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Conserved domains on  [gi|755552127|ref|XP_011244030|]
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methyltransferase-like protein 7A isoform X2 [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10549394)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Gene Ontology:  GO:0032259|GO:0008168|GO:0008757
PubMed:  12504684

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
75-166 2.34e-20

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


:

Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 81.17  E-value: 2.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   75 LEVGCGTGANFK-FYPPGCRVTCIDPNPNFEKFlfksVAENRQLQFERFVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQ 153
Cdd:pfam08241   1 LDVGCGTGLLTElLARLGARVTGVDISPEMLEL----AREKAPREGLTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEDP 75
                          90
                  ....*....|...
gi 755552127  154 EKILREVCRVLKP 166
Cdd:pfam08241  76 ERALREIARVLKP 88
 
Name Accession Description Interval E-value
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
75-166 2.34e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 81.17  E-value: 2.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   75 LEVGCGTGANFK-FYPPGCRVTCIDPNPNFEKFlfksVAENRQLQFERFVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQ 153
Cdd:pfam08241   1 LDVGCGTGLLTElLARLGARVTGVDISPEMLEL----AREKAPREGLTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEDP 75
                          90
                  ....*....|...
gi 755552127  154 EKILREVCRVLKP 166
Cdd:pfam08241  76 ERALREIARVLKP 88
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
64-166 6.88e-18

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: 76.19  E-value: 6.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  64 EFAGPSGKLTLLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKFLfKSVAENRQLQFErFVVAAGEDMHqVTDGSVDVVV 142
Cdd:COG2226   16 AALGLRPGARVLDLGCGTGRLaLALAERGARVTGVDISPEMLELA-RERAAEAGLNVE-FVVGDAEDLP-FPDGSFDLVI 92
                         90       100
                 ....*....|....*....|....
gi 755552127 143 CTLVLCSVKNQEKILREVCRVLKP 166
Cdd:COG2226   93 SSFVLHHLPDPERALAEIARVLKP 116
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
73-166 8.42e-14

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: 64.76  E-value: 8.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  73 TLLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLfKSVAENRQLQFERFVVAAGEDMHQVTDGSVDVVVCTLVL-CS 149
Cdd:cd02440    1 RVLDLGCGTGALALALasGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLhHL 79
                         90
                 ....*....|....*..
gi 755552127 150 VKNQEKILREVCRVLKP 166
Cdd:cd02440   80 VEDLARFLEEARRLLKP 96
PRK08317 PRK08317
hypothetical protein; Provisional
50-166 1.03e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.40  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  50 QMASQKRELFSNLQEFAGPSGkltlLEVGCGTGaNFKFY-----PPGCRVTCIDPNPNFEKFlfksvAENRQLQ---FER 121
Cdd:PRK08317   3 DFRRYRARTFELLAVQPGDRV----LDVGCGPG-NDARElarrvGPEGRVVGIDRSEAMLAL-----AKERAAGlgpNVE 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755552127 122 FVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:PRK08317  73 FVRGDADGL-PFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRP 116
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
50-166 2.49e-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: 46.51  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   50 QMASQKRELFSNLQEFAGPSgkltLLEVGCGTG----ANFKFYPPGcRVTCIDPNPNFEKFLFKSVAENRQlqferFVVA 125
Cdd:TIGR02072  18 EMAKRLLALLKEKGIFIPAS----VLDIGCGTGyltrALLKRFPQA-EFIALDISAGMLAQAKTKLSENVQ-----FICG 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 755552127  126 ageDMHQ--VTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:TIGR02072  88 ---DAEKlpLEDSSFDLIVSNLALQWCDDLSQALSELARVLKP 127
 
Name Accession Description Interval E-value
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
75-166 2.34e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 81.17  E-value: 2.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   75 LEVGCGTGANFK-FYPPGCRVTCIDPNPNFEKFlfksVAENRQLQFERFVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQ 153
Cdd:pfam08241   1 LDVGCGTGLLTElLARLGARVTGVDISPEMLEL----AREKAPREGLTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEDP 75
                          90
                  ....*....|...
gi 755552127  154 EKILREVCRVLKP 166
Cdd:pfam08241  76 ERALREIARVLKP 88
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
64-166 6.88e-18

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: 76.19  E-value: 6.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  64 EFAGPSGKLTLLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKFLfKSVAENRQLQFErFVVAAGEDMHqVTDGSVDVVV 142
Cdd:COG2226   16 AALGLRPGARVLDLGCGTGRLaLALAERGARVTGVDISPEMLELA-RERAAEAGLNVE-FVVGDAEDLP-FPDGSFDLVI 92
                         90       100
                 ....*....|....*....|....
gi 755552127 143 CTLVLCSVKNQEKILREVCRVLKP 166
Cdd:COG2226   93 SSFVLHHLPDPERALAEIARVLKP 116
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
75-166 6.76e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.21  E-value: 6.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   75 LEVGCGTGANFKFYPP--GCRVTCIDPNPNFEKFLfKSVAENRQLQFErFVVAAGEDMHqVTDGSVDVVVCTLVL--CSV 150
Cdd:pfam13649   2 LDLGCGTGRLTLALARrgGARVTGVDLSPEMLERA-RERAAEAGLNVE-FVQGDAEDLP-FPDGSFDLVVSSGVLhhLPD 78
                          90
                  ....*....|....*.
gi 755552127  151 KNQEKILREVCRVLKP 166
Cdd:pfam13649  79 PDLEAALREIARVLKP 94
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
75-166 1.04e-14

