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Conserved domains on  [gi|8777361|dbj|BAA96951|]
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protein carboxyl methylase-like [Arabidopsis thaliana]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 13525419)

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:0008168|GO:1904047
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WBS_methylT pfam12589
Methyltransferase involved in Williams-Beuren syndrome; This domain family is found in ...
202-287 6.94e-27

Methyltransferase involved in Williams-Beuren syndrome; This domain family is found in eukaryotes, and is typically between 72 and 83 amino acids in length. The family is found in association with pfam08241. This family is made up of S-adenosylmethionine-dependent methyltransferases. The proteins are deleted in Williams-Beuren syndrome (WBS), a complex developmental disorder with multisystemic manifestations including supravalvular aortic stenosis (SVAS) and a specific cognitive phenotype.


:

Pssm-ID: 432656  Cd Length: 81  Bit Score: 100.01  E-value: 6.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361    202 LTCGTVQTSIQTSKNEYDESCSEddnsddeESEEVGVSDRNRPRKRQRTNTK--VKGREWVLRKKEQSRRKGKNVPADSK 279
Cdd:pfam12589   1 LFVGGVQQQLPKGLGEDGEECSE-------EQNTVKYERRRRPRKKRKKKGKkaVKGREWILRKKERRRRRGKDVPPDSK 73

                  ....*...
gi 8777361    280 FTSRKRRT 287
Cdd:pfam12589  74 YTGRKRKP 81
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
34-187 3.13e-15

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


:

Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 71.95  E-value: 3.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   34 AKLSERALELLALPEDgvpRFLLDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAVEREVEGDLLLGDMGQgLGLRSGV 113
Cdd:COG4976  32 ALLAEELLARLPPGPF---GRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLLVADLAD-LAEPDGR 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361  114 IDGAISISAVQWLcnADkssheprlrLKAFFGSLYRCLSRGARAVFQV--------YPENIAQrelILRQALQAGFG-GG 184
Cdd:COG4976 108 FDLIVAADVLTYL--GD---------LAAVFAGVARALKPGGLFIFSVedadgsgrYAHSLDY---VRDLLAAAGFEvPG 173

                ...
gi 8777361  185 LVV 187
Cdd:COG4976 174 LLV 176
 
Name Accession Description Interval E-value
WBS_methylT pfam12589
Methyltransferase involved in Williams-Beuren syndrome; This domain family is found in ...
202-287 6.94e-27

Methyltransferase involved in Williams-Beuren syndrome; This domain family is found in eukaryotes, and is typically between 72 and 83 amino acids in length. The family is found in association with pfam08241. This family is made up of S-adenosylmethionine-dependent methyltransferases. The proteins are deleted in Williams-Beuren syndrome (WBS), a complex developmental disorder with multisystemic manifestations including supravalvular aortic stenosis (SVAS) and a specific cognitive phenotype.


Pssm-ID: 432656  Cd Length: 81  Bit Score: 100.01  E-value: 6.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361    202 LTCGTVQTSIQTSKNEYDESCSEddnsddeESEEVGVSDRNRPRKRQRTNTK--VKGREWVLRKKEQSRRKGKNVPADSK 279
Cdd:pfam12589   1 LFVGGVQQQLPKGLGEDGEECSE-------EQNTVKYERRRRPRKKRKKKGKkaVKGREWILRKKERRRRRGKDVPPDSK 73

                  ....*...
gi 8777361    280 FTSRKRRT 287
Cdd:pfam12589  74 YTGRKRKP 81
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
34-187 3.13e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 71.95  E-value: 3.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   34 AKLSERALELLALPEDgvpRFLLDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAVEREVEGDLLLGDMGQgLGLRSGV 113
Cdd:COG4976  32 ALLAEELLARLPPGPF---GRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLLVADLAD-LAEPDGR 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361  114 IDGAISISAVQWLcnADkssheprlrLKAFFGSLYRCLSRGARAVFQV--------YPENIAQrelILRQALQAGFG-GG 184
Cdd:COG4976 108 FDLIVAADVLTYL--GD---------LAAVFAGVARALKPGGLFIFSVedadgsgrYAHSLDY---VRDLLAAAGFEvPG 173

