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Conserved domains on  [gi|2616562530|ref|XP_060625847|]
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acetylserotonin O-methyltransferase [Anolis sagrei]

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 ...
 118-327 1.02e-112

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: 325.90  E-value: 1.02e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 118 WHYLTDAIREGKNQYERAFGISskdVFEALYRSEEEMIKFMYGLNATWSICGRDVLAAFNLSPFTVIYDLGGGAGALAHE 197
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGIS---LFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 198 CISLYPNCTVTIFDLSKVVETAKKHFVSSEEQRITFHEGDFFKDPIPEADLYILARILHDWADDKCVQLLTKVQKVCKPG 277
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHFSAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2616562530 278 GGVLLVETLLNEDKSGPLESQLYSLNMLVQTEGKERTATEFTKLLIEAGF 327
Cdd:pfam00891 158 GKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGF 207
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
 13-101 8.33e-40

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


:

Pssm-ID: 465287  Cd Length: 87  Bit Score: 135.38  E-value: 8.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530  13 LIQYQNGFLISKVMFTACEMGIFDLLRESKetLSTKTIAERLGSSIRGMERLLDACVGLKLLRVDIKQEGAFYGNTEISN 92
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEGP--LSAEEVAARLGASVDGTERLLDACVALGLLEREKTDGKGLYSNTELAS 78


                  ....*....
gi 2616562530  93 LYLTRSGSK 101
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 ...
 118-327 1.02e-112

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: 325.90  E-value: 1.02e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 118 WHYLTDAIREGKNQYERAFGISskdVFEALYRSEEEMIKFMYGLNATWSICGRDVLAAFNLSPFTVIYDLGGGAGALAHE 197
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGIS---LFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 198 CISLYPNCTVTIFDLSKVVETAKKHFVSSEEQRITFHEGDFFKDPIPEADLYILARILHDWADDKCVQLLTKVQKVCKPG 277
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHFSAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2616562530 278 GGVLLVETLLNEDKSGPLESQLYSLNMLVQTEGKERTATEFTKLLIEAGF 327
Cdd:pfam00891 158 GKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGF 207
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
 13-101 8.33e-40

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


Pssm-ID: 465287  Cd Length: 87  Bit Score: 135.38  E-value: 8.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530  13 LIQYQNGFLISKVMFTACEMGIFDLLRESKetLSTKTIAERLGSSIRGMERLLDACVGLKLLRVDIKQEGAFYGNTEISN 92
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEGP--LSAEEVAARLGASVDGTERLLDACVALGLLEREKTDGKGLYSNTELAS 78


                  ....*....
gi 2616562530  93 LYLTRSGSK 101
Cdd:pfam16864  79 TYLVSSSPK 87
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
180-285 2.69e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 62.15  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 180 PFTVIYDLGGGAGALAHECISLYPNCTVTIFDLSKV-VETAKKHFvsseeQRITFHEGDFFK-DPIPEADLYILARILHd 257
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEmLARARARL-----PNVRFVVADLRDlDPPEPFDLVVSNAALH- 74

                          90       100
                  ....*....|....*....|....*...
gi 2616562530 258 WADDKcVQLLTKVQKVCKPgGGVLLVET 285
Cdd:COG4106    75 WLPDH-AALLARLAAALAP-GGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 184-287 2.07e-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: 48.58  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 184 IYDLGGGAGALAHEcISLYPNCTVTIFDLS-KVVETAKKHFVSSEEQRITFHEGDFFK---DPIPEADLyILARILHDWA 259
Cdd:cd02440     2 VLDLGCGTGALALA-LASGPGARVTGVDISpVALELARKAAAALLADNVEVLKGDAEElppEADESFDV-IISDPPLHHL 79

                          90       100
                  ....*....|....*....|....*...
gi 2616562530 260 DDKCVQLLTKVQKVCKPgGGVLLVETLL 287
Cdd:cd02440    80 VEDLARFLEEARRLLKP-GGVLVLTLVL 106
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 172-245 4.61e-07

