NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462533031|ref|XP_054228541|]
View 

protein arginine N-methyltransferase 8 isoform X4 [Homo sapiens]

Protein Classification

COG4076 superfamily protein( domain architecture ID 1905023)

COG4076 superfamily protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
86-208 3.51e-33

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: 119.76  E-value: 3.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031  86 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 164
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462533031 165 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWL 208
Cdd:COG4076    90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLL 132
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
86-208 3.51e-33

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 119.76  E-value: 3.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031  86 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 164
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462533031 165 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWL 208
Cdd:COG4076    90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLL 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
115-184 3.73e-10

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: 55.51  E-value: 3.73e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462533031 115 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIIS 184
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEElPPEADESFDVIIS 72
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
107-183 5.62e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 57.85  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031 107 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKIIKA-------NHLDNIITIFKGKveevelpvEKV 179
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV------DIDPQAVEAarenaelNGVELNVYLPQGD--------LKA 180

                  ....
gi 2462533031 180 DIII 183
Cdd:PRK00517  181 DVIV 184
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
108-183 3.12e-09

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: 56.12  E-value: 3.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533031 108 HVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKAN-HLDNIITIFKGKVEEvELPVEKVDIII 183
Cdd:pfam06325 158 LVKPGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAAKENaELNGVEARLEVYLPG-DLPKEKADVVV 230
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
89-183 4.22e-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: 36.15  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031  89 MLKDEVRTLTYRNSMYHnkhvfKDKVVLDVGSGTGILSMFAAKA-GAKKVFGIE-----CSSIsdysEKIIKANHLDNII 162
Cdd:TIGR02469   2 MTKREVRALTLAKLRLR-----PGDVLWDIGAGTGSVTIEAARLvPNGRVYAIErnpeaLDLI----ERNLRRFGVSNIV 72
                          90       100
                  ....*....|....*....|.
gi 2462533031 163 TIFKGKVEEVELPVEKVDIII 183
Cdd:TIGR02469  73 IVEGDAPEAPEALLPDPDAVF 93
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
86-208 3.51e-33

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 119.76  E-value: 3.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031  86 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 164
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462533031 165 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWL 208
Cdd:COG4076    90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLL 132
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
107-183 2.40e-13

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 67.51  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031 107 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKI----IKANHLDNIITIFKGKVeeveLPVEKVDII 182
Cdd:COG2264   144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVD---IDPVAVEAarenAELNGVEDRIEVVLGDL----LEDGPYDLV 216

                  .
gi 2462533031 183 I 183
Cdd:COG2264   217 V 217
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
106-184 2.50e-10

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 56.56  E-value: 2.50e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462533031 106 NKHVFKDKVVLDVGSGTGILSMFAAKAGAkKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIIS 184
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVD---ISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVIC 93
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
115-184 3.73e-10

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: 55.51  E-value: 3.73e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462533031 115 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIIS 184
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEElPPEADESFDVIIS 72
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
107-183 5.62e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 57.85  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031 107 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKIIKA-------NHLDNIITIFKGKveevelpvEKV 179
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV------DIDPQAVEAarenaelNGVELNVYLPQGD--------LKA 180

                  ....
gi 2462533031 180 DIII 183
Cdd:PRK00517  181 DVIV 184
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
108-183 3.12e-09

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: 56.12  E-value: 3.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533031 108 HVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKAN-HLDNIITIFKGKVEEvELPVEKVDIII 183
Cdd:pfam06325 158 LVKPGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAAKENaELNGVEARLEVYLPG-DLPKEKADVVV 230
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
115-184 5.26e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.18  E-value: 5.26e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462533031 115 VLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKII-----KANHLDNIITIFKGKVEEVELPVEKVDIIIS 184
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGV------DLSPEMLerareRAAEAGLNVEFVQGDAEDLPFPDGSFDLVVS 69
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
115-184 8.68e-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: 51.30  E-value: 8.68e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462533031 115 VLDVGSGTGILS-MFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNIITIFKGKVEEV--ELPVEKVDIIIS 184
Cdd:COG4123    41 VLDLGTGTGVIAlMLAQRSPGARITGVEIQPEAaELARRNVALNGLEDRITVIHGDLKEFaaELPPGSFDLVVS 114
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
110-184 2.19e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.52  E-value: 2.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533031 110 FKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKANH--LDNIITIFKGKVEEVELpVEKVDIIIS 184
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVD---IDPEALEIARENAerLGVRVDFIRADVTRIPL-GGSVDTVVM 116
PRK14968 PRK14968
putative methyltransferase; Provisional
111-191 7.52e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 45.27  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031 111 KDKVVLDVGSGTGILSMFAAKAGaKKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVEL--PV--EKVDIII--- 183
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKNG-KKVVGVD---INPYAVECAKCNAKLNNIRNNGVEVIRSDLfePFrgDKFDVILfnp 98
                          90
                  ....*....|....*....
gi 2462533031 184 -----------SEWMGYCL 191
Cdd:PRK14968   99 pylpteeeeewDDWLNYAL 117
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
111-184 7.97e-06

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: 44.21  E-value: 7.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462533031 111 KDKVVLDVGSGTGILSMFAAKAGAkKVFGIecssisDYSEKII-----KANHLDNIITIFKGKVEEVELPVEKVDIIIS 184
Cdd:COG2226    22 PGARVLDLGCGTGRLALALAERGA-RVTGV------DISPEMLelareRAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS 93
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
111-183 9.53e-06