                ...
gi 8777361  185 LVV 187
Cdd:COG4976 174 LLV 176
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
56-154 3.25e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.73  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361     56 LDIGCGSGLSGETLSED-GHHWIGLDISASMLHVAVER----EVEGDLLLGDMgQGLGLRSGVIDGAISISAVQWLCNAD 130
Cdd:pfam13649   2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERaaeaGLNVEFVQGDA-EDLPFPDGSFDLVVSSGVLHHLPDPD 80
                          90       100
                  ....*....|....*....|....
gi 8777361    131 kssheprlrLKAFFGSLYRCLSRG 154
Cdd:pfam13649  81 ---------LEAALREIARVLKPG 95
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
40-179 6.17e-10

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: 58.07  E-value: 6.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361     40 ALELLALPEDG---VPRFLLDIGCGSGLSGETLSE--DGHHWIGLDISASMLHVAVEREVEGDL-LLGDMGQgLGLRSGV 113
Cdd:TIGR02072  20 AKRLLALLKEKgifIPASVLDIGCGTGYLTRALLKrfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEK-LPLEDSS 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8777361    114 IDGAISISAVQWLCNadkssheprlrLKAFFGSLYRCLSRGARAVFQVY-PENIAQreliLRQALQA 179
Cdd:TIGR02072  99 FDLIVSNLALQWCDD-----------LSQALSELARVLKPGGLLAFSTFgPGTLHE----LRQSFGQ 150
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
20-192 1.37e-09

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 57.46  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361    20 ARKYTSSSrivEIQAKLSERALELLalPEDGVPRfLLDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAVEREVEGDLL 99
Cdd:PRK10258  17 AAHYEQHA---ELQRQSADALLAML--PQRKFTH-VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAADHYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   100 LGDMgQGLGLRSGVIDGAISISAVQWlCNAdkssheprlrLKAFFGSLYRCLSRGARAVFQvypeNIAQRELI-LRQALQ 178
Cdd:PRK10258  91 AGDI-ESLPLATATFDLAWSNLAVQW-CGN----------LSTALRELYRVVRPGGVVAFT----TLVQGSLPeLHQAWQ 154
                        170
                 ....*....|....
gi 8777361   179 AgfggglVVDYPHS 192
Cdd:PRK10258 155 A------VDERPHA 162
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
55-162 1.50e-07

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: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   55 LLDIGCGSGLSGETLSED-GHHWIGLDISASMLHVAVEREVEG-----DLLLGDMGQGLGLRSGVIDGAISISAVQWLCn 128
Cdd:cd02440   2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALladnvEVLKGDAEELPPEADESFDVIISDPPLHHLV- 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 8777361  129 adkssheprLRLKAFFGSLYRCLSRGARAVFQVY 162
Cdd:cd02440  81 ---------EDLARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
WBS_methylT pfam12589
Methyltransferase involved in Williams-Beuren syndrome; This domain family is found in ...
202-287 6.94e-27

Methyltransferase involved in Williams-Beuren syndrome; This domain family is found in eukaryotes, and is typically between 72 and 83 amino acids in length. The family is found in association with pfam08241. This family is made up of S-adenosylmethionine-dependent methyltransferases. The proteins are deleted in Williams-Beuren syndrome (WBS), a complex developmental disorder with multisystemic manifestations including supravalvular aortic stenosis (SVAS) and a specific cognitive phenotype.


Pssm-ID: 432656  Cd Length: 81  Bit Score: 100.01  E-value: 6.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361    202 LTCGTVQTSIQTSKNEYDESCSEddnsddeESEEVGVSDRNRPRKRQRTNTK--VKGREWVLRKKEQSRRKGKNVPADSK 279
Cdd:pfam12589   1 LFVGGVQQQLPKGLGEDGEECSE-------EQNTVKYERRRRPRKKRKKKGKkaVKGREWILRKKERRRRRGKDVPPDSK 73

                  ....*...
gi 8777361    280 FTSRKRRT 287
Cdd:pfam12589  74 YTGRKRKP 81
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
34-187 3.13e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 71.95  E-value: 3.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   34 AKLSERALELLALPEDgvpRFLLDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAVEREVEGDLLLGDMGQgLGLRSGV 113
Cdd:COG4976  32 ALLAEELLARLPPGPF---GRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLLVADLAD-LAEPDGR 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361  114 IDGAISISAVQWLcnADkssheprlrLKAFFGSLYRCLSRGARAVFQV--------YPENIAQrelILRQALQAGFG-GG 184
Cdd:COG4976 108 FDLIVAADVLTYL--GD---------LAAVFAGVARALKPGGLFIFSVedadgsgrYAHSLDY---VRDLLAAAGFEvPG 173

