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Conserved domains on  [gi|1958789912|ref|XP_038935265|]
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methyltransferase-like protein 7A isoform X1 [Rattus norvegicus]

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 3.48e-19

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


:

Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 78.86  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  75 LEVGCGTGANFK-FYPPGCRVTCIDPNPNFEKFlfksVAENRHLQFERFLVAVGEDMhQVADGSVDVVVCTLVLCSVKSQ 153
Cdd:pfam08241   1 LDVGCGTGLLTElLARLGARVTGVDISPEMLEL----AREKAPREGLTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|...
gi 1958789912 154 EKILREVCRVLRP 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 3.48e-19

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 78.86  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  75 LEVGCGTGANFK-FYPPGCRVTCIDPNPNFEKFlfksVAENRHLQFERFLVAVGEDMhQVADGSVDVVVCTLVLCSVKSQ 153
Cdd:pfam08241   1 LDVGCGTGLLTElLARLGARVTGVDISPEMLEL----AREKAPREGLTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|...
gi 1958789912 154 EKILREVCRVLRP 166
Cdd:pfam08241  76 ERALREIARVLKP 88
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 54-166 4.09e-17

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: 75.03  E-value: 4.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  54 RKRELFSNLQEFAGpsgkLSLLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKFLfKSVAENRHLQFErFLVAVGEDMHq 132
Cdd:COG2226    10 GREALLAALGLRPG----ARVLDLGCGTGRLaLALAERGARVTGVDISPEMLELA-RERAAEAGLNVE-FVVGDAEDLP- 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958789912 133 VADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:COG2226    83 FPDGSFDLVISSFVLHHLPDPERALAEIARVLKP 116
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-166 1.72e-12

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: 61.68  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  74 LLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLFKSVAENRHLQFErFLVAVGEDMHQVADGSVDVVVCTLVL-CSV 150
Cdd:cd02440     2 VLDLGCGTGALALALasGPGARVTGVDISPVALELARKAAAALLADNVE-VLKGDAEELPPEADESFDVIISDPPLhHLV 80

                          90
                  ....*....|....*.
gi 1958789912 151 KSQEKILREVCRVLRP 166
Cdd:cd02440    81 EDLARFLEEARRLLKP 96
PRK08317 PRK08317
hypothetical protein; Provisional
 55-166 9.32e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.09  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  55 KRELFSNLQEFAGPSGklslLEVGCGTGaNFKFY-----PPGCRVTCIDPNPNFEKFlfksvAENR---HLQFERFLVAV 126
Cdd:PRK08317    8 RARTFELLAVQPGDRV----LDVGCGPG-NDARElarrvGPEGRVVGIDRSEAMLAL-----AKERaagLGPNVEFVRGD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958789912 127 GEDMhQVADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:PRK08317   78 ADGL-PFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRP 116
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 50-166 1.35e-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: 47.67  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  50 QMATRkreLFSNLQEFaGPSGKLSLLEVGCGTG----ANFKFYPPGcRVTCIDPNPNFEKFLFKSVAENRHlqferFLVA 125
Cdd:TIGR02072  18 EMAKR---LLALLKEK-GIFIPASVLDIGCGTGyltrALLKRFPQA-EFIALDISAGMLAQAKTKLSENVQ-----FICG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958789912 126 vgeDMHQ--VADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 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 3.48e-19

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 78.86  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  75 LEVGCGTGANFK-FYPPGCRVTCIDPNPNFEKFlfksVAENRHLQFERFLVAVGEDMhQVADGSVDVVVCTLVLCSVKSQ 153
Cdd:pfam08241   1 LDVGCGTGLLTElLARLGARVTGVDISPEMLEL----AREKAPREGLTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|...
gi 1958789912 154 EKILREVCRVLRP 166
Cdd:pfam08241  76 ERALREIARVLKP 88
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 54-166 4.09e-17

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: 75.03  E-value: 4.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  54 RKRELFSNLQEFAGpsgkLSLLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKFLfKSVAENRHLQFErFLVAVGEDMHq 132
Cdd:COG2226    10 GREALLAALGLRPG----ARVLDLGCGTGRLaLALAERGARVTGVDISPEMLELA-RERAAEAGLNVE-FVVGDAEDLP- 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958789912 133 VADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:COG2226    83 FPDGSFDLVISSFVLHHLPDPERALAEIARVLKP 116
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 75-166 5.27e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 70.67  E-value: 5.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  75 LEVGCGTGANFKFYPP--GCRVTCIDPNPNFEKFLfKSVAENRHLQFErFLVAVGEDMHqVADGSVDVVVCTLVL--CSV 150
Cdd:pfam13649   2 LDLGCGTGRLTLALARrgGARVTGVDLSPEMLERA-RERAAEAGLNVE-FVQGDAEDLP-FPDGSFDLVVSSGVLhhLPD 78

