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Conserved domains on  [gi|189571605|ref|NP_653360|]
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acetylserotonin O-methyltransferase [Rattus norvegicus]

Protein Classification

acetylserotonin O-methyltransferase( domain architecture ID 11245788)

acetylserotonin O-methyltransferase catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
116-327 1.42e-102

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


:

Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 303.56  E-value: 1.42e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  116 WAHLAAGVREGRNQYSRAVGISaedPFSAIYRSEPERLLFMRGLQETWSLCGGRVLTAFDLSRFRVICDLGGGSGALAQE 195
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGIS---LFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  196 AARLYPGSSVCVFDLPDVIAAARTHFlSPGARPSVRFVAGDFFRSRLPRADLFILARVLHDWADGACVELLGRLHRACRP 275
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHF-SAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 189571605  276 GGALLLVEAVLAKGGAGPLRSLLLSLNMMLQAEGWERQASDYRNLATRAGFP 327
Cdd:pfam00891 157 GGKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGFS 208
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
16-99 2.48e-32

dimerization domain; This domain, found in methyltransferases, functions as a dimerization domain.


:

Pssm-ID: 465287  Cd Length: 87  Bit Score: 117.66  E-value: 2.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605   16 LMSLAHGFMVSQVLFAALDLGIFDLAAQGPVAAEAVAQTGGWSPRGTQLLMDACTRLGLLR---GAGDGSYTNSALSSTF 92
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEGPLSAEEVAARLGASVDGTERLLDACVALGLLErekTDGKGLYSNTELASTY 80

                  ....*..
gi 189571605   93 LVSGSPQ 99
Cdd:pfam16864  81 LVSSSPK 87
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
116-327 1.42e-102

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 303.56  E-value: 1.42e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  116 WAHLAAGVREGRNQYSRAVGISaedPFSAIYRSEPERLLFMRGLQETWSLCGGRVLTAFDLSRFRVICDLGGGSGALAQE 195
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGIS---LFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  196 AARLYPGSSVCVFDLPDVIAAARTHFlSPGARPSVRFVAGDFFRSRLPRADLFILARVLHDWADGACVELLGRLHRACRP 275
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHF-SAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 189571605  276 GGALLLVEAVLAKGGAGPLRSLLLSLNMMLQAEGWERQASDYRNLATRAGFP 327
Cdd:pfam00891 157 GGKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGFS 208
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
16-99 2.48e-32

dimerization domain; This domain, found in methyltransferases, functions as a dimerization domain.


Pssm-ID: 465287  Cd Length: 87  Bit Score: 117.66  E-value: 2.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605   16 LMSLAHGFMVSQVLFAALDLGIFDLAAQGPVAAEAVAQTGGWSPRGTQLLMDACTRLGLLR---GAGDGSYTNSALSSTF 92
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEGPLSAEEVAARLGASVDGTERLLDACVALGLLErekTDGKGLYSNTELASTY 80

                  ....*..
gi 189571605   93 LVSGSPQ 99
Cdd:pfam16864  81 LVSSSPK 87
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
178-283 3.59e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 71.01  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 178 RFRVICDLGGGSGALAQEAARLYPGSSVCVFDL-PDVIAAARTHFlspgarPSVRFVAGDFFRSRLPR-ADLFILARVLH 255
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLsPEMLARARARL------PNVRFVVADLRDLDPPEpFDLVVSNAALH 74
                         90       100
                 ....*....|....*....|....*...
gi 189571605 256 DWADgaCVELLGRLHRACRPGGALLLVE 283
Cdd:COG4106   75 WLPD--HAALLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
182-282 4.16e-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: 48.20  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 182 ICDLGGGSGALAQEAARlYPGSSVCVFDL-PDVIAAARTHFLSPGArPSVRFVAGDFFR---SRLPRADLFILARVLHDW 257
Cdd:cd02440    2 VLDLGCGTGALALALAS-GPGARVTGVDIsPVALELARKAAAALLA-DNVEVLKGDAEElppEADESFDVIISDPPLHHL 79
                         90       100
                 ....*....|....*....|....*
gi 189571605 258 ADgACVELLGRLHRACRPGGALLLV 282
Cdd:cd02440   80 VE-DLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
116-327 1.42e-102

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 303.56  E-value: 1.42e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  116 WAHLAAGVREGRNQYSRAVGISaedPFSAIYRSEPERLLFMRGLQETWSLCGGRVLTAFDLSRFRVICDLGGGSGALAQE 195
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGIS---LFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  196 AARLYPGSSVCVFDLPDVIAAARTHFlSPGARPSVRFVAGDFFRSRLPRADLFILARVLHDWADGACVELLGRLHRACRP 275
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHF-SAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 189571605  276 GGALLLVEAVLAKGGAGPLRSLLLSLNMMLQAEGWERQASDYRNLATRAGFP 327
Cdd:pfam00891 157 GGKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGFS 208
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
16-99 2.48e-32

dimerization domain; This domain, found in methyltransferases, functions as a dimerization domain.


