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Conserved domains on  [gi|124806534|ref|XP_001350750|]
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serine hydroxymethyltransferase [Plasmodium falciparum 3D7]

Protein Classification

serine hydroxymethyltransferase( domain architecture ID 11488001)

serine hydroxymethyltransferase catalyzes the reversible, simultaneous conversions of L-serine to glycine (retro-aldol cleavage) and tetrahydrofolate to 5,10-methylenetetrahydrofolate (hydrolysis)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
1-441 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 240264  Cd Length: 452  Bit Score: 824.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   1 MFNNDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKR 80
Cdd:PTZ00094   9 LPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  81 ALEAFNVSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEKKKVSITSDLFESKLYKCNSEGY 160
Cdd:PTZ00094  89 ALEAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEKGL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 161 VDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILR 240
Cdd:PTZ00094 169 IDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 241 GPRSALIFFNKKRNPGIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVT 320
Cdd:PTZ00094 249 GPRSGLIFYRKKVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVT 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 321 NGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEKDMEFIADMLLKAILL 400
Cdd:PTZ00094 329 GGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVKL 408
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 124806534 401 TDELQQKYGKKLVDFKKGLVNNPKIDELKKEVVQWAKNLPF 441
Cdd:PTZ00094 409 AQEIQKQVGKKLVDFKKALEKNPELQKLRQEVVEFASQFPF 449
 
Name Accession Description Interval E-value
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
1-441 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 824.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   1 MFNNDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKR 80
Cdd:PTZ00094   9 LPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  81 ALEAFNVSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEKKKVSITSDLFESKLYKCNSEGY 160
Cdd:PTZ00094  89 ALEAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEKGL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 161 VDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILR 240
Cdd:PTZ00094 169 IDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 241 GPRSALIFFNKKRNPGIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVT 320
Cdd:PTZ00094 249 GPRSGLIFYRKKVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVT 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 321 NGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEKDMEFIADMLLKAILL 400
Cdd:PTZ00094 329 GGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVKL 408
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 124806534 401 TDELQQKYGKKLVDFKKGLVNNPKIDELKKEVVQWAKNLPF 441
Cdd:PTZ00094 409 AQEIQKQVGKKLVDFKKALEKNPELQKLRQEVVEFASQFPF 449
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
9-435 0e+00

Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.


Pssm-ID: 99733  Cd Length: 402  Bit Score: 572.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   9 KYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALEAFNVS 88
Cdd:cd00378    2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  89 eeewGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDekkKVSITSDLFESKLYKCNSE-GYVDMESVR 167
Cdd:cd00378   82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPEtGLIDYDALE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 168 NLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRGPRSALI 247
Cdd:cd00378  155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 248 FFNKkrnPGIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVTNGTDNHL 327
Cdd:cd00378  235 LTRK---GELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 328 IVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVD-CVSPSGIRIGTPALTTRGCKEKDMEFIADMLLKAILLTDELqq 406
Cdd:cd00378  312 VLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDV-- 389
                        410       420
                 ....*....|....*....|....*....
gi 124806534 407 kygkklvdfkkglvnnPKIDELKKEVVQW 435
Cdd:cd00378  390 ----------------AVAEEVRKEVAEL 402
SHMT pfam00464
Serine hydroxymethyltransferase;
7-394 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 522.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534    7 LQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALEAFN 86
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   87 VSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEKKKVSITSDLFESKLYKCNSE-GYVDMES 165
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPEtGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  166 VRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRGPRSA 245
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  246 LIFFNK------KRNPGI----DQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRN 315
Cdd:pfam00464 241 MIFYRKgvksvdKTGKEIlyelEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124806534  316 LDLVTNGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEKDMEFIADML 394
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
4-440 0e+00

Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439882  Cd Length: 414  Bit Score: 518.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   4 NDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALE 83
Cdd:COG0112    2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  84 AFNVseeEWgVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGffdekKKVSITSDLFESKLYKCNSE-GYVD 162
Cdd:COG0112   82 LFGA---EH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPEtGLID 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 163 MESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRGP 242
Cdd:COG0112  153 YDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 243 RSALIFFNKKrnpgIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVTNG 322
Cdd:COG0112  233 RGGLILCNEE----LAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGG 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 323 TDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSD-----VdcvsPSGIRIGTPALTTRGCKEKDMEFIADMLLKA 397
Cdd:COG0112  309 TDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDprspfV----TSGIRIGTPAVTTRGMKEAEMEEIAELIADV 384
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 124806534 398 IlltdelqqkygkklvdfkKGLVNNPKIDELKKEVVQWAKNLP 440
Cdd:COG0112  385 L------------------DNPEDEAVLAEVREEVKELCKRFP 409
 