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 50.55  E-value: 4.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2616562530 172 VLAAFNLSPFTVIYDLGGGAGALAhecISL---YPNCTVTIFDLSKV-VETAKKHFVSSEEQRITFHEGDFFkDPIPE 245
Cdd:PRK09328  100 ALEALLLKEPLRVLDLGTGSGAIA---LALakeRPDAEVTAVDISPEaLAVARRNAKHGLGARVEFLQGDWF-EPLPG 173
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 180-257 2.47e-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: 39.26  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 180 PFTVIYDLGGGAGALAHECISLYPNCTVTIFDLSK-----VVETAKKHFVsseEQRITFHEGDFFkDPIP--EADL---- 248
Cdd:TIGR00536 114 PILHILDLGTGSGCIALALAYEFPNAEVIAVDISPdalavAEENAEKNQL---EHRVEFIQSNLF-EPLAgqKIDIivsn 189

                          90
                  ....*....|.
gi 2616562530 249 --YILARILHD 257
Cdd:TIGR00536 190 ppYIDEEDLAD 200
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 118-327 1.02e-112

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: 325.90  E-value: 1.02e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 118 WHYLTDAIREGKNQYERAFGISskdVFEALYRSEEEMIKFMYGLNATWSICGRDVLAAFNLSPFTVIYDLGGGAGALAHE 197
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGIS---LFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 198 CISLYPNCTVTIFDLSKVVETAKKHFVSSEEQRITFHEGDFFKDPIPEADLYILARILHDWADDKCVQLLTKVQKVCKPG 277
Cdd:pfam00891  78 IVSLYPGCKGIVFDLPHVVEAAPTHFSAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2616562530 278 GGVLLVETLLNEDKSGPLESQLYSLNMLVQTEGKERTATEFTKLLIEAGF 327
Cdd:pfam00891 158 GKVILVESLLGADPSGPLHTQLYSLNMLAQTEGRERTEAEYSELLTGAGF 207
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
 13-101 8.33e-40

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


Pssm-ID: 465287  Cd Length: 87  Bit Score: 135.38  E-value: 8.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530  13 LIQYQNGFLISKVMFTACEMGIFDLLRESKetLSTKTIAERLGSSIRGMERLLDACVGLKLLRVDIKQEGAFYGNTEISN 92
Cdd:pfam16864   1 LLDLIDGFRASKVLFTACELGVFDLLAEGP--LSAEEVAARLGASVDGTERLLDACVALGLLEREKTDGKGLYSNTELAS 78


                  ....*....
gi 2616562530  93 LYLTRSGSK 101
Cdd:pfam16864  79 TYLVSSSPK 87
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
180-285 2.69e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 62.15  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 180 PFTVIYDLGGGAGALAHECISLYPNCTVTIFDLSKV-VETAKKHFvsseeQRITFHEGDFFK-DPIPEADLYILARILHd 257
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEmLARARARL-----PNVRFVVADLRDlDPPEPFDLVVSNAALH- 74

                          90       100
                  ....*....|....*....|....*...
gi 2616562530 258 WADDKcVQLLTKVQKVCKPgGGVLLVET 285
Cdd:COG4106    75 WLPDH-AALLARLAAALAP-GGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 184-278 7.05e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.04  E-value: 7.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 184 IYDLGGGAGALAHECISLYpNCTVTIFDLSKV-VETAKKHFvSSEEQRITFHEGDFFKDPIPEA--DLYILARILHDWAD 260
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEmLERARERA-AEAGLNVEFVQGDAEDLPFPDGsfDLVVSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 2616562530 261 DKCVQLLTKVQKVCKPGG 278
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 170-284 5.66e-11

