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Conserved domains on  [gi|517257663|ref|WP_018446481|]
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MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Rhizobium]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-136 1.76e-17

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: 74.67  E-value: 1.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  28 RLDAFLAGLAP-GAAILELGCGGGQDSAYMLSQGFDVMPTDGSAKLARQAEVLIGRP---VRVMLFQELD-ADSAFDGVW 102
Cdd:COG2227   13 RLAALLARLLPaGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELnvdFVQGDLEDLPlEDGSFDLVI 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 517257663 103 AQASLLHVPrrELPDVFARIRRALRTGGIIHATF 136
Cdd:COG2227   93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLST 124
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-136 1.76e-17

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: 74.67  E-value: 1.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  28 RLDAFLAGLAP-GAAILELGCGGGQDSAYMLSQGFDVMPTDGSAKLARQAEVLIGRP---VRVMLFQELD-ADSAFDGVW 102
Cdd:COG2227   13 RLAALLARLLPaGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELnvdFVQGDLEDLPlEDGSFDLVI 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 517257663 103 AQASLLHVPrrELPDVFARIRRALRTGGIIHATF 136
Cdd:COG2227   93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 42-130 7.98e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 7.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   42 ILELGCGGGQDSAYMLSQ-GFDVMPTDGSA---KLARQAEVLIGRPVRVML--FQELD-ADSAFDGVWAQASLLHVPRRE 114
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPemlERARERAAEAGLNVEFVQgdAEDLPfPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 517257663  115 LPDVFARIRRALRTGG 130
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 42-136 6.14e-08

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: 48.97  E-value: 6.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  42 ILELGCGGGQDSAYMLSQ------GFDVMPtdGSAKLARQAEvLIGRPVRVMLFQ------ELDADSAFDGVWAQASLLH 109
Cdd:cd02440    2 VLDLGCGTGALALALASGpgarvtGVDISP--VALELARKAA-AALLADNVEVLKgdaeelPPEADESFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*..
gi 517257663 110 VPRReLPDVFARIRRALRTGGIIHATF 136
Cdd:cd02440   79 LVED-LARFLEEARRLLKPGGVLVLTL 104
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
36-130 9.36e-05

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 41.64  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  36 LAPGAAiLELGCGGGQDSAYMLSQGFDVMPTDGS-AKLAR-----QAEVLIGRPVRVMLFQELDADSAFDGVWAQASLLH 109
Cdd:PRK11207  29 VKPGKT-LDLGCGNGRNSLYLAANGFDVTAWDKNpMSIANlerikAAENLDNLHTAVVDLNNLTFDGEYDFILSTVVLMF 107

                         90       100
                 ....*....|....*....|.
gi 517257663 110 VPRRELPDVFARIRRALRTGG 130
Cdd:PRK11207 108 LEAKTIPGLIANMQRCTKPGG 128
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-136 1.76e-17

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: 74.67  E-value: 1.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  28 RLDAFLAGLAP-GAAILELGCGGGQDSAYMLSQGFDVMPTDGSAKLARQAEVLIGRP---VRVMLFQELD-ADSAFDGVW 102
Cdd:COG2227   13 RLAALLARLLPaGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELnvdFVQGDLEDLPlEDGSFDLVI 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 517257663 103 AQASLLHVPrrELPDVFARIRRALRTGGIIHATF 136
Cdd:COG2227   93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLST 124
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 6-134 1.43e-16

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 73.04  E-value: 1.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   6 TSAFYEENAETYvnraRSLPKQRLDAFL--AGLAPGAAILELGCGGGQDSAYMLSQ-GFDVMPTDGS---AKLARQ--AE 77
Cdd:COG2230   21 SCAYFEDPDDTL----EEAQEAKLDLILrkLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSpeqLEYAREraAE 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517257663  78 VLIGRPVRVML--FQELDADSAFDGVWAQASLLHVPRRELPDVFARIRRALRTGG--IIHA 134
Cdd:COG2230   97 AGLADRVEVRLadYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGrlLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
6-166 1.34e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 71.18  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   6 TSAFYEENAETY-----VNRARSLPKQRLDAFLAGLAPGAA--ILELGCGGGQDSAYMLSQGFDVMPTDGSAKLARQAEv 78
Cdd:COG4976    7 VEALFDQYADSYdaalvEDLGYEAPALLAEELLARLPPGPFgrVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  79 liGRPVRVMLFQ----ELDA-DSAFDGVWAQASLLHVPrrELPDVFARIRRALRTGGIIHATFKAGDAEGHdsfgryYNY 153
Cdd:COG4976   86 --EKGVYDRLLVadlaDLAEpDGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIFSVEDADGSGR------YAH 155