Name Accession Description Interval E-value
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
1-441 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 824.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   1 MFNNDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKR 80
Cdd:PTZ00094   9 LPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  81 ALEAFNVSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEKKKVSITSDLFESKLYKCNSEGY 160
Cdd:PTZ00094  89 ALEAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEKGL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 161 VDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILR 240
Cdd:PTZ00094 169 IDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 241 GPRSALIFFNKKRNPGIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVT 320
Cdd:PTZ00094 249 GPRSGLIFYRKKVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVT 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 321 NGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEKDMEFIADMLLKAILL 400
Cdd:PTZ00094 329 GGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVKL 408
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 124806534 401 TDELQQKYGKKLVDFKKGLVNNPKIDELKKEVVQWAKNLPF 441
Cdd:PTZ00094 409 AQEIQKQVGKKLVDFKKALEKNPELQKLRQEVVEFASQFPF 449
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
2-440 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 610.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   2 FNNDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRA 81
Cdd:PLN03226  10 WGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  82 LEAFNVSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEKKKVSITSDLFESKLYKCNSE-GY 160
Cdd:PLN03226  90 LEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDEStGL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 161 VDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILR 240
Cdd:PLN03226 170 IDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLR 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 241 GPRSALIFFNKKRNPG----------IDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAEC 310
Cdd:PLN03226 250 GPRGGMIFFRKGPKPPkgqgegavydYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 311 LLKRNLDLVTNGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEKDMEFI 390
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKV 409
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124806534 391 ADMLLKAILLTDELQQKYGKKLVDFKKGLVNN---PKIDELKKEVVQWAKNLP 440
Cdd:PLN03226 410 AEFLHRAVTIALKIQKEHGKKLKDFKKGLESNdfsKDIEALRAEVEEFATSFP 462
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
9-435 0e+00

Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.


Pssm-ID: 99733  Cd Length: 402  Bit Score: 572.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   9 KYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALEAFNVS 88
Cdd:cd00378    2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  89 eeewGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDekkKVSITSDLFESKLYKCNSE-GYVDMESVR 167
Cdd:cd00378   82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPEtGLIDYDALE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 168 NLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRGPRSALI 247
Cdd:cd00378  155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 248 FFNKkrnPGIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVTNGTDNHL 327
Cdd:cd00378  235 LTRK---GELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 328 IVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVD-CVSPSGIRIGTPALTTRGCKEKDMEFIADMLLKAILLTDELqq 406
Cdd:cd00378  312 VLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDV-- 389
                        410       420
                 ....*....|....*....|....*....
gi 124806534 407 kygkklvdfkkglvnnPKIDELKKEVVQW 435
Cdd:cd00378  390 ----------------AVAEEVRKEVAEL 402
SHMT pfam00464
Serine hydroxymethyltransferase;
7-394 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 522.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534    7 LQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALEAFN 86
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   87 VSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEKKKVSITSDLFESKLYKCNSE-GYVDMES 165
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPEtGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  166 VRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRGPRSA 245
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  246 LIFFNK------KRNPGI----DQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRN 315
Cdd:pfam00464 241 MIFYRKgvksvdKTGKEIlyelEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124806534  316 LDLVTNGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEKDMEFIADML 394
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
4-440 0e+00

Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439882  Cd Length: 414  Bit Score: 518.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   4 NDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALE 83
Cdd:COG0112    2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  84 AFNVseeEWgVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGffdekKKVSITSDLFESKLYKCNSE-GYVD 162
Cdd:COG0112   82 LFGA---EH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPEtGLID 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 163 MESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRGP 242
Cdd:COG0112  153 YDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 243 RSALIFFNKKrnpgIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVTNG 322
Cdd:COG0112  233 RGGLILCNEE----LAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGG 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 323 TDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSD-----VdcvsPSGIRIGTPALTTRGCKEKDMEFIADMLLKA 397
Cdd:COG0112  309 TDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDprspfV----TSGIRIGTPAVTTRGMKEAEMEEIAELIADV 384
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 124806534 398 IlltdelqqkygkklvdfkKGLVNNPKIDELKKEVVQWAKNLP 440
Cdd:COG0112  385 L------------------DNPEDEAVLAEVREEVKELCKRFP 409
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
2-440 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 515.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   2 FNNDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRA 81
Cdd:PRK00011   1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  82 LEAFNVseeEWgVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGffdekKKVSITSDLFESKLYKCNSE-GY 160
Cdd:PRK00011  81 KELFGA---EY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEEtGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 161 VDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILR 240
Cdd:PRK00011 152 IDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 241 GPRSALIFFNKKRnpgIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVT 320
Cdd:PRK00011 232 GPRGGLILTNDEE---LAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVS 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 321 NGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVS-PSGIRIGTPALTTRGCKEKDMEFIADMLLKAIl 399
Cdd:PRK00011 309 GGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFvTSGIRIGTPAITTRGFKEAEMKEIAELIADVL- 387
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 124806534 400 ltdelqqkygkklvdfkKGLVNNPKIDELKKEVVQWAKNLP 440
Cdd:PRK00011 388 -----------------DNPDDEAVIEEVKEEVKELCKRFP 411
PLN02271 PLN02271
serine hydroxymethyltransferase
4-436 3.79e-166

