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Conserved domains on  [gi|585110982|gb|EWM28564|]
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Protein of unknown function DUF3321 [Nannochloropsis gaditana]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 53-260 1.30e-38

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.).


The actual alignment was detected with superfamily member pfam11968:

Pssm-ID: 473071  Cd Length: 221  Bit Score: 134.68  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982   53 SRLQESLEALGGRAAYQSASQLSVSFH---STSKWVLARLQAMGIIrmqsapslSPSQPSQKpRLLEVGAITT------- 122
Cdd:pfam11968   1 AEIDAEIEALGGLEAYQLASKLGQSKDrggDSSKVLVEWLKPLLVR--------LKLGEGKL-RALEVGALSTknaiskc 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982  123 TLLDcpavQTTAIDLLSRHARIQQIDFFHLPQPPLST--FDVIVASMLINSLPTASARGDFLRRCHAYL----EASKGYL 196
Cdd:pfam11968  72 GLFD----EVTRIDLNSQEPGILQQDFMERPLPRDESekFDLISLSLVLNFVPDPADRGEMLKRCTKFLrppgPASPPSL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585110982  197 FLILPSSCLTHSKYMTVGKFRSLVTTrVGFAVVEEKWTPKTVAFVLRASGKCDEGRLTAGREKV 260
Cdd:pfam11968 148 FLVLPLPCVTNSRYMDEERLQAIMSS-LGFRLVKQKETKKLIYWLWEWNGKRPAKPKFFKKEEL 210
 
Name Accession Description Interval E-value
Bmt2 pfam11968
25S rRNA (adenine(2142)-N(1))-methyltransferase, Bmt2; This entry represents Bmt2 and its ...
 53-260 1.30e-38

25S rRNA (adenine(2142)-N(1))-methyltransferase, Bmt2; This entry represents Bmt2 and its homogues. In Saccharomyces cerevisiae, Bmt2 is a nucleolar S-adenosylmethionine-dependent rRNA methyltransferase that is responsible for the N-1-methyl-adenosine base modification of 25S rRNA.It specifically methylates the N1 position of adenine 2142 in 25S rRNA.


Pssm-ID: 371825  Cd Length: 221  Bit Score: 134.68  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982   53 SRLQESLEALGGRAAYQSASQLSVSFH---STSKWVLARLQAMGIIrmqsapslSPSQPSQKpRLLEVGAITT------- 122
Cdd:pfam11968   1 AEIDAEIEALGGLEAYQLASKLGQSKDrggDSSKVLVEWLKPLLVR--------LKLGEGKL-RALEVGALSTknaiskc 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982  123 TLLDcpavQTTAIDLLSRHARIQQIDFFHLPQPPLST--FDVIVASMLINSLPTASARGDFLRRCHAYL----EASKGYL 196
Cdd:pfam11968  72 GLFD----EVTRIDLNSQEPGILQQDFMERPLPRDESekFDLISLSLVLNFVPDPADRGEMLKRCTKFLrppgPASPPSL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585110982  197 FLILPSSCLTHSKYMTVGKFRSLVTTrVGFAVVEEKWTPKTVAFVLRASGKCDEGRLTAGREKV 260
Cdd:pfam11968 148 FLVLPLPCVTNSRYMDEERLQAIMSS-LGFRLVKQKETKKLIYWLWEWNGKRPAKPKFFKKEEL 210
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 133-202 3.12e-04

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: 39.62  E-value: 3.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585110982 133 TAIDLLSRHARIQQIDFFH-----LPQPPlSTFDVIVASMLINSLPTASArgdFLRRCHAYLeASKGYLFLILPS 202
Cdd:COG2227   57 EALEIARERAAELNVDFVQgdledLPLED-GSFDLVICSEVLEHLPDPAA---LLRELARLL-KPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 113-200 1.00e-03

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: 37.79  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982 113 RLLEVGA----ITTTLLDCPAVQTTAIDLLSR---HARIQQI------------DFFHLPQPPLSTFDVIVASMLINSLP 173
Cdd:cd02440    1 RVLDLGCgtgaLALALASGPGARVTGVDISPValeLARKAAAalladnvevlkgDAEELPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 585110982 174 TASARgdFLRRCHAYLeASKGYLFLIL 200
Cdd:cd02440   81 EDLAR--FLEEARRLL-KPGGVLVLTL 104
 
Name Accession Description Interval E-value
Bmt2 pfam11968
25S rRNA (adenine(2142)-N(1))-methyltransferase, Bmt2; This entry represents Bmt2 and its ...
 53-260 1.30e-38

25S rRNA (adenine(2142)-N(1))-methyltransferase, Bmt2; This entry represents Bmt2 and its homogues. In Saccharomyces cerevisiae, Bmt2 is a nucleolar S-adenosylmethionine-dependent rRNA methyltransferase that is responsible for the N-1-methyl-adenosine base modification of 25S rRNA.It specifically methylates the N1 position of adenine 2142 in 25S rRNA.


Pssm-ID: 371825  Cd Length: 221  Bit Score: 134.68  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982   53 SRLQESLEALGGRAAYQSASQLSVSFH---STSKWVLARLQAMGIIrmqsapslSPSQPSQKpRLLEVGAITT------- 122
Cdd:pfam11968   1 AEIDAEIEALGGLEAYQLASKLGQSKDrggDSSKVLVEWLKPLLVR--------LKLGEGKL-RALEVGALSTknaiskc 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982  123 TLLDcpavQTTAIDLLSRHARIQQIDFFHLPQPPLST--FDVIVASMLINSLPTASARGDFLRRCHAYL----EASKGYL 196
Cdd:pfam11968  72 GLFD----EVTRIDLNSQEPGILQQDFMERPLPRDESekFDLISLSLVLNFVPDPADRGEMLKRCTKFLrppgPASPPSL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585110982  197 FLILPSSCLTHSKYMTVGKFRSLVTTrVGFAVVEEKWTPKTVAFVLRASGKCDEGRLTAGREKV 260
Cdd:pfam11968 148 FLVLPLPCVTNSRYMDEERLQAIMSS-LGFRLVKQKETKKLIYWLWEWNGKRPAKPKFFKKEEL 210
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 133-202 3.12e-04

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: 39.62  E-value: 3.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585110982 133 TAIDLLSRHARIQQIDFFH-----LPQPPlSTFDVIVASMLINSLPTASArgdFLRRCHAYLeASKGYLFLILPS 202
Cdd:COG2227   57 EALEIARERAAELNVDFVQgdledLPLED-GSFDLVICSEVLEHLPDPAA---LLRELARLL-KPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 103-230 9.38e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.95  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982  103 LSPSQPSQKpRLLEVGAITTTLLDCPA---VQTTAIDL------LSRHARIQQIDFFHLPQPPLSTFDVIVASMLINSLP 173
Cdd:pfam13489  16 LLPKLPSPG-RVLDFGCGTGIFLRLLRaqgFSVTGVDPspiaieRALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVP 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585110982  174 TASArgdFLRRCHAYLeASKGYLFLILPSS----------------CLTHSKYMTVGKFRSLVtTRVGFAVVE 230
Cdd:pfam13489  95 DPPA---LLRQIAALL-KPGGLLLLSTPLAsdeadrlllewpylrpRNGHISLFSARSLKRLL-EEAGFEVVS 162
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 113-200 1.00e-03

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: 37.79  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585110982 113 RLLEVGA----ITTTLLDCPAVQTTAIDLLSR---HARIQQI------------DFFHLPQPPLSTFDVIVASMLINSLP 173
Cdd:cd02440    1 RVLDLGCgtgaLALALASGPGARVTGVDISPValeLARKAAAalladnvevlkgDAEELPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 585110982 174 TASARgdFLRRCHAYLeASKGYLFLIL 200
Cdd:cd02440   81 EDLAR--FLEEARRLL-KPGGVLVLTL 104
 
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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