                          90
                  ....*....|....*.
gi 1958789912 151 KSQEKILREVCRVLRP 166
Cdd:pfam13649  79 PDLEAALREIARVLKP 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 56-166 1.08e-13

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: 65.42  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  56 RELFSNLQEFAGPSGKLslLEVGCGTGAN-FKFYPPGCRVTCIDPNPNFEKflfksVAENRHLQFE-RFLVAVGEDMhQV 133
Cdd:COG2227    12 RRLAALLARLLPAGGRV--LDVGCGTGRLaLALARRGADVTGVDISPEALE-----IARERAAELNvDFVQGDLEDL-PL 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958789912 134 ADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:COG2227    84 EDGSFDLVICSEVLEHLPDPAALLRELARLLKP 116
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-166 3.95e-13

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 63.16  E-value: 3.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  75 LEVGCGTGANFKF---YPPGCRVTCIDPNPNFEKFLFKSVAENRHLQFERfLVAVGEDMHQVADGSVDVVVCTLVLCSVK 151
Cdd:pfam08242   1 LEIGCGTGTLLRAlleALPGLEYTGLDISPAALEAARERLAALGLLNAVR-VELFQLDLGELDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*
gi 1958789912 152 SQEKILREVCRVLRP 166
Cdd:pfam08242  80 DPRAVLRNIRRLLKP 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-166 1.72e-12

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: 61.68  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  74 LLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLFKSVAENRHLQFErFLVAVGEDMHQVADGSVDVVVCTLVL-CSV 150
Cdd:cd02440     2 VLDLGCGTGALALALasGPGARVTGVDISPVALELARKAAAALLADNVE-VLKGDAEELPPEADESFDVIISDPPLhHLV 80

                          90
                  ....*....|....*.
gi 1958789912 151 KSQEKILREVCRVLRP 166
Cdd:cd02440    81 EDLARFLEEARRLLKP 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 68-166 7.91e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.50  E-value: 7.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  68 PSGKLSLLEVGCGTGA-NFKFYP---PGCRVTCIDpnpnFEKFLFKSVAEN-RHLQFERFLVAVG--EDM-HQVADGSVD 139
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHlSFELAEelgPNAEVVGID----ISEEAIEKARENaQKLGFDNVEFEQGdiEELpELLEDDKFD 76

                          90       100
                  ....*....|....*....|....*..
gi 1958789912 140 VVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:pfam13847  77 VVISNCVLNHIPDPDKVLQEILRVLKP 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
56-166 4.38e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.85  E-value: 4.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  56 RELFSNLQEFAGPSGKLSLLEVGCGTGANFKFYPP-GCRVTCIDPNPNFekfLfkSVAENRHLQfERFLVAvgeDMHQVA 134
Cdd:COG4976    32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPrGYRLTGVDLSEEM---L--AKAREKGVY-DRLLVA---DLADLA 102

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958789912 135 --DGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:COG4976   103 epDGRFDLIVAADVLTYLGDLAAVFAGVARALKP 136
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 54-166 9.78e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 52.82  E-value: 9.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  54 RKRELFSNLQEFAG--PSGKlSLLEVGCGTGANFK-FYPPGCRVTCIDPNPNFEkflFKSVAENRHLQFERFLVAVGEdm 130
Cdd:pfam13489   5 RERLLADLLLRLLPklPSPG-RVLDFGCGTGIFLRlLRAQGFSVTGVDPSPIAI---ERALLNVRFDQFDEQEAAVPA-- 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958789912 131 hqvadGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:pfam13489  79 -----GKFDVIVAREVLEHVPDPPALLRQIAALLKP 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
73-166 1.29e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 50.98  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  73 SLLEVGCGTGAN---FKFYPPGCRVTCIDPNPNF-EKflfksvAENRHLQFeRFLVAvgeDMHQVA-DGSVDVVVCTLVL 147
Cdd:COG4106     4 RVLDLGCGTGRLtalLAERFPGARVTGVDLSPEMlAR------ARARLPNV-RFVVA---DLRDLDpPEPFDLVVSNAAL 73

