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Conserved domains on  [gi|2106649953|ref|XP_043998861|]
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acetylserotonin O-methyltransferase 2 [Gambusia affinis]

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 ...
 121-329 1.64e-90

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: 269.66  E-value: 1.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 121 WNNLADAIREGRNQYEKTFGLPSahfFQAIYRSEEEMLKFMGIMSCHWVLDGHDVVTAFDLSRFQKVVDLGGCTGALANE 200
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISL---FEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 201 MARAYPASSVTVFDLPEVVEAAQKHFK--QDSGVTFQSGDFFSGEIPGADLYVLARVIHDWPEEKCLELLKKIYETCKPG 278
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHFSagEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2106649953 279 GGVLLVEALLFENRRGPIMAQIFSLNMLVQTQGRERTPSEYTHMLNKSGFR 329
Cdd:pfam00891 158 GKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGFS 208
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
 16-104 4.29e-36

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


:

Pssm-ID: 465287  Cd Length: 87  Bit Score: 125.75  E-value: 4.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953  16 LLEYFNGFRVSKIIFSACELGVFDLLLKSqdALSAQHVAHELGTSVDGMERLLDALVGIEILEVEKAEGTALYSSTDVAN 95
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEG--PLSAEEVAARLGASVDGTERLLDACVALGLLEREKTDGKGLYSNTELAS 78


                  ....*....
gi 2106649953  96 LYLAKGSAK 104
Cdd:pfam16864  79 TYLVSSSPK 87
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 121-329 1.64e-90

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: 269.66  E-value: 1.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 121 WNNLADAIREGRNQYEKTFGLPSahfFQAIYRSEEEMLKFMGIMSCHWVLDGHDVVTAFDLSRFQKVVDLGGCTGALANE 200
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISL---FEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 201 MARAYPASSVTVFDLPEVVEAAQKHFK--QDSGVTFQSGDFFSGEIPGADLYVLARVIHDWPEEKCLELLKKIYETCKPG 278
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHFSagEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2106649953 279 GGVLLVEALLFENRRGPIMAQIFSLNMLVQTQGRERTPSEYTHMLNKSGFR 329
Cdd:pfam00891 158 GKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGFS 208
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
 16-104 4.29e-36

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


Pssm-ID: 465287  Cd Length: 87  Bit Score: 125.75  E-value: 4.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953  16 LLEYFNGFRVSKIIFSACELGVFDLLLKSqdALSAQHVAHELGTSVDGMERLLDALVGIEILEVEKAEGTALYSSTDVAN 95
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEG--PLSAEEVAARLGASVDGTERLLDACVALGLLEREKTDGKGLYSNTELAS 78


                  ....*....
gi 2106649953  96 LYLAKGSAK 104
Cdd:pfam16864  79 TYLVSSSPK 87
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 180-340 7.18e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.00  E-value: 7.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 180 DLSRFQKVVDLGgC-TGALANEMARAYpASSVTVFDL-PEVVEAAQKHFKQD--SGVTFQSGDFF-SGEIPGA--DLYVL 252
Cdd:COG0500    23 RLPKGGRVLDLG-CgTGRNLLALAARF-GGRVIGIDLsPEAIALARARAAKAglGNVEFLVADLAeLDPLPAEsfDLVVA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 253 ARVIHDWPEEKCLELLKKIYETCKPgGGVLLVEALLFENRRGPIM---AQIFSLNMLVQTQGRERTPSEYTHMLNKSGFR 329
Cdd:COG0500   101 FGVLHHLPPEEREALLRELARALKP-GGVLLLSASDAAAALSLARlllLATASLLELLLLLRLLALELYLRALLAAAATE 179

                         170
                  ....*....|.
gi 2106649953 330 NVLVCRTGKSY 340
Cdd:COG0500   180 DLRSDALLESA 190
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 186-289 9.79e-06

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: 43.96  E-value: 9.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 186 KVVDLGGCTGALANEMARaYPASSVTVFDL-PEVVEAAQKHF--KQDSGVTFQSGDFFSG---EIPGADLYVLARVIHDW 259
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDIsPVALELARKAAaaLLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2106649953 260 PEEKcLELLKKIYETCKPgGGVLLVEALLF 289
Cdd:cd02440    80 VEDL-ARFLEEARRLLKP-GGVLVLTLVLA 107
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 159-340 1.21e-05