                        170
                 ....*....|...
gi 517257663 154 PSAEWLSELLTNG 166
Cdd:COG4976  156 SLDYVRDLLAAAG 168
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 10-132 7.02e-15

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: 68.10  E-value: 7.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  10 YEENAETYVNRARSLPkqrldafLAGLAPGAAILELGCGGGQDSAYMLSQGFDVMPTDGSAKLARQAEVLIGRPVRVMLF 89
Cdd:COG2226    1 FDRVAARYDGREALLA-------ALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEF 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 517257663  90 QELDA------DSAFDGVWAQASLLHVPRRElpDVFARIRRALRTGGII 132
Cdd:COG2226   74 VVGDAedlpfpDGSFDLVISSFVLHHLPDPE--RALAEIARVLKPGGRL 120
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
38-136 2.46e-14

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 65.62  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  38 PGAAILELGCGGGQDSAYMLSQ--GFDVMPTDGSAKLARQAEVLIGR-PVRVMLFQELDADSAFDGVWAQASLLHVPrrE 114
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNvRFVVADLRDLDPPEPFDLVVSNAALHWLP--D 78

                         90       100
                 ....*....|....*....|..
gi 517257663 115 LPDVFARIRRALRTGGIIHATF 136
Cdd:COG4106   79 HAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 42-130 7.98e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 7.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   42 ILELGCGGGQDSAYMLSQ-GFDVMPTDGSA---KLARQAEVLIGRPVRVML--FQELD-ADSAFDGVWAQASLLHVPRRE 114
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPemlERARERAAEAGLNVEFVQgdAEDLPfPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 517257663  115 LPDVFARIRRALRTGG 130
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 43-132 1.23e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 63.84  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   43 LELGCGGGQDSAYMLSQGFDVMPTDGSAKLARQAEVLIGRP---VRVMLFQELD-ADSAFDGVWAQASLLHVPRRElpDV 118
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREgltFVVGDAEDLPfPDNSFDLVLSSEVLHHVEDPE--RA 78

                          90
                  ....*....|....
gi 517257663  119 FARIRRALRTGGII 132
Cdd:pfam08241  79 LREIARVLKPGGIL 92
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 15-168 2.80e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.46  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  15 ETYVNRARSLPKQRLDAFLAGLAPGAAILELGCGGGQDSAYMLSQ------GFDVMPtDGSAKLARQAEVLIGRPVRVML 88
Cdd:COG0500    3 DSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARfggrviGIDLSP-EAIALARARAAKAGLGNVEFLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  89 -----FQELDADSaFDGVWAQASLLHVPRRELPDVFARIRRALRTGGIIHATFkAGDAEGHDSFGRYYNYPSAEWLSELL 163
Cdd:COG0500   82 adlaeLDPLPAES-FDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSA-SDAAAALSLARLLLLATASLLELLLL 159


                 ....*
gi 517257663 164 TNGGW 168
Cdd:COG0500  160 LRLLA 164
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 42-136 6.14e-08

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: 48.97  E-value: 6.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  42 ILELGCGGGQDSAYMLSQ------GFDVMPtdGSAKLARQAEvLIGRPVRVMLFQ------ELDADSAFDGVWAQASLLH 109
Cdd:cd02440    2 VLDLGCGTGALALALASGpgarvtGVDISP--VALELARKAA-AALLADNVEVLKgdaeelPPEADESFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*..
gi 517257663 110 VPRReLPDVFARIRRALRTGGIIHATF 136
Cdd:cd02440   79 LVED-LARFLEEARRLLKPGGVLVLTL 104
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 10-131 5.59e-05

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 42.70  E-value: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   10 YEENAETYVNRARSLpKQRLDAFLAGLAPGAAILELGCGGGQDSAYMLSQ-GFDVMP---TDGSAKLARQ--AEVLIGRP 83
Cdd:pfam02353  34 YFERPDMTLEEAQQA-KLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERyDVNVVGltlSKNQYKLARKrvAAEGLARK 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 517257663   84 VRVMLFQELDADSAFDGVWAQASLLHVPRRELPDVFARIRRALRTGGI 131
Cdd:pfam02353 113 VEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 43-132 7.62e-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: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   43 LELGCGGGQDSAYMLSQ-------GFDvmPTDGSAKLARQ--AEVLIGRPVRVMLFQELDADS---AFDGVWAQASLLHV 110
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpgleytGLD--ISPAALEAARErlAALGLLNAVRVELFQLDLGELdpgSFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|..
gi 517257663  111 PRRElpDVFARIRRALRTGGII 132
Cdd:pfam08242  79 ADPR--AVLRNIRRLLKPGGVL 98
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
36-130 9.36e-05