                          90
                  ....*....|....*....
gi 1958789912 148 CSVKSQEKILREVCRVLRP 166
Cdd:COG4106    74 HWLPDHAALLARLAAALAP 92
PRK08317 PRK08317
hypothetical protein; Provisional
 55-166 9.32e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.09  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  55 KRELFSNLQEFAGPSGklslLEVGCGTGaNFKFY-----PPGCRVTCIDPNPNFEKFlfksvAENR---HLQFERFLVAV 126
Cdd:PRK08317    8 RARTFELLAVQPGDRV----LDVGCGPG-NDARElarrvGPEGRVVGIDRSEAMLAL-----AKERaagLGPNVEFVRGD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958789912 127 GEDMhQVADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:PRK08317   78 ADGL-PFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRP 116
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 62-166 1.81e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.91  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  62 LQEFAGPSGKLSLLEVGCGTGANFKFY--PPGCRVTCIDPNPNFEKFLfKSVAENRHLQFERFLVAVGEDMHQVADGSVD 139
Cdd:COG0500    18 LALLERLPKGGRVLDLGCGTGRNLLALaaRFGGRVIGIDLSPEAIALA-RARAAKAGLGNVEFLVADLAELDPLPAESFD 96

                          90       100
                  ....*....|....*....|....*....
gi 1958789912 140 VVVCTLVLCSV--KSQEKILREVCRVLRP 166
Cdd:COG0500    97 LVVAFGVLHHLppEEREALLRELARALKP 125
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 50-166 1.35e-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: 47.67  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  50 QMATRkreLFSNLQEFaGPSGKLSLLEVGCGTG----ANFKFYPPGcRVTCIDPNPNFEKFLFKSVAENRHlqferFLVA 125
Cdd:TIGR02072  18 EMAKR---LLALLKEK-GIFIPASVLDIGCGTGyltrALLKRFPQA-EFIALDISAGMLAQAKTKLSENVQ-----FICG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958789912 126 vgeDMHQ--VADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:TIGR02072  88 ---DAEKlpLEDSSFDLIVSNLALQWCDDLSQALSELARVLKP 127
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 49-166 3.52e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.31  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  49 EQMATRKRELfsnLQEFAGPSGKLSLLEVGCGTGANFKF----YppGCRVTCIDPNPNFEKFlFKSVAENRHLQFE-RFL 123
Cdd:COG2230    33 EEAQEAKLDL---ILRKLGLKPGMRVLDIGCGWGGLALYlarrY--GVRVTGVTLSPEQLEY-ARERAAEAGLADRvEVR 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958789912 124 VAvgeDMHQV-ADGSVDVVVCTLVLCSV--KSQEKILREVCRVLRP 166
Cdd:COG2230   107 LA---DYRDLpADGQFDAIVSIGMFEHVgpENYPAYFAKVARLLKP 149
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 49-166 2.05e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 41.28  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  49 EQMATRKRELFSNLQEFAGPSGKLSLLEVGCGTGANFKFY-PPGCRVTCIDPNPNFekflfksVAENRHLQ-FERFLVAV 126
Cdd:PRK10258   21 EQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWrERGSQVTALDLSPPM-------LAQARQKDaADHYLAGD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958789912 127 GEDMhQVADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP 166
Cdd:PRK10258   94 IESL-PLATATFDLAWSNLAVQWCGNLSTALRELYRVVRP 132
arsM PRK11873
arsenite methyltransferase;
133-169 5.82e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 39.93  E-value: 5.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958789912 133 VADGSVDVVVCTLVLCSVKSQEKILREVCRVLRP-----VSD 169
Cdd:PRK11873  142 VADNSVDVIISNCVINLSPDKERVFKEAFRVLKPggrfaISD 183
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 56-147 1.13e-03

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: 39.17  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789912  56 RELFSNLQEfAGPSGK-LSLLEVGCGTG----ANFKFYPPGCRVTCIDPNP---NFEKFLFKSVAEN--RHLQFERFLVA 125
Cdd:COG5459    66 RAALAELAE-AGPDFApLTVLDVGAGPGtaawAAADAWPSLLDATLLERSAaalALGRRLARAAANPalETAEWRLADLA 144

                          90       100
                  ....*....|....*....|..
gi 1958789912 126 VGEdmhqvADGSVDVVVCTLVL 147
Cdd:COG5459   145 AAL-----PAPPADLVVASYVL 161
 
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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