                ...
gi 8777361  185 LVV 187
Cdd:COG4976 174 LLV 176
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
36-181 1.31e-14

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: 69.25  E-value: 1.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   36 LSERALELLALPEDGVprfLLDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAVER----EVEGDLLLGDMGQgLGLRS 111
Cdd:COG2226  10 GREALLAALGLRPGAR---VLDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaeaGLNVEFVVGDAED-LPFPD 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361  112 GVIDGAISISAVQWLcnadksshePRLRlkAFFGSLYRCLSRGARAVFQVYpeNIAQRELILRQALQAGF 181
Cdd:COG2226  86 GSFDLVISSFVLHHL---------PDPE--RALAEIARVLKPGGRLVVVDF--SPPDLAELEELLAEAGF 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
52-161 9.01e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 60.22  E-value: 9.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   52 PRFLLDIGCGSGLSGETLSE--DGHHWIGLDISASMLHVAVEREVEGDLLLGDMGQgLGLRSGViDGAISISAVQWLCNa 129
Cdd:COG4106   2 PRRVLDLGCGTGRLTALLAErfPGARVTGVDLSPEMLARARARLPNVRFVVADLRD-LDPPEPF-DLVVSNAALHWLPD- 78
                        90       100       110
                ....*....|....*....|....*....|..
gi 8777361  130 dkssheprlrLKAFFGSLYRCLSRGARAVFQV 161
Cdd:COG4106  79 ----------HAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
56-154 3.25e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.73  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361     56 LDIGCGSGLSGETLSED-GHHWIGLDISASMLHVAVER----EVEGDLLLGDMgQGLGLRSGVIDGAISISAVQWLCNAD 130
Cdd:pfam13649   2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERaaeaGLNVEFVQGDA-EDLPFPDGSFDLVVSSGVLHHLPDPD 80
                          90       100
                  ....*....|....*....|....
gi 8777361    131 kssheprlrLKAFFGSLYRCLSRG 154
Cdd:pfam13649  81 ---------LEAALREIARVLKPG 95
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
40-190 3.89e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 61.09  E-value: 3.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   40 ALELLALPEDGVPRFLLDIGCGSGLSGETLSE-DGHHWIGLDISASMLHVAVEREVEG-----DLLLGDMGQGLGLRSGV 113
Cdd:COG0500  15 AALLALLERLPKGGRVLDLGCGTGRNLLALAArFGGRVIGIDLSPEAIALARARAAKAglgnvEFLVADLAELDPLPAES 94
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8777361  114 IDGAISISAVQWLcnadksshePRLRLKAFFGSLYRCLSRGARAVFQVYPENIAQRELILRQALQAGFGGGLVVDYP 190
Cdd:COG0500  95 FDLVVAFGVLHHL---------PPEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLRL 162
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
55-162 7.25e-11

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: 58.49  E-value: 7.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   55 LLDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAVER--EVEGDLLLGDMgQGLGLRSGVIDGAISISAVQWLcnadks 132
Cdd:COG2227  28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaELNVDFVQGDL-EDLPLEDGSFDLVICSEVLEHL------ 100
                        90       100       110
                ....*....|....*....|....*....|
gi 8777361  133 sHEPRlrlkAFFGSLYRCLSRGARAVFQVY 162
Cdd:COG2227 101 -PDPA----ALLRELARLLKPGGLLLLSTP 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
56-159 4.42e-10

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 55.36  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361     56 LDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAVER--EVEGDLLLGDMGQgLGLRSGVIDGAISISAVQWLcnadkss 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKapREGLTFVVGDAED-LPFPDNSFDLVLSSEVLHHV------- 72
                          90       100
                  ....*....|....*....|....*.
gi 8777361    134 HEPRlrlkAFFGSLYRCLSRGARAVF 159
Cdd:pfam08241  73 EDPE----RALREIARVLKPGGILII 94
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
40-179 6.17e-10