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: 59.62  E-value: 5.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 170 RDVLAAFNLSPFTVIYDLGGGAGALAHECISLypNCTVTIFDLSKV-VETAKKHFvSSEEQRITFHEGDFFKDPIPEA-- 246
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEmLELARERA-AEAGLNVEFVVGDAEDLPFPDGsf 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2616562530 247 DLYILARILHDWADDkcVQLLTKVQKVCKPGGGVLLVE 284
Cdd:COG2226    89 DLVISSFVLHHLPDP--ERALAEIARVLKPGGRLVVVD 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 184-327 3.88e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 55.69  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 184 IYDLGGGAGALAHECISLYpNCTVTIFDLSKV-VETAKKHFVSSEEQRITFHEGDFFK-DPIPEA--DLYILARILHDWA 259
Cdd:COG0500    30 VLDLGCGTGRNLLALAARF-GGRVIGIDLSPEaIALARARAAKAGLGNVEFLVADLAElDPLPAEsfDLVVAFGVLHHLP 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 260 DDKCVQLLTKVQKVCKPGGGVLLVETLLNEDKSGPLES--QLYSLNMLVQTEGKERTATEFTKLLIEAGF 327
Cdd:COG0500   109 PEEREALLRELARALKPGGVLLLSASDAAAALSLARLLllATASLLELLLLLRLLALELYLRALLAAAAT 178
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 182-326 4.52e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 51.65  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 182 TVIYDLGGGAGALAHECIS-LYPNCTVTIFDLSK-VVETAKKHFVSSEEQRITFHEGDFFKDPIPEA----DLYILARIL 255
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEeAIEKARENAQKLGFDNVEFEQGDIEELPELLEddkfDVVISNCVL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2616562530 256 HDWADdkCVQLLTKVQKVCKPGGGVLLVEtllnEDKSGPLESQLYSLN-MLVQTEGKERTATEFTKLLIEAG 326
Cdd:pfam13847  85 NHIPD--PDKVLQEILRVLKPGGRLIISD----PDSLAELPAHVKEDStYYAGCVGGAILKKKLYELLEEAG 150
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 186-278 8.46e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 49.67  E-value: 8.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 186 DLGGGAGALAHECISLYPNCTVTIFDLSK-VVETAKKHFVSSEEQ---RITFHEGDFFKDPIPEADLYILARILHDWADD 261
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPGLEYTGLDISPaALEAARERLAALGLLnavRVELFQLDLGELDPGSFDVVVASNVLHHLADP 81

                          90
                  ....*....|....*..
gi 2616562530 262 KcvQLLTKVQKVCKPGG 278
Cdd:pfam08242  82 R--AVLRNIRRLLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 184-287 2.07e-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: 48.58  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 184 IYDLGGGAGALAHEcISLYPNCTVTIFDLS-KVVETAKKHFVSSEEQRITFHEGDFFK---DPIPEADLyILARILHDWA 259
Cdd:cd02440     2 VLDLGCGTGALALA-LASGPGARVTGVDISpVALELARKAAAALLADNVEVLKGDAEElppEADESFDV-IISDPPLHHL 79

                          90       100
                  ....*....|....*....|....*...
gi 2616562530 260 DDKCVQLLTKVQKVCKPgGGVLLVETLL 287
Cdd:cd02440    80 VEDLARFLEEARRLLKP-GGVLVLTLVL 106
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 172-245 4.61e-07

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 50.55  E-value: 4.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2616562530 172 VLAAFNLSPFTVIYDLGGGAGALAhecISL---YPNCTVTIFDLSKV-VETAKKHFVSSEEQRITFHEGDFFkDPIPE 245
Cdd:PRK09328  100 ALEALLLKEPLRVLDLGTGSGAIA---LALakeRPDAEVTAVDISPEaLAVARRNAKHGLGARVEFLQGDWF-EPLPG 173
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
187-257 3.26e-05

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 44.05  E-value: 3.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2616562530 187 LGGGAGALAHECISLYPNCTVTIFDLS-KVVETAKKHF----VSSEEQRITFHEGD---FFKDPIPEADLyilarILHD 257
Cdd:COG0421    44 IGGGDGGLARELLKHPPVERVDVVEIDpEVVELAREYFpllaPAFDDPRLRVVIGDgraFLREAEESYDV-----IIVD 117
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 172-257 3.54e-05

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 44.76  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 172 VLAAFNLSPFTVIYDLGGGAGALAhecISL---YPNCTVTIFDLSKV-VETAK----KHFVsseEQRITFHEGDFFkDPI 243
Cdd:COG2890   104 ALALLPAGAPPRVLDLGTGSGAIA---LALakeRPDARVTAVDISPDaLAVARrnaeRLGL---EDRVRFLQGDLF-EPL 176

                          90       100
                  ....*....|....*....|...
gi 2616562530 244 PEA---DL------YILARILHD 257
Cdd:COG2890   177 PGDgrfDLivsnppYIPEDEIAL 199
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 180-257 2.47e-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: 39.26  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2616562530 180 PFTVIYDLGGGAGALAHECISLYPNCTVTIFDLSK-----VVETAKKHFVsseEQRITFHEGDFFkDPIP--EADL---- 248
Cdd:TIGR00536 114 PILHILDLGTGSGCIALALAYEFPNAEVIAVDISPdalavAEENAEKNQL---EHRVEFIQSNLF-EPLAgqKIDIivsn 189

                          90
                  ....*....|.
gi 2616562530 249 --YILARILHD 257
Cdd:TIGR00536 190 ppYIDEEDLAD 200
 
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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