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Conserved domains on  [gi|5174529|ref|NP_005902|]
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S-adenosylmethionine synthase isoform type-2 [Homo sapiens]

Protein Classification

methionine adenosyltransferase( domain architecture ID 11488017)

methionine adenosyltransferase catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PTZ00104 PTZ00104
S-adenosylmethionine synthase; Provisional
16-395 0e+00

S-adenosylmethionine synthase; Provisional


:

Pssm-ID: 240268  Cd Length: 398  Bit Score: 711.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    16 GTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDS 95
Cdd:PTZ00104   9 GHFLFTSESVSEGHPDKLCDQISDAVLDACLAQDPLSKVACETCAKTGMVMVFGEITTKAVVDYQKVVRDTVKEIGYDDT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    96 SKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPW 175
Cdd:PTZ00104  89 EKGLDYKTCNVLVAIEQQSPDIAQGVHVGKKEEDIGAGDQGIMFGYATDETEELMPLTHELATKLAKRLSELRKNGILPW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   176 LRPDSKTQVTVQYMQDRGAVL-PIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGG 254
Cdd:PTZ00104 169 LRPDAKTQVTVEYEYDTRGGLtPKRVHTILISTQHDEGVSNEEIREDLMEHVIKPVIPAKLLDEETKYHLNPSGRFVIGG 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   255 PQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFH 334
Cdd:PTZ00104 249 PHGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDPSKVDRSAAYAARWIAKSLVAAGLCKRCLVQVSYAIGVAEPLSIHVNT 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5174529   335 YGTSQK--SERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGR--DSFPWEVPKKLKY 395
Cdd:PTZ00104 329 YGTGKKgyDDEDLLEIVQKNFDLRPGDIIKELDLRRPIFQKTASYGHFGRsdPEFTWEVPKDLEH 393
 
Name Accession Description Interval E-value
PTZ00104 PTZ00104
S-adenosylmethionine synthase; Provisional
16-395 0e+00

S-adenosylmethionine synthase; Provisional


Pssm-ID: 240268  Cd Length: 398  Bit Score: 711.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    16 GTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDS 95
Cdd:PTZ00104   9 GHFLFTSESVSEGHPDKLCDQISDAVLDACLAQDPLSKVACETCAKTGMVMVFGEITTKAVVDYQKVVRDTVKEIGYDDT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    96 SKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPW 175
Cdd:PTZ00104  89 EKGLDYKTCNVLVAIEQQSPDIAQGVHVGKKEEDIGAGDQGIMFGYATDETEELMPLTHELATKLAKRLSELRKNGILPW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   176 LRPDSKTQVTVQYMQDRGAVL-PIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGG 254
Cdd:PTZ00104 169 LRPDAKTQVTVEYEYDTRGGLtPKRVHTILISTQHDEGVSNEEIREDLMEHVIKPVIPAKLLDEETKYHLNPSGRFVIGG 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   255 PQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFH 334
Cdd:PTZ00104 249 PHGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDPSKVDRSAAYAARWIAKSLVAAGLCKRCLVQVSYAIGVAEPLSIHVNT 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5174529   335 YGTSQK--SERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGR--DSFPWEVPKKLKY 395
Cdd:PTZ00104 329 YGTGKKgyDDEDLLEIVQKNFDLRPGDIIKELDLRRPIFQKTASYGHFGRsdPEFTWEVPKDLEH 393
S-AdoMet_synt cd18079
S-adenosylmethionine synthetase; S-adenosylmethionine synthetase (EC 2.5.1.6), also known as ...
19-391 0e+00

S-adenosylmethionine synthetase; S-adenosylmethionine synthetase (EC 2.5.1.6), also known as methionine adenosyltransferase, catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP in two steps, the formation of AdoMet and hydrolysis of the tripolyphosphate, which occurs prior to release of the product from the enzyme, which consists of three structural domains that have a similar alpha+beta fold.


