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Conserved domains on  [gi|1327848381|ref|NP_001346467|]
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methyltransferase-like protein 27 isoform 2 [Mus musculus]

Protein Classification

class I SAM-dependent DNA methyltransferase( domain architecture ID 11471966)

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047
PubMed:  23180741|12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-127 9.85e-23

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


:

Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 90.06  E-value: 9.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976    11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                          90
                  ....*....|....*..
gi 1327848381 111 LYHHLSLCTLGQEPLPD 127
Cdd:COG4976    89 VYDRLLVADLADLAEPD 105
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-127 9.85e-23

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 90.06  E-value: 9.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976    11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                          90
                  ....*....|....*..
gi 1327848381 111 LYHHLSLCTLGQEPLPD 127
Cdd:COG4976    89 VYDRLLVADLADLAEPD 105
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-109 1.43e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.34  E-value: 1.43e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1327848381  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARAR 109
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARER 39
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 64-109 2.90e-08

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 52.15  E-value: 2.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1327848381  64 GSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARAR 109
Cdd:PRK07580   60 GDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDISPQMVEEARER 104
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-113 5.09e-07

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 48.41  E-value: 5.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  30 RFYDDWAPEYDQDVAALKYRAPRL----AVDCLsRAFRGSPhdalILDVACGTGLVAVELQARG--FLQVQGVDGSPEML 103
Cdd:TIGR01934   3 EMFDRIAPKYDLLNDLLSFGLHRLwrrrAVKLI-GVFKGQK----VLDVACGTGDLAIELAKSApdRGKVTGVDFSSEML 77

                          90
                  ....*....|
gi 1327848381 104 KQARARGLYH 113
Cdd:TIGR01934  78 EVAKKKSELP 87
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-120 1.84e-05

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: 42.42  E-value: 1.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327848381  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSLCTL 120
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEV 51
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-127 9.85e-23

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 90.06  E-value: 9.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976    11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                          90
                  ....*....|....*..
gi 1327848381 111 LYHHLSLCTLGQEPLPD 127
Cdd:COG4976    89 VYDRLLVADLADLAEPD 105
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-109 1.43e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.34  E-value: 1.43e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1327848381  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARAR 109
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARER 39
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 32-127 3.26e-11

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: 58.85  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  32 YDDWAPEYDQDVAALKYRAPRlavdclsrafrgspHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARGL 111
Cdd:COG2226     1 FDRVAARYDGREALLAALGLR--------------PGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAA 65

                          90       100
                  ....*....|....*....|
gi 1327848381 112 YHHLSLCTL----GQEPLPD 127
Cdd:COG2226    66 EAGLNVEFVvgdaEDLPFPD 85
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 66-132 1.75e-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: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  66 PHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARGL-----YHHLSLCTLGQEP--------------LP 126
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAelnvdFVQGDLEDLPLEDgsfdlvicsevlehLP 101


                  ....*.
gi 1327848381 127 DPEGGL 132
Cdd:COG2227   102 DPAALL 107
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-137 1.93e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 54.92  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  45 ALKYRAPRLAVDCLSRAFRGSPHDALILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSLCTL---- 120
Cdd:COG0500     4 SYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFlvad 83

                          90
                  ....*....|....*....
gi 1327848381 121 --GQEPLPDPEGGLVCLTT 137
Cdd:COG0500    84 laELDPLPAESFDLVVAFG 102
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
71-109 2.30e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.82  E-value: 2.30e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1327848381  71 ILDVACGTGLVAVELQARG-FLQVQGVDGSPEMLKQARAR 109
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARAR 44
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 64-109 2.90e-08

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 52.15  E-value: 2.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1327848381  64 GSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARAR 109
Cdd:PRK07580   60 GDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDISPQMVEEARER 104
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 72-127 3.24e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 46.89  E-value: 3.24e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327848381  72 LDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG-----LYHHLSLCTLgqePLPD 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKApreglTFVVGDAEDL---PFPD 57
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 33-117 4.07e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 49.00  E-value: 4.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  33 DDWAPEYDQ--DVAAL----KYRapRLAVDCLsrafrGSPHDALILDVACGTGLVAVEL--QARGFLQVQGVDGSPEMLK 104
Cdd:PRK00216   18 DSIAPKYDLmnDLLSFglhrVWR--RKTIKWL-----GVRPGDKVLDLACGTGDLAIALakAVGKTGEVVGLDFSEGMLA 90

                          90
                  ....*....|....*..
gi 1327848381 105 QARAR----GLYHHLSL 117
Cdd:PRK00216   91 VGREKlrdlGLSGNVEF 107
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-113 5.09e-07

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 48.41  E-value: 5.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  30 RFYDDWAPEYDQDVAALKYRAPRL----AVDCLsRAFRGSPhdalILDVACGTGLVAVELQARG--FLQVQGVDGSPEML 103
Cdd:TIGR01934   3 EMFDRIAPKYDLLNDLLSFGLHRLwrrrAVKLI-GVFKGQK----VLDVACGTGDLAIELAKSApdRGKVTGVDFSSEML 77