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 41.64  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  36 LAPGAAiLELGCGGGQDSAYMLSQGFDVMPTDGS-AKLAR-----QAEVLIGRPVRVMLFQELDADSAFDGVWAQASLLH 109
Cdd:PRK11207  29 VKPGKT-LDLGCGNGRNSLYLAANGFDVTAWDKNpMSIANlerikAAENLDNLHTAVVDLNNLTFDGEYDFILSTVVLMF 107

                         90       100
                 ....*....|....*....|.
gi 517257663 110 VPRRELPDVFARIRRALRTGG 130
Cdd:PRK11207 108 LEAKTIPGLIANMQRCTKPGG 128
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 17-172 1.18e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 40.87  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   17 YVNRARSLPKQRLDAFLAGLAPGAAILELGCGGGQDSAYMLSQGFDVMPTDGSaklARQAEVLIGRPVRVMLFQELDADS 96
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPS---PIAIERALLNVRFDQFDEQEAAVP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   97 A--FDGVWAQASLLHVPrrELPDVFARIRRALRTGG-IIHATFKAGDAEGH--------DSFGRYYNYPSAEWLSELLTN 165
Cdd:pfam13489  78 AgkFDVIVAREVLEHVP--DPPALLRQIAALLKPGGlLLLSTPLASDEADRlllewpylRPRNGHISLFSARSLKRLLEE 155


                  ....*..
gi 517257663  166 GGWGNIA 172
Cdd:pfam13489 156 AGFEVVS 162
PRK08317 PRK08317
hypothetical protein; Provisional
 26-130 1.29e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 41.46  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  26 KQRLDAFLAgLAPGAAILELGCGGGQDSAYMLSQgfdVMPT------DGSAKL---ARQAEVLIGRPVRVML--FQELD- 93
Cdd:PRK08317   8 RARTFELLA-VQPGDRVLDVGCGPGNDARELARR---VGPEgrvvgiDRSEAMlalAKERAAGLGPNVEFVRgdADGLPf 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 517257663  94 ADSAFDGVWAQASLLHVPrrELPDVFARIRRALRTGG 130
Cdd:PRK08317  84 PDGSFDAVRSDRVLQHLE--DPARALAEIARVLRPGG 118
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 36-130 3.80e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.42  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  36 LAPGAAILELGCGGGQDSAYMlSQGFD--VMPTDGSAKLARQA-EVLIGRPVRVMlFQELDA------DSAFDGVWAQAS 106
Cdd:PLN02336 264 LKPGQKVLDVGCGIGGGDFYM-AENFDvhVVGIDLSVNMISFAlERAIGRKCSVE-FEVADCtkktypDNSFDVIYSRDT 341

                         90       100
                 ....*....|....*....|....
gi 517257663 107 LLHVprRELPDVFARIRRALRTGG 130
Cdd:PLN02336 342 ILHI--QDKPALFRSFFKWLKPGG 363
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 42-135 4.36e-03

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 36.65  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663  42 ILELGCGGGQDSAYMLSQ-------GFDVMpTDGSAKLARQAEVLiGRP-VRVM-----LFQELDADSAFDGVWaqasLL 108
Cdd:COG0220   36 VLEIGFGKGEFLVELAAAnpdinfiGIEVH-EPGVAKALKKAEEE-GLTnVRLLrgdavELLELFPDGSLDRIY----LN 109

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517257663 109 ---------HVPRReL--PDVFARIRRALRTGGIIH-AT 135
Cdd:COG0220  110 fpdpwpkkrHHKRR-LvqPEFLALLARVLKPGGELHlAT 147
TehB pfam03848
Tellurite resistance protein TehB;
36-130 5.80e-03

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 36.37  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517257663   36 LAPGAAiLELGCGGGQDSAYMLSQGFDVMPTD------GSAKLARQAEVLIGRPVRVMLFQELDADSAFDGVWAQASLLH 109
Cdd:pfam03848  29 VKPGKV-LDLGCGQGRNSLYLSLLGYDVTAWDknensiANLQRIKEKENLDNIHTALYDINNATIDENYDFILSTVVLMF 107

                          90       100
                  ....*....|....*....|.
gi 517257663  110 VPRRELPDVFARIRRALRTGG 130
Cdd:pfam03848 108 LEPERIPGIIANMQECTNPGG 128
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 42-67 8.20e-03

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 36.07  E-value: 8.20e-03
                         10        20
                 ....*....|....*....|....*.
gi 517257663  42 ILELGCGGGQDSAYMLSQGFDVMPTD 67
Cdd:PRK12335 124 ALDLGCGQGRNSLYLALLGFDVTAVD 149
 
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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