Pssm-ID: 350837  Cd Length: 371  Bit Score: 701.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   19 LFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKG 98
Cdd:cd18079   1 LFTSESVTEGHPDKICDQISDAILDACLAQDPNSRVACETLVTTGLVIIAGEITTKAYVDIEKIVREVIKEIGYDDSDFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   99 FDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRP 178
Cdd:cd18079  81 FDAKTCGVLVSIHEQSPDIAQGVDEGLELEEIGAGDQGIMFGYATDETPELMPLPIVLAHKLARRLAEVRKNGTLPWLRP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529  179 DSKTQVTVQYMQDRgavlPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGD 258
Cdd:cd18079 161 DGKTQVTVEYEDGK----PVRVDTIVVSTQHDEDVSLEELREDIIEKVIKPVIPEELLDEDTKYLINPTGRFVIGGPAGD 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529  259 AGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTS 338
Cdd:cd18079 237 TGLTGRKIIVDTYGGYARHGGGAFSGKDPTKVDRSAAYAARYIAKNIVAAGLAKRCEVQLSYAIGVAEPVSIYVDTFGTG 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5174529  339 QKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGR--DSFPWEVPK 391
Cdd:cd18079 317 KISDEKIEEIIKKNFDLRPAGIIEDLDLRRPIYRKTAAYGHFGRedEDFPWEKTD 371
metK TIGR01034
S-adenosylmethionine synthetase; Tandem isozymes of this S-adenosylmethionine synthetase in E. ...
19-394 0e+00

S-adenosylmethionine synthetase; Tandem isozymes of this S-adenosylmethionine synthetase in E. coli are designated MetK and MetX. [Central intermediary metabolism, Other]


Pssm-ID: 273406  Cd Length: 377  Bit Score: 654.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529     19 LFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKG 98
Cdd:TIGR01034   1 LFTSESVSEGHPDKIADQISDAVLDAILKQDPKSKVACETFVKTGLVLIGGEITTSAYVDIQEVARNTIKDIGYTDSDYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529     99 FDYKTCNVLVALEQQSPDIAQGVHLDRNEEdIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRP 178
Cdd:TIGR01034  81 FDAKTCAVLDAIGNQSPDIAQGVDKANPEE-QGAGDQGIMFGYATNETPELMPLPITLAHKLLKRAAELRKSGTLPWLRP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    179 DSKTQVTVQYMQDRgavlPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGD 258
Cdd:TIGR01034 160 DGKSQVTIQYEDNK----PVRVDTVVLSTQHDPDISQKDLREAIIEEIIKPVLPAEFLDEKTKFFINPTGRFVIGGPMGD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    259 AGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTS 338
Cdd:TIGR01034 236 TGLTGRKIIVDTYGGWARHGGGAFSGKDPSKVDRSAAYAARYIAKNIVAAGLADRCEVQLSYAIGVAEPVSIMVETFGTS 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 5174529    339 QKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLK 394
Cdd:TIGR01034 316 KKSSEELLNVVKENFDLRPGGIIEKLDLLKPIYRKTAAYGHFGREEFPWEKPDKLE 371
MetK COG0192
S-adenosylmethionine synthetase [Coenzyme transport and metabolism]; S-adenosylmethionine ...
18-388 0e+00

S-adenosylmethionine synthetase [Coenzyme transport and metabolism]; S-adenosylmethionine synthetase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 439962 [Multi-domain]  Cd Length: 384  Bit Score: 652.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   18 FLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSK 97
Cdd:COG0192   2 YLFTSESVTEGHPDKVCDQISDAILDAILAQDPNARVACETLVTTGLVVVAGEITTSAYVDIPEIVRETIKEIGYTSSEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   98 GFDYKTCNVLVALEQQSPDIAQGVHLDRNE-EDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWL 176
Cdd:COG0192  82 GFDADTCAVLTSIHEQSPDIAQGVDEALDElDEQGAGDQGIMFGYACNETPELMPLPISLAHRLARRLAEVRKSGELPYL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529  177 RPDSKTQVTVQYMQDRgavlPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQ 256
Cdd:COG0192 162 RPDGKSQVTVEYEDGK----PVRIDTVVVSTQHDPDVSQEQLREDIIEEVIKPVLPAELLDDDTKYLINPTGRFVIGGPQ 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529  257 GDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYG 336
Cdd:COG0192 238 GDAGLTGRKIIVDTYGGYARHGGGAFSGKDPTKVDRSAAYAARYVAKNIVAAGLADRCEVQLAYAIGVAEPVSIYVDTFG 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 5174529  337 TSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRD--SFPWE 388
Cdd:COG0192 318 TGKVSDEKIEEAVREVFDLRPAGIIERLDLRRPIYRKTAAYGHFGREdlDFPWE 371
S-AdoMet_synt_C pfam02773
S-adenosylmethionine synthetase, C-terminal domain; The three domains of S-adenosylmethionine ...
252-388 7.81e-89

