-IVLIKGKIEEV--SLPVEKVDVII 324
Cdd:COG2521 134 DRVLDTCTGLGYTAIEALKRGAREVITVEKDPN---VLELAELNpwsrELANErIKIILGDASEVikTFPDESFDAII 208
zf-C2H2_2 pfam12756
C2H2 type zinc-finger (2 copies); This family contains two copies of a C2H2-like zinc finger ...
48-97 8.27e-03

C2H2 type zinc-finger (2 copies); This family contains two copies of a C2H2-like zinc finger domain.


Pssm-ID: 463690  Cd Length: 98  Bit Score: 36.11  E-value: 8.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 29789323    48 CLFCDRLFASAEETFSHCKLEHQFNI---DSMVHKhglefygyIKLINFIRLK 97
Cdd:pfam12756   1 CLFCGHTSSTVEENLEHMFKSHGFFIperEYLVDL--------EGLLNYLREK 45
 
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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