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: 58.07  E-value: 6.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361     40 ALELLALPEDG---VPRFLLDIGCGSGLSGETLSE--DGHHWIGLDISASMLHVAVEREVEGDL-LLGDMGQgLGLRSGV 113
Cdd:TIGR02072  20 AKRLLALLKEKgifIPASVLDIGCGTGYLTRALLKrfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEK-LPLEDSS 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8777361    114 IDGAISISAVQWLCNadkssheprlrLKAFFGSLYRCLSRGARAVFQVY-PENIAQreliLRQALQA 179
Cdd:TIGR02072  99 FDLIVSNLALQWCDD-----------LSQALSELARVLKPGGLLAFSTFgPGTLHE----LRQSFGQ 150
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
33-161 1.15e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 56.09  E-value: 1.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   33 QAKLsERALELLALPEDGVprfLLDIGCGSGLSGETLSED-GHHWIGLDISASMLHVAVEREVEGDL------LLGDMGQ 105
Cdd:COG2230  37 EAKL-DLILRKLGLKPGMR---VLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLadrvevRLADYRD 112
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8777361  106 gLGLRsGVIDGAISISAVQwlcnadkssHEPRLRLKAFFGSLYRCLSRGARAVFQV 161
Cdd:COG2230 113 -LPAD-GQFDAIVSIGMFE---------HVGPENYPAYFAKVARLLKPGGRLLLHT 157
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
20-192 1.37e-09

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 57.46  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361    20 ARKYTSSSrivEIQAKLSERALELLalPEDGVPRfLLDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAVEREVEGDLL 99
Cdd:PRK10258  17 AAHYEQHA---ELQRQSADALLAML--PQRKFTH-VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAADHYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   100 LGDMgQGLGLRSGVIDGAISISAVQWlCNAdkssheprlrLKAFFGSLYRCLSRGARAVFQvypeNIAQRELI-LRQALQ 178
Cdd:PRK10258  91 AGDI-ESLPLATATFDLAWSNLAVQW-CGN----------LSTALRELYRVVRPGGVVAFT----TLVQGSLPeLHQAWQ 154
                        170
                 ....*....|....
gi 8777361   179 AgfggglVVDYPHS 192
Cdd:PRK10258 155 A------VDERPHA 162
PRK08317 PRK08317
hypothetical protein; Provisional
38-158 1.11e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.48  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361    38 ERALELLAL-PEDGVprflLDIGCGSG-----LSGETlSEDGHhWIGLDISASMLHVAVEREVEG----DLLLGDmGQGL 107
Cdd:PRK08317   9 ARTFELLAVqPGDRV----LDVGCGPGndareLARRV-GPEGR-VVGIDRSEAMLALAKERAAGLgpnvEFVRGD-ADGL 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 8777361   108 GLRSGVIDGAISISAVQWLCNADKSSHEprlrlkaffgsLYRCLSRGARAV 158
Cdd:PRK08317  82 PFPDGSFDAVRSDRVLQHLEDPARALAE-----------IARVLRPGGRVV 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
55-162 1.50e-07

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: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361   55 LLDIGCGSGLSGETLSED-GHHWIGLDISASMLHVAVEREVEG-----DLLLGDMGQGLGLRSGVIDGAISISAVQWLCn 128
Cdd:cd02440   2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALladnvEVLKGDAEELPPEADESFDVIISDPPLHHLV- 80
                        90       100       110
                ....*....|....*....|....*....|....
gi 8777361  129 adkssheprLRLKAFFGSLYRCLSRGARAVFQVY 162
Cdd:cd02440  81 ---------EDLARFLEEARRLLKPGGVLVLTLV 105
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
17-92 5.01e-05

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 43.63  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8777361     17 DTEARKYTSSSRIVEIQAKLSE-----RALELLALPEDGVP-RFLLDIGCGSGLSGETLSEDGHHWIGLDISASMLHVAV 90
Cdd:TIGR02021  15 QRWARIYGSGDPVSRVRQTVREgraamRRKLLDWLPKDPLKgKRVLDAGCGTGLLSIELAKRGAIVKAVDISEQMVQMAR 94

                  ..
gi 8777361     91 ER 92
Cdd:TIGR02021  95 NR 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
56-92 1.20e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 40.43  E-value: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 8777361     56 LDIGCGSGLSGETLSEDGHHW--IGLDISASMLHVAVER 92
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARER 39
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
38-92 1.14e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 39.54  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8777361    38 ER---ALELLALPEDGVPRFLLDIGCGSGLSGETLSEdghHW-----IGLDISASMLHVAVER 92
Cdd:PRK01683  15 ERtrpARDLLARVPLENPRYVVDLGCGPGNSTELLVE---RWpaariTGIDSSPAMLAEARSR 74
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
55-92 1.77e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.98  E-value: 1.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 8777361    55 LLDIGCGSGLSGETLSEDGH---HWIGLDISASMLHVAVER 92
Cdd:PRK00216  55 VLDLACGTGDLAIALAKAVGktgEVVGLDFSEGMLAVGREK 95
 
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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