S-adenosylmethionine synthetase, C-terminal domain; The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.


Pssm-ID: 460688 [Multi-domain]  Cd Length: 138  Bit Score: 264.63  E-value: 7.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    252 IGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSIS 331
Cdd:pfam02773   1 IGGPQGDTGLTGRKIIVDTYGGYARHGGGAFSGKDPTKVDRSAAYAARYIAKNIVAAGLAKRCEVQLSYAIGVAEPVSIY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5174529    332 IFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDS-FPWE 388
Cdd:pfam02773  81 VDTFGTGKVSDEKILEIVRENFDLRPAGIIERLDLRRPIYRKTAAYGHFGREPdFPWE 138
 
Name Accession Description Interval E-value
PTZ00104 PTZ00104
S-adenosylmethionine synthase; Provisional
16-395 0e+00

S-adenosylmethionine synthase; Provisional


Pssm-ID: 240268  Cd Length: 398  Bit Score: 711.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    16 GTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDS 95
Cdd:PTZ00104   9 GHFLFTSESVSEGHPDKLCDQISDAVLDACLAQDPLSKVACETCAKTGMVMVFGEITTKAVVDYQKVVRDTVKEIGYDDT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    96 SKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPW 175
Cdd:PTZ00104  89 EKGLDYKTCNVLVAIEQQSPDIAQGVHVGKKEEDIGAGDQGIMFGYATDETEELMPLTHELATKLAKRLSELRKNGILPW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   176 LRPDSKTQVTVQYMQDRGAVL-PIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGG 254
Cdd:PTZ00104 169 LRPDAKTQVTVEYEYDTRGGLtPKRVHTILISTQHDEGVSNEEIREDLMEHVIKPVIPAKLLDEETKYHLNPSGRFVIGG 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   255 PQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFH 334
Cdd:PTZ00104 249 PHGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDPSKVDRSAAYAARWIAKSLVAAGLCKRCLVQVSYAIGVAEPLSIHVNT 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5174529   335 YGTSQK--SERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGR--DSFPWEVPKKLKY 395
Cdd:PTZ00104 329 YGTGKKgyDDEDLLEIVQKNFDLRPGDIIKELDLRRPIFQKTASYGHFGRsdPEFTWEVPKDLEH 393
S-AdoMet_synt cd18079
S-adenosylmethionine synthetase; S-adenosylmethionine synthetase (EC 2.5.1.6), also known as ...
19-391 0e+00

S-adenosylmethionine synthetase; S-adenosylmethionine synthetase (EC 2.5.1.6), also known as methionine adenosyltransferase, catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP in two steps, the formation of AdoMet and hydrolysis of the tripolyphosphate, which occurs prior to release of the product from the enzyme, which consists of three structural domains that have a similar alpha+beta fold.