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 46.42  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 159 KFMGIMSCHWVLDGH-------DVVTAFDLS-RFQKVVDLGGCTGALANEMARAYPASSVTVFDLPEVVEAAQKHFKQDS 230
Cdd:PLN02490   81 RFLSIVYDHIINPGHwtedmrdDALEPADLSdRNLKVVDVGGGTGFTTLGIVKHVDAKNVTILDQSPHQLAKAKQKEPLK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 231 GVTFQSGDffSGEIP----GADLYVLARVIHDWPEEKclELLKKIYETCKPGGGVLLVeallfenrrGPI-----MAQIF 301
Cdd:PLN02490  161 ECKIIEGD--AEDLPfptdYADRYVSAGSIEYWPDPQ--RGIKEAYRVLKIGGKACLI---------GPVhptfwLSRFF 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2106649953 302 S-LNMLVQTQgrertpSEYTHMLNKSGFRNVLVCRTGKSY 340
Cdd:PLN02490  228 AdVWMLFPKE------EEYIEWFTKAGFKDVKLKRIGPKW 261
TIGR00740 TIGR00740
tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, ...
 186-293 3.97e-05

tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, in preparing the uridine-5-oxyacetic acid (cmo5U) at position 34. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273244  Cd Length: 239  Bit Score: 44.23  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 186 KVVDLGGCTGALANEMARAYPASSVTVFDL---PEVVEAAQKH---FKQDSGVTFQSGDFFSGEIPGADLYVLARVIHDW 259
Cdd:TIGR00740  56 NVYDLGCSLGAATLSARRNIHHDNCKIIAIdnsPAMIERCRQHiaaYHAEIPVDIICGDIRDIAIENASMVILNFTLQFL 135

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2106649953 260 PEEKCLELLKKIYETCKPGGGVLLVEALLFENRR 293
Cdd:TIGR00740 136 EPEDRIALLDKIYEGLNPGGALVLSEKFRFEDAK 169
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 121-329 1.64e-90

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: 269.66  E-value: 1.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 121 WNNLADAIREGRNQYEKTFGLPSahfFQAIYRSEEEMLKFMGIMSCHWVLDGHDVVTAFDLSRFQKVVDLGGCTGALANE 200
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISL---FEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 201 MARAYPASSVTVFDLPEVVEAAQKHFK--QDSGVTFQSGDFFSGEIPGADLYVLARVIHDWPEEKCLELLKKIYETCKPG 278
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHFSagEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2106649953 279 GGVLLVEALLFENRRGPIMAQIFSLNMLVQTQGRERTPSEYTHMLNKSGFR 329
Cdd:pfam00891 158 GKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGFS 208
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
 16-104 4.29e-36

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


Pssm-ID: 465287  Cd Length: 87  Bit Score: 125.75  E-value: 4.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953  16 LLEYFNGFRVSKIIFSACELGVFDLLLKSqdALSAQHVAHELGTSVDGMERLLDALVGIEILEVEKAEGTALYSSTDVAN 95
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEG--PLSAEEVAARLGASVDGTERLLDACVALGLLEREKTDGKGLYSNTELAS 78


                  ....*....
gi 2106649953  96 LYLAKGSAK 104
Cdd:pfam16864  79 TYLVSSSPK 87
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 187-279 1.94e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 187 VVDLGGCTGALANEMARAYPASsVTVFDL-PEVVEAAQKHFKQDS-GVTFQSGDFFSGEIPGA--DLYVLARVIHDWPEE 262
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR-VTGVDLsPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGsfDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 2106649953 263 KCLELLKKIYETCKPGG 279
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 180-340 7.18e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.00  E-value: 7.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 180 DLSRFQKVVDLGgC-TGALANEMARAYpASSVTVFDL-PEVVEAAQKHFKQD--SGVTFQSGDFF-SGEIPGA--DLYVL 252
Cdd:COG0500    23 RLPKGGRVLDLG-CgTGRNLLALAARF-GGRVIGIDLsPEAIALARARAAKAglGNVEFLVADLAeLDPLPAEsfDLVVA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 253 ARVIHDWPEEKCLELLKKIYETCKPgGGVLLVEALLFENRRGPIM---AQIFSLNMLVQTQGRERTPSEYTHMLNKSGFR 329
Cdd:COG0500   101 FGVLHHLPPEEREALLRELARALKP-GGVLLLSASDAAAALSLARlllLATASLLELLLLLRLLALELYLRALLAAAATE 179

                         170
                  ....*....|.
gi 2106649953 330 NVLVCRTGKSY 340
Cdd:COG0500   180 DLRSDALLESA 190
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 173-285 4.44e-08