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 66.62  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   75 LEVGCGTGANFKF---YPPGCRVTCIDPNPNFEKFLFKSVAENRQLQFERfVVAAGEDMHQVTDGSVDVVVCTLVLCSVK 151
Cdd:pfam08242   1 LEIGCGTGTLLRAlleALPGLEYTGLDISPAALEAARERLAALGLLNAVR-VELFQLDLGELDPGSFDVVVASNVLHHLA 79
                          90
                  ....*....|....*
gi 755552127  152 NQEKILREVCRVLKP 166
Cdd:pfam08242  80 DPRAVLRNIRRLLKP 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
56-166 2.44e-14

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: 66.58  E-value: 2.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  56 RELFSNLQEFAGPSGKLtlLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKflfksVAENRQLQFE-RFVVAAGEDMhQV 133
Cdd:COG2227   12 RRLAALLARLLPAGGRV--LDVGCGTGRLaLALARRGADVTGVDISPEALE-----IARERAAELNvDFVQGDLEDL-PL 83
                         90       100       110
                 ....*....|....*....|....*....|...
gi 755552127 134 TDGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:COG2227   84 EDGSFDLVICSEVLEHLPDPAALLRELARLLKP 116
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
73-166 8.42e-14

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: 64.76  E-value: 8.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  73 TLLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLfKSVAENRQLQFERFVVAAGEDMHQVTDGSVDVVVCTLVL-CS 149
Cdd:cd02440    1 RVLDLGCGTGALALALasGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLhHL 79
                         90
                 ....*....|....*..
gi 755552127 150 VKNQEKILREVCRVLKP 166
Cdd:cd02440   80 VEDLARFLEEARRLLKP 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
68-166 8.67e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 60.51  E-value: 8.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   68 PSGKLTLLEVGCGTGA-NFKFYP---PGCRVTCIDpnpnFEKFLFKSVAEN-RQLQFERFVVAAG--EDM-HQVTDGSVD 139
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHlSFELAEelgPNAEVVGID----ISEEAIEKARENaQKLGFDNVEFEQGdiEELpELLEDDKFD 76
                          90       100
                  ....*....|....*....|....*..
gi 755552127  140 VVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:pfam13847  77 VVISNCVLNHIPDPDKVLQEILRVLKP 103
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
47-166 3.65e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 56.28  E-value: 3.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   47 YNEQMAsqkRELFSNLQEFAG--PSGKlTLLEVGCGTGANFK-FYPPGCRVTCIDPNPNfekflfksvAENRQLQFERFV 123
Cdd:pfam13489   1 YAHQRE---RLLADLLLRLLPklPSPG-RVLDFGCGTGIFLRlLRAQGFSVTGVDPSPI---------AIERALLNVRFD 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 755552127  124 VAAgEDMHQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:pfam13489  68 QFD-EQEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKP 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
73-166 8.55e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 53.67  E-value: 8.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  73 TLLEVGCGTGAN---FKFYPPGCRVTCIDPNPNFekflfksVAENRQLQFE-RFVVAageDMHQVT-DGSVDVVVCTLVL 147
Cdd:COG4106    4 RVLDLGCGTGRLtalLAERFPGARVTGVDLSPEM-------LARARARLPNvRFVVA---DLRDLDpPEPFDLVVSNAAL 73
                         90
                 ....*....|....*....
gi 755552127 148 CSVKNQEKILREVCRVLKP 166
Cdd:COG4106   74 HWLPDHAALLARLAAALAP 92
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
56-166 1.85e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 54.62  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  56 RELFSNLQEFAGPSGKLTLLEVGCGTGANFKFYPP-GCRVTCIDPNPNFekfLfkSVAENRQLQfERFVVAageDMHQVT 134
Cdd:COG4976   32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPrGYRLTGVDLSEEM---L--AKAREKGVY-DRLLVA---DLADLA 102
                         90       100       110
                 ....*....|....*....|....*....|....
gi 755552127 135 --DGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:COG4976  103 epDGRFDLIVAADVLTYLGDLAAVFAGVARALKP 136
PRK08317 PRK08317
hypothetical protein; Provisional
50-166 1.03e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.40  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  50 QMASQKRELFSNLQEFAGPSGkltlLEVGCGTGaNFKFY-----PPGCRVTCIDPNPNFEKFlfksvAENRQLQ---FER 121
Cdd:PRK08317   3 DFRRYRARTFELLAVQPGDRV----LDVGCGPG-NDARElarrvGPEGRVVGIDRSEAMLAL-----AKERAAGlgpNVE 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755552127 122 FVVAAGEDMhQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:PRK08317  73 FVRGDADGL-PFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRP 116
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
62-166 2.25e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.84  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  62 LQEFAGPSGKLTLLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLfKSVAENRQLQFERFVVAAGEDMHQVTDGSVD 139
Cdd:COG0500   18 LALLERLPKGGRVLDLGCGTGRNLLALaaRFGGRVIGIDLSPEAIALA-RARAAKAGLGNVEFLVADLAELDPLPAESFD 96
                         90       100
                 ....*....|....*....|....*....
gi 755552127 140 VVVCTLVLCSV--KNQEKILREVCRVLKP 166
Cdd:COG0500   97 LVVAFGVLHHLppEEREALLRELARALKP 125
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
73-166 2.07e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.39  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  73 TLLEVGCGTGANFKF----YppGCRVTCIDPNPNfekflfksvaenrQLQF-ERFVVAAG---------EDMHQVT-DGS 137
Cdd:COG2230   54 RVLDIGCGWGGLALYlarrY--GVRVTGVTLSPE-------------QLEYaRERAAEAGladrvevrlADYRDLPaDGQ 118
                         90       100       110
                 ....*....|....*....|....*....|.
gi 755552127 138 VDVVVCTLVLCSV--KNQEKILREVCRVLKP 166
Cdd:COG2230  119 FDAIVSIGMFEHVgpENYPAYFAKVARLLKP 149
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
50-166 2.49e-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: 46.51  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   50 QMASQKRELFSNLQEFAGPSgkltLLEVGCGTG----ANFKFYPPGcRVTCIDPNPNFEKFLFKSVAENRQlqferFVVA 125
Cdd:TIGR02072  18 EMAKRLLALLKEKGIFIPAS----VLDIGCGTGyltrALLKRFPQA-EFIALDISAGMLAQAKTKLSENVQ-----FICG 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 755552127  126 ageDMHQ--VTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:TIGR02072  88 ---DAEKlpLEDSSFDLIVSNLALQWCDDLSQALSELARVLKP 127
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
56-147 1.45e-04