Pssm-ID: 350837  Cd Length: 371  Bit Score: 701.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   19 LFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKG 98
Cdd:cd18079   1 LFTSESVTEGHPDKICDQISDAILDACLAQDPNSRVACETLVTTGLVIIAGEITTKAYVDIEKIVREVIKEIGYDDSDFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   99 FDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRP 178
Cdd:cd18079  81 FDAKTCGVLVSIHEQSPDIAQGVDEGLELEEIGAGDQGIMFGYATDETPELMPLPIVLAHKLARRLAEVRKNGTLPWLRP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529  179 DSKTQVTVQYMQDRgavlPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGD 258
Cdd:cd18079 161 DGKTQVTVEYEDGK----PVRVDTIVVSTQHDEDVSLEELREDIIEKVIKPVIPEELLDEDTKYLINPTGRFVIGGPAGD 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529  259 AGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTS 338
Cdd:cd18079 237 TGLTGRKIIVDTYGGYARHGGGAFSGKDPTKVDRSAAYAARYIAKNIVAAGLAKRCEVQLSYAIGVAEPVSIYVDTFGTG 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5174529  339 QKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGR--DSFPWEVPK 391
Cdd:cd18079 317 KISDEKIEEIIKKNFDLRPAGIIEDLDLRRPIYRKTAAYGHFGRedEDFPWEKTD 371
metK TIGR01034
S-adenosylmethionine synthetase; Tandem isozymes of this S-adenosylmethionine synthetase in E. ...
19-394 0e+00

S-adenosylmethionine synthetase; Tandem isozymes of this S-adenosylmethionine synthetase in E. coli are designated MetK and MetX. [Central intermediary metabolism, Other]


Pssm-ID: 273406  Cd Length: 377  Bit Score: 654.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529     19 LFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKG 98
Cdd:TIGR01034   1 LFTSESVSEGHPDKIADQISDAVLDAILKQDPKSKVACETFVKTGLVLIGGEITTSAYVDIQEVARNTIKDIGYTDSDYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529     99 FDYKTCNVLVALEQQSPDIAQGVHLDRNEEdIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRP 178
Cdd:TIGR01034  81 FDAKTCAVLDAIGNQSPDIAQGVDKANPEE-QGAGDQGIMFGYATNETPELMPLPITLAHKLLKRAAELRKSGTLPWLRP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    179 DSKTQVTVQYMQDRgavlPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGD 258
Cdd:TIGR01034 160 DGKSQVTIQYEDNK----PVRVDTVVLSTQHDPDISQKDLREAIIEEIIKPVLPAEFLDEKTKFFINPTGRFVIGGPMGD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    259 AGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTS 338
Cdd:TIGR01034 236 TGLTGRKIIVDTYGGWARHGGGAFSGKDPSKVDRSAAYAARYIAKNIVAAGLADRCEVQLSYAIGVAEPVSIMVETFGTS 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 5174529    339 QKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLK 394
Cdd:TIGR01034 316 KKSSEELLNVVKENFDLRPGGIIEKLDLLKPIYRKTAAYGHFGREEFPWEKPDKLE 371
MetK COG0192
S-adenosylmethionine synthetase [Coenzyme transport and metabolism]; S-adenosylmethionine ...
18-388 0e+00

S-adenosylmethionine synthetase [Coenzyme transport and metabolism]; S-adenosylmethionine synthetase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 439962 [Multi-domain]  Cd Length: 384  Bit Score: 652.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   18 FLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSK 97
Cdd:COG0192   2 YLFTSESVTEGHPDKVCDQISDAILDAILAQDPNARVACETLVTTGLVVVAGEITTSAYVDIPEIVRETIKEIGYTSSEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   98 GFDYKTCNVLVALEQQSPDIAQGVHLDRNE-EDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWL 176
Cdd:COG0192  82 GFDADTCAVLTSIHEQSPDIAQGVDEALDElDEQGAGDQGIMFGYACNETPELMPLPISLAHRLARRLAEVRKSGELPYL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529  177 RPDSKTQVTVQYMQDRgavlPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQ 256
Cdd:COG0192 162 RPDGKSQVTVEYEDGK----PVRIDTVVVSTQHDPDVSQEQLREDIIEEVIKPVLPAELLDDDTKYLINPTGRFVIGGPQ 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529  257 GDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYG 336
Cdd:COG0192 238 GDAGLTGRKIIVDTYGGYARHGGGAFSGKDPTKVDRSAAYAARYVAKNIVAAGLADRCEVQLAYAIGVAEPVSIYVDTFG 317
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 5174529  337 TSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRD--SFPWE 388
Cdd:COG0192 318 TGKVSDEKIEEAVREVFDLRPAGIIERLDLRRPIYRKTAAYGHFGREdlDFPWE 371
PLN02243 PLN02243
S-adenosylmethionine synthase
17-393 0e+00