Pssm-ID: 465287  Cd Length: 87  Bit Score: 117.66  E-value: 2.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605   16 LMSLAHGFMVSQVLFAALDLGIFDLAAQGPVAAEAVAQTGGWSPRGTQLLMDACTRLGLLR---GAGDGSYTNSALSSTF 92
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEGPLSAEEVAARLGASVDGTERLLDACVALGLLErekTDGKGLYSNTELASTY 80

                  ....*..
gi 189571605   93 LVSGSPQ 99
Cdd:pfam16864  81 LVSSSPK 87
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
178-283 3.59e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 71.01  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 178 RFRVICDLGGGSGALAQEAARLYPGSSVCVFDL-PDVIAAARTHFlspgarPSVRFVAGDFFRSRLPR-ADLFILARVLH 255
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLsPEMLARARARL------PNVRFVVADLRDLDPPEpFDLVVSNAALH 74
                         90       100
                 ....*....|....*....|....*...
gi 189571605 256 DWADgaCVELLGRLHRACRPGGALLLVE 283
Cdd:COG4106   75 WLPD--HAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
182-277 1.85e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 60.27  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  182 ICDLGGGSGALAQEAARLYpGSSVCVFDL-PDVIAAARTHFLSPGARpsVRFVAGDFFRSRLPRA--DLFILARVLHDWA 258
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLsPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGsfDLVVSSGVLHHLP 77
                          90
                  ....*....|....*....
gi 189571605  259 DGACVELLGRLHRACRPGG 277
Cdd:pfam13649  78 DPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
169-283 2.14e-10

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: 58.47  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 169 RVLTAFDLSRFRVICDLGGGSGALAQEAARLypGSSVCVFDL-PDVIAAARTHFLSPGARpsVRFVAGDFFRSRLPRA-- 245
Cdd:COG2226   13 ALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDIsPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGsf 88
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 189571605 246 DLFILARVLHDWADgaCVELLGRLHRACRPGGALLLVE 283
Cdd:COG2226   89 DLVISSFVLHHLPD--PERALAEIARVLKPGGRLVVVD 124
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
184-279 3.15e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 53.91  E-value: 3.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  184 DLGGGSGALAQEAARLYPGSSVCVFDL-PDVIAAARTHF--LSPGARPSVRFVAGDFFRSRLPRADLFILARVLHDWADG 260
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPGLEYTGLDIsPAALEAARERLaaLGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLADP 81
                          90
                  ....*....|....*....
gi 189571605  261 AcvELLGRLHRACRPGGAL 279
Cdd:pfam08242  82 R--AVLRNIRRLLKPGGVL 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
182-281 7.44e-09

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: 53.87  E-value: 7.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 182 ICDLGGGSGALAQEAARLypGSSVCVFDL-PDVIAAARTHflspGARPSVRFVAGDFFRSRLP--RADLFILARVLH--- 255
Cdd:COG2227   28 VLDVGCGTGRLALALARR--GADVTGVDIsPEALEIARER----AAELNVDFVQGDLEDLPLEdgSFDLVICSEVLEhlp 101
                         90       100
                 ....*....|....*....|....*.
gi 189571605 256 DWAdgacvELLGRLHRACRPGGALLL 281
Cdd:COG2227  102 DPA-----ALLRELARLLKPGGLLLL 122
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
182-345 1.07e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.84  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 182 ICDLGGGSGALAQEAARLYpGSSVCVFDL-PDVIAAARtHFLSPGARPSVRFVAGDFFRS---RLPRADLFILARVLHDW 257
Cdd:COG0500   30 VLDLGCGTGRNLLALAARF-GGRVIGIDLsPEAIALAR-ARAAKAGLGNVEFLVADLAELdplPAESFDLVVAFGVLHHL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 258 ADGACVELLGRLHRACRPGGALLLVEAVLAKG--GAGPLRSLLLSLNMMLQAEGWERQASDYRNLATRAGFPRLQLRRPG 335
Cdd:COG0500  108 PPEEREALLRELARALKPGGVLLLSASDAAAAlsLARLLLLATASLLELLLLLRLLALELYLRALLAAAATEDLRSDALL 187
                        170
                 ....*....|
gi 189571605 336 GPYHAMLARR 345
Cdd:COG0500  188 ESANALEYLL 197
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
182-282 4.16e-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: 48.20  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 182 ICDLGGGSGALAQEAARlYPGSSVCVFDL-PDVIAAARTHFLSPGArPSVRFVAGDFFR---SRLPRADLFILARVLHDW 257
Cdd:cd02440    2 VLDLGCGTGALALALAS-GPGARVTGVDIsPVALELARKAAAALLA-DNVEVLKGDAEElppEADESFDVIISDPPLHHL 79
                         90       100
                 ....*....|....*....|....*
gi 189571605 258 ADgACVELLGRLHRACRPGGALLLV 282
Cdd:cd02440   80 VE-DLARFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
161-282 9.51e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.84  E-value: 9.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 161 ETWSLCGGRVLTAFDLSRFRVICDLGGGSGALAQEAARLypGSSVCVFDL-PDVIAAARTHFLspgarpSVRFVAGDF-- 237
Cdd:COG4976   29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLsEEMLAKAREKGV------YDRLLVADLad 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 189571605 238 FRSRLPRADLFILARVLHDWADGAcvELLGRLHRACRPGGALLLV 282
Cdd:COG4976  101 LAEPDGRFDLIVAADVLTYLGDLA--AVFAGVARALKPGGLFIFS 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
184-281 1.99e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 45.73  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  184 DLGGGSGALAQEAARLypGSSVCVFDL-PDVIAAARTHflspGARPSVRFVAGDFFRSRLP--RADLFILARVLHDWADG 260
Cdd:pfam08241   2 DVGCGTGLLTELLARL--GARVTGVDIsPEMLELAREK----APREGLTFVVGDAEDLPFPdnSFDLVLSSEVLHHVEDP 75
                          90       100
                  ....*....|....*....|.
gi 189571605  261 AcvELLGRLHRACRPGGALLL 281
Cdd:pfam08241  76 E--RALREIARVLKPGGILII 94
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
181-321 2.35e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 47.03  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605  181 VICDLGGGSGALAQEAA-RLYPGSSVCVFDL-PDVIAAARTHFLSPGARpSVRFVAGDFFrsRLP------RADLFILAR 252
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAeELGPNAEVVGIDIsEEAIEKARENAQKLGFD-NVEFEQGDIE--ELPelleddKFDVVISNC 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189571605  253 VLHDWADGACVelLGRLHRACRPGGALLLVEAVLAKGGAGPLRSLLLSLNMMLQAEGWERQASDYRNLA 321
Cdd:pfam13847  83 VLNHIPDPDKV--LQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKLYELLEEA 149
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
180-249 6.85e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 46.95  E-value: 6.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189571605 180 RVICDLGGGSGALAQEAARLYPGSSVCVFDLPDVIAAARTHFLSPGARPSVRFVAGDFFRSRLP-RADLFI 249
Cdd:COG4076   37 DVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPeKADVII 107
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
185-250 9.33e-06