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: 51.53  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 173 HDVVTAFDLSRFQKVVDLGGCTGALANEMARAypASSVTVFDL-PEVVEAAQKHFKQ-DSGVTFQSGDFFSGEIPGA--D 248
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDIsPEMLELARERAAEaGLNVEFVVGDAEDLPFPDGsfD 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2106649953 249 LYVLARVIHDWPEEKclELLKKIYETCKPGGGVLLVE 285
Cdd:COG2226    90 LVISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVD 124
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 188-279 4.51e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 47.36  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 188 VDLGGCTGALANEMARAYPASSVTVFDL-PEVVEAAQKHFKQDSG-----VTFQSGDFFSGEIPGADLYVLARVIHDWPE 261
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDIsPAALEAARERLAALGLlnavrVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 2106649953 262 EKclELLKKIYETCKPGG 279
Cdd:pfam08242  81 PR--AVLRNIRRLLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 186-285 1.57e-06

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: 46.55  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 186 KVVDLGGCTGALANEMARAypASSVTVFDL-PEVVEAAQKHFKqDSGVTFQSGDFFSGEIPGA--DLYVLARVIHDWPEE 262
Cdd:COG2227    27 RVLDVGCGTGRLALALARR--GADVTGVDIsPEALEIARERAA-ELNVDFVQGDLEDLPLEDGsfDLVICSEVLEHLPDP 103

                          90       100
                  ....*....|....*....|...
gi 2106649953 263 KclELLKKIYETCKPgGGVLLVE 285
Cdd:COG2227   104 A--ALLRELARLLKP-GGLLLLS 123
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 186-289 9.79e-06

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: 43.96  E-value: 9.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 186 KVVDLGGCTGALANEMARaYPASSVTVFDL-PEVVEAAQKHF--KQDSGVTFQSGDFFSG---EIPGADLYVLARVIHDW 259
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDIsPVALELARKAAaaLLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2106649953 260 PEEKcLELLKKIYETCKPgGGVLLVEALLF 289
Cdd:cd02440    80 VEDL-ARFLEEARRLLKP-GGVLVLTLVLA 107
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 159-340 1.21e-05

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 46.42  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 159 KFMGIMSCHWVLDGH-------DVVTAFDLS-RFQKVVDLGGCTGALANEMARAYPASSVTVFDLPEVVEAAQKHFKQDS 230
Cdd:PLN02490   81 RFLSIVYDHIINPGHwtedmrdDALEPADLSdRNLKVVDVGGGTGFTTLGIVKHVDAKNVTILDQSPHQLAKAKQKEPLK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 231 GVTFQSGDffSGEIP----GADLYVLARVIHDWPEEKclELLKKIYETCKPGGGVLLVeallfenrrGPI-----MAQIF 301
Cdd:PLN02490  161 ECKIIEGD--AEDLPfptdYADRYVSAGSIEYWPDPQ--RGIKEAYRVLKIGGKACLI---------GPVhptfwLSRFF 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2106649953 302 S-LNMLVQTQgrertpSEYTHMLNKSGFRNVLVCRTGKSY 340
Cdd:PLN02490  228 AdVWMLFPKE------EEYIEWFTKAGFKDVKLKRIGPKW 261
TIGR00740 TIGR00740
tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, ...
 186-293 3.97e-05

tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, in preparing the uridine-5-oxyacetic acid (cmo5U) at position 34. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273244  Cd Length: 239  Bit Score: 44.23  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 186 KVVDLGGCTGALANEMARAYPASSVTVFDL---PEVVEAAQKH---FKQDSGVTFQSGDFFSGEIPGADLYVLARVIHDW 259
Cdd:TIGR00740  56 NVYDLGCSLGAATLSARRNIHHDNCKIIAIdnsPAMIERCRQHiaaYHAEIPVDIICGDIRDIAIENASMVILNFTLQFL 135

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2106649953 260 PEEKCLELLKKIYETCKPGGGVLLVEALLFENRR 293
Cdd:TIGR00740 136 EPEDRIALLDKIYEGLNPGGALVLSEKFRFEDAK 169
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 178-331 6.99e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 42.80  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 178 AFDLSRFQKVVDLGGCTGALANEMARAYPasSVTVFDLPEVVEAAQKHFKQDSGVTFQSGDFFSGEipgADL----YVLA 253
Cdd:pfam13489  17 LPKLPSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERALLNVRFDQFDEQEAAVPAGK---FDVivarEVLE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 254 RViHDWPEekcleLLKKIYETCKPGGGVLLVEAL-------LFENRRGP-IMAQIFSLnmlvqtqgreRTPSEYTHMLNK 325
Cdd:pfam13489  92 HV-PDPPA-----LLRQIAALLKPGGLLLLSTPLasdeadrLLLEWPYLrPRNGHISL----------FSARSLKRLLEE 155