S-adenosylmethionine synthase


Pssm-ID: 177886 [Multi-domain]  Cd Length: 386  Bit Score: 608.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    17 TFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSS 96
Cdd:PLN02243   3 TFLFTSESVNEGHPDKLCDQISDAVLDACLAQDPDSKVACETCTKTNMVMVFGEITTKAKVDYEKIVRDTCREIGFVSDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    97 KGFDYKTCNVLVALEQQSPDIAQGVH--LDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLP 174
Cdd:PLN02243  83 VGLDADKCKVLVNIEQQSPDIAQGVHghLTKKPEEIGAGDQGHMFGYATDETPELMPLTHVLATKLGARLTEVRKNGTCP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   175 WLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGG 254
Cdd:PLN02243 163 WLRPDGKTQVTVEYKNEGGAMVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529   255 PQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFH 334
Cdd:PLN02243 243 PHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVAAGLARRCIVQVSYAIGVPEPLSVFVDT 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5174529   335 YGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKK---PIYQRTAAYGHFGRD--SFPWEVPKKL 393
Cdd:PLN02243 323 YGTGKIPDKEILKIVKENFDFRPGMIAINLDLKRggnGRFQKTAAYGHFGRDdpDFTWEVVKPL 386
S-AdoMet_synt_C pfam02773
S-adenosylmethionine synthetase, C-terminal domain; The three domains of S-adenosylmethionine ...
252-388 7.81e-89

S-adenosylmethionine synthetase, C-terminal domain; The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.


Pssm-ID: 460688 [Multi-domain]  Cd Length: 138  Bit Score: 264.63  E-value: 7.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    252 IGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSIS 331
Cdd:pfam02773   1 IGGPQGDTGLTGRKIIVDTYGGYARHGGGAFSGKDPTKVDRSAAYAARYIAKNIVAAGLAKRCEVQLSYAIGVAEPVSIY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5174529    332 IFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDS-FPWE 388
Cdd:pfam02773  81 VDTFGTGKVSDEKILEIVRENFDLRPAGIIERLDLRRPIYRKTAAYGHFGREPdFPWE 138
S-AdoMet_synt_M pfam02772
S-adenosylmethionine synthetase, central domain; The three domains of S-adenosylmethionine ...
129-250 2.25e-75

S-adenosylmethionine synthetase, central domain; The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.


Pssm-ID: 460687 [Multi-domain]  Cd Length: 118  Bit Score: 229.20  E-value: 2.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529    129 DIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRgavlPIRVHTIVISVQ 208
Cdd:pfam02772   1 EIGAGDQGIMFGYACDETPELMPLPISLAHRLARRLAEVRKDGTLPYLRPDGKTQVTVEYDDGK----PVRIDTIVVSTQ 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 5174529    209 HDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRF 250
Cdd:pfam02772  77 HDPDVSLEQLREDIIEEVIKPVLPAELLDDDTKYHINPTGRF 118
S-AdoMet_synt_N pfam00438
S-adenosylmethionine synthetase, N-terminal domain; The three domains of S-adenosylmethionine ...
17-114 1.75e-66

S-adenosylmethionine synthetase, N-terminal domain; The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.


Pssm-ID: 459810 [Multi-domain]  Cd Length: 98  Bit Score: 206.05  E-value: 1.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174529     17 TFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSS 96
Cdd:pfam00438   1 KYLFTSESVTEGHPDKVCDQISDAILDAFLAQDPNSRVACETLVTTGLVVVAGEITTKAYVDIEKIVRDTIKEIGYDDAE 80
                          90
                  ....*....|....*...
gi 5174529     97 KGFDYKTCNVLVALEQQS 114
Cdd:pfam00438  81 YGFDADTCAVLVAIHEQS 98
 
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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