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 41.48  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  56 RELFSNLQEfAGPSGK-LTLLEVGCGTG----ANFKFYPPGCRVTCIDPNP---NFEKFLFKSVAEN--RQLQFERFVVA 125
Cdd:COG5459   66 RAALAELAE-AGPDFApLTVLDVGAGPGtaawAAADAWPSLLDATLLERSAaalALGRRLARAAANPalETAEWRLADLA 144
                         90       100
                 ....*....|....*....|..
gi 755552127 126 AGEDmhqvtDGSVDVVVCTLVL 147
Cdd:COG5459  145 AALP-----APPADLVVASYVL 161
arsM PRK11873
arsenite methyltransferase;
133-166 4.84e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 39.93  E-value: 4.84e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 755552127 133 VTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:PRK11873 142 VADNSVDVIISNCVINLSPDKERVFKEAFRVLKP 175
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
49-166 6.55e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 39.36  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  49 EQMASQKRELFSNLQEFAGPSGKLTLLEVGCGTGANFKFY-PPGCRVTCIDPNPNFekflfksVAENRQLQFERFVVAAG 127
Cdd:PRK10258  21 EQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWrERGSQVTALDLSPPM-------LAQARQKDAADHYLAGD 93
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755552127 128 EDMHQVTDGSVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:PRK10258  94 IESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRP 132
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
67-166 1.23e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 38.57  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127   67 GPSGKLTLLEVGCGTGA-NFKFYP---PGCRVTCIDPNPNFEKFLFKSVAENRQLQFErFVVAAGEDMhQVTDGSVDVVV 142
Cdd:pfam01209  39 GVKRGNKFLDVAGGTGDwTFGLSDsagSSGKVVGLDINENMLKEGEKKAKEEGKYNIE-FLQGNAEEL-PFEDDSFDIVT 116
                          90       100
                  ....*....|....*....|....
gi 755552127  143 CTLVLCSVKNQEKILREVCRVLKP 166
Cdd:pfam01209 117 ISFGLRNFPDYLKVLKEAFRVLKP 140
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
66-166 2.62e-03

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.44  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755552127  66 AGPSGKLTLLEVGCGTG--ANF--KFYPPGCRVTCIDPNPNF-----EKFLfksvAENRQLQFErFVVAAGEDMhQVTDG 136
Cdd:PRK00216  47 LGVRPGDKVLDLACGTGdlAIAlaKAVGKTGEVVGLDFSEGMlavgrEKLR----DLGLSGNVE-FVQGDAEAL-PFPDN 120
                         90       100       110
                 ....*....|....*....|....*....|
gi 755552127 137 SVDVVVCTLVLCSVKNQEKILREVCRVLKP 166
Cdd:PRK00216 121 SFDAVTIAFGLRNVPDIDKALREMYRVLKP 150
 
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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