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 45.97  E-value: 9.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189571605 185 LGGGSGALAQEAARLYPGSSVCVFDL-PDVIAAARTHF--LSPGAR-PSVRFVAGD---FFRSRLPRADLFIL 250
Cdd:COG0421   44 IGGGDGGLARELLKHPPVERVDVVEIdPEVVELAREYFplLAPAFDdPRLRVVIGDgraFLREAEESYDVIIV 116
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
167-282 7.14e-05

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 43.64  E-value: 7.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 167 GGRVL-TAFDLSRFRVICDLGGGSGALAQEAARLYPGSSVCVFDL-PDVIAAARTHFLSPGARpSVRFVAGDFFrSRLPR 244
Cdd:COG2813   37 GTRLLlEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVnARAVELARANAAANGLE-NVEVLWSDGL-SGVPD 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 189571605 245 ADL-FIL----ARVLHDWADGACVELLGRLHRACRPGGALLLV 282
Cdd:COG2813  115 GSFdLILsnppFHAGRAVDKEVAHALIADAARHLRPGGELWLV 157
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
167-281 1.20e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.53  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 167 GGRVLtafdlsrfrvicDLGGGSGALAQEAARLYpGSSVCVFDLPDV-IAAARTHFLSPGARPSVRFVAGDFFRSRLP-R 244
Cdd:COG2230   52 GMRVL------------DIGCGWGGLALYLARRY-GVRVTGVTLSPEqLEYARERAAEAGLADRVEVRLADYRDLPADgQ 118
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 189571605 245 ADLFILARVLHDWADGACVELLGRLHRACRPGGALLL 281
Cdd:COG2230  119 FDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
196-352 2.39e-03

O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442544  Cd Length: 246  Bit Score: 39.56  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 196 AARLYPGSSVCVF--DLPDVIAAaRTHFLSP-GARPSVRFVAGDFF----RSRLPRAD-------LFILARVLHDWADGA 261
Cdd:COG3315   71 AYRLDNPGGVRWFevDLPEVIAL-KRRLLPElGPPARLRLVAVDLRdpdwPDALPAAGfdpsrptLFIAEGVLMYLTEEA 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189571605 262 CVELLGRLHRACRPGGALLLvEAVLAKGGAGPLRSLLLSLNMMLQAE--GWERQASDYRNLATRAGFPRLQLRRPGGPYH 339
Cdd:COG3315  150 VRALLRRIAALFPPGSELAF-DYVPPLALKGSKKHPAVRKLRRDLGApfKFGIDPDDPAELLEEPGWRLVEELSPLELLA 228
                        170
                 ....*....|...
gi 189571605 340 AMLARRGPRPGII 352
Cdd:COG3315  229 RYLPLRPLRAPRL 241
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
180-244 6.44e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 37.58  E-value: 6.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189571605 180 RVICDLGGGSGALAqEAARLYPGSSVCVFDL-PDVIAAARTHFLSPGARpsVRFVAGDFFRSRLPR 244
Cdd:COG2263   47 KTVLDLGCGTGMLA-IGAALLGAKKVVGVDIdPEALEIARENAERLGVR--VDFIRADVTRIPLGG 109
 
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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