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 480.07  E-value: 3.79e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   4 NDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALE 83
Cdd:PLN02271 126 NQPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALA 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  84 AFNVSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEK-KKVSITSDLFESKLYKCNSE-GYV 161
Cdd:PLN02271 206 AFGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGgKKVSGASIFFESLPYKVNPQtGYI 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 162 DMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRG 241
Cdd:PLN02271 286 DYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRG 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 242 PRSALIFFNKKRNP----------------GIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSK 305
Cdd:PLN02271 366 PRGGIIFYRKGPKLrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQ 445
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 306 ALAECLLKRNLDLVTNGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEK 385
Cdd:PLN02271 446 ALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLES 525
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124806534 386 DMEFIADMLLKAILLTDELQQKYGKKLVDFKKGLVNNPKIDELKKEVVQWA 436
Cdd:PLN02271 526 DFETIADFLLRAAQIASAVQREHGKLQKEFLKGLQNNKDIVELRNRVEAFA 576
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
1-415 3.97e-157

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 450.56  E-value: 3.97e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534   1 MFNNDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKR 80
Cdd:PRK13034   3 FFFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIER 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  81 ALEAFNVSEeewgVNVQPLSGSAANvQALY-ALVGVKGKIMGMHLCSGGHLTHGffdekKKVSITSDLFESKLYKCNSE- 158
Cdd:PRK13034  83 AKQLFGCDY----ANVQPHSGSQAN-GAVYlALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLt 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 159 GYVDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKI 238
Cdd:PRK13034 153 GLIDYDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 239 LRGPRSALIFFNkkrNPGIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDL 318
Cdd:PRK13034 233 LRGPRGGMILTN---DEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDL 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 319 VTNGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDcvSP---SGIRIGTPALTTRGCKEKDMEFIADMLL 395
Cdd:PRK13034 310 VSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTE--SPfvtSGIRIGTPAGTTRGFGEAEFREIANWIL 387
                        410       420
                 ....*....|....*....|..
gi 124806534 396 KAI--LLTDELQQKYGKKLVDF 415
Cdd:PRK13034 388 DVLddLGNAALEQRVRKEVKAL 409
PRK13580 PRK13580
glycine hydroxymethyltransferase;
20-396 3.21e-105

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 320.83  E-value: 3.21e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  20 KEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALEAFNVSEeewgVNVQPL 99
Cdd:PRK13580  43 QELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEH----AYVQPH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 100 SGSAANVQALYALV------------GVKG-------------------KIMGMHLCSGGHLTHGFfdekkKVSITSDLF 148
Cdd:PRK13580 119 SGADANLVAFWAILahkvespaleklGAKTvndlteedwealraelgnqRLLGMSLDSGGHLTHGF-----RPNISGKMF 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 149 ESKLYKCNSE-GYVDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLN---NP 224
Cdd:PRK13580 194 HQRSYGVDPDtGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTgdeDP 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 225 FTYADVVTTTTHKILRGPRSALIFFNKKRNPGIDQKInssvfPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNS 304
Cdd:PRK13580 274 VPHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-----PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNA 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 305 KALAECLLKRNLDLVTNGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCV-SPSGIRIGTPALTTRGCK 383
Cdd:PRK13580 349 RALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAwYTSGIRLGTPALTTLGMG 428
                        410
                 ....*....|...
gi 124806534 384 EKDMEFIADMLLK 396
Cdd:PRK13580 429 SDEMDEVAELIVK 441
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
74-250 9.08e-16

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 74.73  E-value: 9.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534  74 EELCYKRALEAFNVSEeeWGVNVQPlSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHgfFDEKKKvsitsdlFESKLY 153
Cdd:cd01494    2 LEELEEKLARLLQPGN--DKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV--AAELAG-------AKPVPV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124806534 154 KCNSEGYVDMES--VRNLALSFQPKVIICGYTSYPRDI--DYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYAD 229
Cdd:cd01494   70 PVDDAGYGGLDVaiLEELKAKPNVALIVITPNTTSGGVlvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGAD 149
                        170       180
                 ....*....|....*....|.
gi 124806534 230 VVTTTTHKILRGPRSALIFFN 250
Cdd:cd01494  150 VVTFSLHKNLGGEGGGVVIVK 170
 
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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