                          90
                  ....*....|
gi 1327848381 104 KQARARGLYH 113
Cdd:TIGR01934  78 EVAKKKSELP 87
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-120 1.84e-05

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: 42.42  E-value: 1.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327848381  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSLCTL 120
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEV 51
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 36-127 3.45e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 43.21  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  36 APEYDQDVAALKYRAPRLAVDCLSRAFrgsphdALILDVACGTGLVAVELQARGfLQVQGVDGSPEMLKQARARGLYHHL 115
Cdd:PRK10258   17 AAHYEQHAELQRQSADALLAMLPQRKF------THVLDAGCGPGWMSRYWRERG-SQVTALDLSPPMLAQARQKDAADHY 89

                          90
                  ....*....|..
gi 1327848381 116 SLCTLGQEPLPD 127
Cdd:PRK10258   90 LAGDIESLPLAT 101
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 71-109 6.64e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.45  E-value: 6.64e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1327848381  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARAR 109
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARER 93
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 72-131 8.80e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 40.04  E-value: 8.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327848381  72 LDVACGTGLVAVEL-QARGFLQVQGVDGSPEMLKQARARGL---YHHLSLCTLGQEPLPDPEGG 131
Cdd:pfam08242   1 LEIGCGTGTLLRALlEALPGLEYTGLDISPAALEAARERLAalgLLNAVRVELFQLDLGELDPG 64
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 35-111 7.76e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 39.29  E-value: 7.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327848381  35 WAPeyDQDVAALKYRApRLAVDCLSRAfrGSPHDALILDVACGTGLVAVELQAR-GFLQVQGVDGSPEMLKQARARGL 111
Cdd:PRK14103    2 WDP--DVYLAFADHRG-RPFYDLLARV--GAERARRVVDLGCGPGNLTRYLARRwPGAVIEALDSSPEMVAAARERGV 74
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-102 7.91e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.56  E-value: 7.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848381  46 LKYRAPRLAVDCLSRAFRGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEM 102
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF-SVTGVDPSPIA 56
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 34-109 1.07e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 38.77  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  34 DWAPE-YdqdvaaLKYRAPRL--AVDCLSRAfrgsPHDAL--ILDVACGTGLVAVELQAR-GFLQVQGVDGSPEMLKQAR 107
Cdd:PRK01683    3 DWNPSlY------LKFEDERTrpARDLLARV----PLENPryVVDLGCGPGNSTELLVERwPAARITGIDSSPAMLAEAR 72


                  ..
gi 1327848381 108 AR 109
Cdd:PRK01683   73 SR 74
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
71-168 1.31e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 38.57  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848381  71 ILDVACGTGLVAVEL--QARGFLQVQGVDGSPEMLKQARAR----GLYHHLSLCTLGQEpLPDPEGGLVCLTTRTNPSNL 144
Cdd:pfam01209  46 FLDVAGGTGDWTFGLsdSAGSSGKVVGLDINENMLKEGEKKakeeGKYNIEFLQGNAEE-LPFEDDSFDIVTISFGLRNF 124

                          90       100
                  ....*....|....*....|....*
gi 1327848381 145 P-YKETLEATLDSLERAGVWECLVT 168
Cdd:pfam01209 125 PdYLKVLKEAFRVLKPGGRVVCLEF 149
PRK08317 PRK08317
hypothetical protein; Provisional
 71-118 1.65e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 38.38  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327848381  71 ILDVACGTGLVAVELQAR----GflQVQGVDGSPEMLKQARARGLYHHLSLC 118
Cdd:PRK08317   23 VLDVGCGPGNDARELARRvgpeG--RVVGIDRSEAMLALAKERAAGLGPNVE 72
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
51-108 8.64e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 36.04  E-value: 8.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1327848381  51 PRLAVDCLSRAF-RGSPHDALILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARA 108
Cdd:COG2263    28 AELAAELLHLAYlRGDIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARE 86
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 63-133 9.14e-03

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: 36.11  E-value: 9.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848381  63 RGSPHDALILDVACGTGLVAVELQARgFLQVQ--GVDGSPEMLKQAR----ARGLYHHLSLCTLgqePLPDPEGGLV 133
Cdd:TIGR02072  30 KGIFIPASVLDIGCGTGYLTRALLKR-FPQAEfiALDISAGMLAQAKtklsENVQFICGDAEKL---PLEDSSFDLI 102
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 71-109 9.39e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 35.47  E-value: 9.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1327848381  71 ILDVACGTG----LVAVELQARGflQVQGVDGSPEMLKQARAR 109
Cdd:pfam13847   7 VLDLGCGTGhlsfELAEELGPNA--EVVGIDISEEAIEKAREN 47
 
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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