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 45.94  E-value: 9.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462533031 111 KDKVVLDVGSGTGILSMFAAKAgAKKVFGIECS--SISDySEKIIKANHLDNiITIFKGKVEEV---ELPVEKVDIII 183
Cdd:COG2265   233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpeAVED-ARENARLNGLKN-VEFVAGDLEEVlpeLLWGGRPDVVV 307
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
116-187 1.54e-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: 1.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462533031 116 LDVGSGTGILSMFAAKAGAkKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWM 187
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVD---ISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEV 68
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
115-188 2.05e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 43.38  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031 115 VLDVGSGTGILSMFAAKAGAKKVFGIecsSIS----DYSEKIIKANHLDNIITIFKGKVEEVELPvEKVDIIIS----EW 186
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGV---TLSpeqlEYARERAAEAGLADRVEVRLADYRDLPAD-GQFDAIVSigmfEH 130

                  ..
gi 2462533031 187 MG 188
Cdd:COG2230   131 VG 132
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
115-184 1.34e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 41.44  E-value: 1.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462533031 115 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIIS 184
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGN-VEFLVADLAElDPLPAESFDLVVA 100
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
111-184 8.90e-04

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


Pssm-ID: 426399  Cd Length: 179  Bit Score: 39.11  E-value: 8.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533031 111 KDKVVLDVGSGTGILSMFAAKAGAKKVFGIecSSISDYSEKIIKANHLDNIIT-IFKGKVEE--VELPVEKVDIIIS 184
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGKVVGV--DLGPMQLWKPRNDPGVTFIQGdIRDPETLDllEELLGRKVDLVLS 95
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
109-184 1.32e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 39.11  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533031 109 VFKDKVVLDVGSGTGILSMFAAKAgAKKVFGIEC-SSISDYSEKIIKAnhlDNIITIFKGKVEEVELPveKVDIIIS 184
Cdd:PRK14896   27 DTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIA---AGNVEIIEGDALKVDLP--EFNKVVS 97
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
111-184 1.95e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.78  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031 111 KDKVVLDVGSGTGILSMFAAK--AGAKKVFGIE--CSSISdYSEKIIKANHLDNiITIFKGKVEEVELPVE--KVDIIIS 184
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDisEEAIE-KARENAQKLGFDN-VEFEQGDIEELPELLEddKFDVVIS 80
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
115-165 2.78e-03

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 37.73  E-value: 2.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462533031 115 VLDVGSGTGILS-MFAAKAGAK-KVFGIECS-SISDYSEKIIKANHLDNIITIF 165
Cdd:pfam01135  77 VLEIGSGSGYLTaCFARMVGEVgRVVSIEHIpELVEIARRNLEKLGLENVIVVV 130
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
89-183 4.22e-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: 36.15  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031  89 MLKDEVRTLTYRNSMYHnkhvfKDKVVLDVGSGTGILSMFAAKA-GAKKVFGIE-----CSSIsdysEKIIKANHLDNII 162
Cdd:TIGR02469   2 MTKREVRALTLAKLRLR-----PGDVLWDIGAGTGSVTIEAARLvPNGRVYAIErnpeaLDLI----ERNLRRFGVSNIV 72
                          90       100
                  ....*....|....*....|.
gi 2462533031 163 TIFKGKVEEVELPVEKVDIII 183
Cdd:TIGR02469  73 IVEGDAPEAPEALLPDPDAVF 93
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
70-184 4.41e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 36.90  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031  70 MTSRDY---YFDSYAHfgIHEEMLkdeVRTLTYRNSMYHNKHVF------KDKVVLDVGSGTGILSMFAAKAGaKKVFGI 140
Cdd:COG4976     1 MALDAYveaLFDQYAD--SYDAAL---VEDLGYEAPALLAEELLarlppgPFGRVLDLGCGTGLLGEALRPRG-YRLTGV 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462533031 141 ecssisDYSEKII---KANHLDniITIFKGKVEEVELPVEKVDIIIS 184
Cdd:COG4976    75 ------DLSEEMLakaREKGVY--DRLLVADLADLAEPDGRFDLIVA 113
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
111-184 4.65e-03

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: 36.80  E-value: 4.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462533031 111 KDKVVLDVGSGTGILSMFAAKAGAKKVfgIECSSISDY----SEKIIKANHLDNiITIFKGKVEEvELPVEKVDIIIS 184
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPDAE--LTMVDINARalesARENLAANGLEN-GEVVASDVYS-GVEDGKFDLIIS 104
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
89-172 5.45e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 36.70  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031  89 MLKDEVRTLTYRNSmyhnkHVFKDKVVLDVGSGTGILSMFAAK-AGAK-KVFGIecssisDYSEKII--------KANHL 158
Cdd:PRK00377   23 MTKEEIRALALSKL-----RLRKGDMILDIGCGTGSVTVEASLlVGETgKVYAV------DKDEKAInltrrnaeKFGVL 91
                          90
                  ....*....|....
gi 2462533031 159 DNIITIfKGKVEEV 172
Cdd:PRK00377   92 NNIVLI-KGEAPEI 104
arsM PRK11873
arsenite methyltransferase;
114-184 7.28e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 36.85  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533031 114 VVLDVGSGTGILSMFAAKA-GAK-KVFGIecssisDYSEKII---KANH----LDNiITIFKGKVEEVELPVEKVDIIIS 184
Cdd:PRK11873   80 TVLDLGSGGGFDCFLAARRvGPTgKVIGV------DMTPEMLakaRANArkagYTN-VEFRLGEIEALPVADNSVDVIIS 152
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH