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Conserved domains on  [gi|19922074|ref|NP_610732|]
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Hen1 methyltransferase [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bacter_Hen1 super family cl37382
3' terminal RNA ribose 2'-O-methyltransferase Hen1; Members of this protein family are ...
22-236 1.29e-32

3' terminal RNA ribose 2'-O-methyltransferase Hen1; Members of this protein family are bacterial Hen1, a 3' terminal RNA ribose 2'-O-methyltransferase that acts in bacterial RNA repair. All members of the seed alignment belong to a cassette with the RNA repair enzyme polynucleotide kinase-phosphatase (Pnkp). Chemically similar Hen1 in eukaryotes acts instead on small regulatory RNAs. [Transcription, RNA processing, Protein synthesis, tRNA and rRNA base modification]


The actual alignment was detected with superfamily member TIGR04074:

Pssm-ID: 274962 [Multi-domain]  Cd Length: 462  Bit Score: 127.42  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922074    22 DPPVYEQRYCATIQILEDArwkdQIKKVVEFGCAEMRFFQLMRRIETIEHIGLVDIDKSLLMRnltSVNPLVSDYI--RS 99
Cdd:TIGR04074 263 PPSLNRQRLEAVVAALRES----GARSVLDLGCGEGKLLRLLLAEKQFERIAGVDVSARELEI---AARRLKLDRMpeRQ 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922074   100 RAsplKVQILQGNVADSSEELRDTDAVIAIELIEHVYDDVLAKIPVNIFGFMQPKLVVFSTPNSDFNVIFtrfnPLLP-N 178
Cdd:TIGR04074 336 RE---RIQLFQGSLTYRDKRLKGFDAAVLVEVIEHLDPPRLPALERVVFEFARPRTVIVTTPNAEYNVLF----ESLPaG 408
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19922074   179 GFRHEDHKFEWSRDEFKNWCLGIVEKYpNYMFSLTGVGNPPKEyesVGPVSQIAIFVR 236
Cdd:TIGR04074 409 GLRHRDHRFEWTRAEFAAWAEGVAERF-GYTVEFLPIGDEDPE---VGAPTQMAVFTR 462
 
Name Accession Description Interval E-value
bacter_Hen1 TIGR04074
3' terminal RNA ribose 2'-O-methyltransferase Hen1; Members of this protein family are ...
22-236 1.29e-32

3' terminal RNA ribose 2'-O-methyltransferase Hen1; Members of this protein family are bacterial Hen1, a 3' terminal RNA ribose 2'-O-methyltransferase that acts in bacterial RNA repair. All members of the seed alignment belong to a cassette with the RNA repair enzyme polynucleotide kinase-phosphatase (Pnkp). Chemically similar Hen1 in eukaryotes acts instead on small regulatory RNAs. [Transcription, RNA processing, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274962 [Multi-domain]  Cd Length: 462  Bit Score: 127.42  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922074    22 DPPVYEQRYCATIQILEDArwkdQIKKVVEFGCAEMRFFQLMRRIETIEHIGLVDIDKSLLMRnltSVNPLVSDYI--RS 99
Cdd:TIGR04074 263 PPSLNRQRLEAVVAALRES----GARSVLDLGCGEGKLLRLLLAEKQFERIAGVDVSARELEI---AARRLKLDRMpeRQ 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922074   100 RAsplKVQILQGNVADSSEELRDTDAVIAIELIEHVYDDVLAKIPVNIFGFMQPKLVVFSTPNSDFNVIFtrfnPLLP-N 178
Cdd:TIGR04074 336 RE---RIQLFQGSLTYRDKRLKGFDAAVLVEVIEHLDPPRLPALERVVFEFARPRTVIVTTPNAEYNVLF----ESLPaG 408
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19922074   179 GFRHEDHKFEWSRDEFKNWCLGIVEKYpNYMFSLTGVGNPPKEyesVGPVSQIAIFVR 236
Cdd:TIGR04074 409 GLRHRDHRFEWTRAEFAAWAEGVAERF-GYTVEFLPIGDEDPE---VGAPTQMAVFTR 462
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
40-162 4.40e-07

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: 48.48  E-value: 4.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922074  40 ARWKDQIKKVVEFGCAEMRFFQLMRRiETIEHIGlVDIDKSLLmrnltsvnplvsDYIRSRASPLKVQILQGNVADSSEE 119
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALAR-RGADVTG-VDISPEAL------------EIARERAAELNVDFVQGDLEDLPLE 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19922074 120 LRDTDAVIAIELIEHVYD--DVLAkipvNIFGFMQPK-LVVFSTPN 162
Cdd:COG2227  85 DGSFDLVICSEVLEHLPDpaALLR----ELARLLKPGgLLLLSTPN 126
 
Name Accession Description Interval E-value
bacter_Hen1 TIGR04074
3' terminal RNA ribose 2'-O-methyltransferase Hen1; Members of this protein family are ...
22-236 1.29e-32

3' terminal RNA ribose 2'-O-methyltransferase Hen1; Members of this protein family are bacterial Hen1, a 3' terminal RNA ribose 2'-O-methyltransferase that acts in bacterial RNA repair. All members of the seed alignment belong to a cassette with the RNA repair enzyme polynucleotide kinase-phosphatase (Pnkp). Chemically similar Hen1 in eukaryotes acts instead on small regulatory RNAs. [Transcription, RNA processing, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274962 [Multi-domain]  Cd Length: 462  Bit Score: 127.42  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922074    22 DPPVYEQRYCATIQILEDArwkdQIKKVVEFGCAEMRFFQLMRRIETIEHIGLVDIDKSLLMRnltSVNPLVSDYI--RS 99
Cdd:TIGR04074 263 PPSLNRQRLEAVVAALRES----GARSVLDLGCGEGKLLRLLLAEKQFERIAGVDVSARELEI---AARRLKLDRMpeRQ 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922074   100 RAsplKVQILQGNVADSSEELRDTDAVIAIELIEHVYDDVLAKIPVNIFGFMQPKLVVFSTPNSDFNVIFtrfnPLLP-N 178
Cdd:TIGR04074 336 RE---RIQLFQGSLTYRDKRLKGFDAAVLVEVIEHLDPPRLPALERVVFEFARPRTVIVTTPNAEYNVLF----ESLPaG 408
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19922074   179 GFRHEDHKFEWSRDEFKNWCLGIVEKYpNYMFSLTGVGNPPKEyesVGPVSQIAIFVR 236
Cdd:TIGR04074 409 GLRHRDHRFEWTRAEFAAWAEGVAERF-GYTVEFLPIGDEDPE---VGAPTQMAVFTR 462
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
40-162 4.40e-07

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: 48.48  E-value: 4.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922074  40 ARWKDQIKKVVEFGCAEMRFFQLMRRiETIEHIGlVDIDKSLLmrnltsvnplvsDYIRSRASPLKVQILQGNVADSSEE 119
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALAR-RGADVTG-VDISPEAL------------EIARERAAELNVDFVQGDLEDLPLE 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19922074 120 LRDTDAVIAIELIEHVYD--DVLAkipvNIFGFMQPK-LVVFSTPN 162
Cdd:COG2227  85 DGSFDLVICSEVLEHLPDpaALLR----ELARLLKPGgLLLLSTPN 126
 
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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