                  ....*.
gi 2106649953 326 SGFRNV 331
Cdd:pfam13489 156 AGFEVV 161
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
185-232 7.03e-05

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 43.28  E-value: 7.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2106649953 185 QKVVDLGGCTGALANEMARAYPASSVTVFDL-PEVVEAAQKHFKQDSGV 232
Cdd:COG0421    39 KRVLIIGGGDGGLARELLKHPPVERVDVVEIdPEVVELAREYFPLLAPA 87
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 188-279 9.57e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 40.73  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 188 VDLGGCTGALANEMARAYPasSVTVFDL-PEVVEAAQKHFkQDSGVTFQSGDFFSGEIPGA--DLYVLARVIHDWPEEKc 264
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDIsPEMLELAREKA-PREGLTFVVGDAEDLPFPDNsfDLVLSSEVLHHVEDPE- 76

                          90
                  ....*....|....*
gi 2106649953 265 lELLKKIYETCKPGG 279
Cdd:pfam08241  77 -RALREIARVLKPGG 90
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 162-284 3.62e-04

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 40.78  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 162 GIMSCHWVLDGHDVVTAFDLSRFQKVVDLGGCTGALANEMARAYPASSVTVFDLPEVVEAAQKHFKQ---DSGVTFQ--- 235
Cdd:pfam10294  25 AVVLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLLPGASVTITDLEEALELLKKNIELnalSSKVVVKvld 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2106649953 236 -----SGDFFSGEIPgaDLYVLARVIHDwpeEKCLELLKKIYETCKPGGGVLLV 284
Cdd:pfam10294 105 wgenlPPDLFDGHPV--DLILAADCVYN---EDSFPLLEKTLKDLLGKESVILV 153
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
174-328 6.63e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 39.98  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 174 DVVTAFDLSRFQKVVDLGGCTGALANEMARAypASSVTVFDL-PEVVEAAQKHFKQDsgvTFQSGDFFSGEIPG--ADLY 250
Cdd:COG4976    37 ELLARLPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLsEEMLAKAREKGVYD---RLLVADLADLAEPDgrFDLI 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2106649953 251 VLARVIHDWPEEKclELLKKIYETCKPGGgvllvealLFenrrgpimaqIFSLNMLVQTQGRERTPSEYTHMLNKSGF 328
Cdd:COG4976   112 VAADVLTYLGDLA--AVFAGVARALKPGG--------LF----------IFSVEDADGSGRYAHSLDYVRDLLAAAGF 169
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 186-327 7.33e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.32  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 186 KVVDLGGCTGALANEMA-RAYPASSVTVFDL-PEVVEAAQKHFKQD--SGVTFQSGDFFsgEIPGA------DLYVLARV 255
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAeELGPNAEVVGIDIsEEAIEKARENAQKLgfDNVEFEQGDIE--ELPELleddkfDVVISNCV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2106649953 256 IHDWPE-EKCLELLKKIYetcKPGGGVLLVEALLFENRRGPIMAQIFSLNMLVQTQGrerTPSEYTHMLNKSG 327
Cdd:pfam13847  84 LNHIPDpDKVLQEILRVL---KPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAI---LKKKLYELLEEAG 150
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 185-283 3.60e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 37.60  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 185 QKVVDLGGCTGALANEMARAYPAsSVTVFDL-PEVVEAAQKHFKQ---DSGVTFQSGDFFSGEIPGA-DLYVLARVIHDW 259
Cdd:COG2230    53 MRVLDIGCGWGGLALYLARRYGV-RVTGVTLsPEQLEYARERAAEaglADRVEVRLADYRDLPADGQfDAIVSIGMFEHV 131

                          90       100
                  ....*....|....*....|....
gi 2106649953 260 PEEKCLELLKKIYETCKPGGGVLL 283
Cdd:COG2230   132 GPENYPAYFAKVARLLKPGGRLLL 155
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 184-285 8.69e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 37.33  E-value: 8.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2106649953 184 FQKVVDLGGCTGALANEMARAYPASSVTVFDL-PEVVEAAQK---HFKQDSGVTFQSGDFFSgEIPGADL--------YV 251
Cdd:TIGR00536 115 ILHILDLGTGSGCIALALAYEFPNAEVIAVDIsPDALAVAEEnaeKNQLEHRVEFIQSNLFE-PLAGQKIdiivsnppYI 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2106649953 252 LARVIHDWPEEK-------------CLELLKKIYE---TCKPGGGVLLVE 285
Cdd:TIGR00536 194 DEEDLADLPNVVrfepllalvggddGLNILRQIIElapDYLKPNGFLVCE 243
 
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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