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Conserved domains on  [gi|1034600889|ref|XP_016880447|]
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serine hydroxymethyltransferase, cytosolic isoform X2 [Homo sapiens]

Protein Classification

serine hydroxymethyltransferase( domain architecture ID 11477583)

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
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
24-441 0e+00

serine hydroxymethyltransferase; Provisional


:

Pssm-ID: 215639  Cd Length: 475  Bit Score: 736.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226   13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226   93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226  173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 264 AGMIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTE 305
Cdd:PLN03226  253 GGMIFFRKGPkppkgqgegavydyedkinfavfpglqggphnhtiaalAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 306 LGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHF 385
Cdd:PLN03226  333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034600889 386 IHRGIELTLQIQSDTGVRatLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL 441
Cdd:PLN03226  413 LHRAVTIALKIQKEHGKK--LKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGF 466
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
24-441 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 736.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226   13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226   93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226  173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 264 AGMIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTE 305
Cdd:PLN03226  253 GGMIFFRKGPkppkgqgegavydyedkinfavfpglqggphnhtiaalAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 306 LGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHF 385
Cdd:PLN03226  333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034600889 386 IHRGIELTLQIQSDTGVRatLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL 441
Cdd:PLN03226  413 LHRAVTIALKIQKEHGKK--LKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGF 466
SHMT pfam00464
Serine hydroxymethyltransferase;
26-386 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 683.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  26 LKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYK 105
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 106 LDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQ 185
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 186 LEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG 265
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 266 MIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTELG 307
Cdd:pfam00464 241 MIFYRKGVksvdktgkeilyelekkinsavfpglqggphnhviaakAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034600889 308 YKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 386
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
27-414 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: 583.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  27 KDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKL 106
Cdd:cd00378     1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 107 DpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTdkkKISATSIFFESMPYKVNPDTGYINYDQL 186
Cdd:cd00378    81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 187 EENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGM 266
Cdd:cd00378   154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 267 IFYRK-------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL 321
Cdd:cd00378   234 ILTRKgelakkinsavfpglqggphlhviaAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 322 VDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIeltlqiqSDT 400
Cdd:cd00378   314 VDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARAL-------KDA 386
                         410
                  ....*....|....
gi 1034600889 401 GVRATLKEFKERLA 414
Cdd:cd00378   387 EDVAVAEEVRKEVA 400
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
21-440 6.78e-179

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: 505.72  E-value: 6.78e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  21 MLaQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:COG0112     1 ML-SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:COG0112    80 KELFGAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:COG0112   151 IDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLR 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 261 GCRAGMIFYRK------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSD 316
Cdd:COG0112   231 GPRGGLILCNEelakkidsavfpglqggplmhviaAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTD 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 317 NHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGieltlq 395
Cdd:COG0112   311 NHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADV------ 384
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1034600889 396 iqsdtgvratlkefkerLAGDKYQAAVQALREEVESFASLFPLPG 440
Cdd:COG0112   385 -----------------LDNPEDEAVLAEVREEVKELCKRFPLYP 412
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
24-441 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 736.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226   13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226   93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226  173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 264 AGMIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTE 305
Cdd:PLN03226  253 GGMIFFRKGPkppkgqgegavydyedkinfavfpglqggphnhtiaalAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 306 LGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHF 385
Cdd:PLN03226  333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034600889 386 IHRGIELTLQIQSDTGVRatLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL 441
Cdd:PLN03226  413 LHRAVTIALKIQKEHGKK--LKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGF 466
SHMT pfam00464
Serine hydroxymethyltransferase;
26-386 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 683.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  26 LKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYK 105
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 106 LDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQ 185
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 186 LEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG 265
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 266 MIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTELG 307
Cdd:pfam00464 241 MIFYRKGVksvdktgkeilyelekkinsavfpglqggphnhviaakAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034600889 308 YKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 386
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
24-441 0e+00

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 679.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PTZ00094   13 QSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDtGYINY 183
Cdd:PTZ00094   93 FGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLIDY 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PTZ00094  172 DKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 264 AGMIFYRK----------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGS 315
Cdd:PTZ00094  252 SGLIFYRKkvkpdienkineavfpglqggphnhqiaAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGT 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 316 DNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIELTLQ 395
Cdd:PTZ00094  332 DNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVKLAQE 411
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1034600889 396 IQSDTGvrATLKEFKERLAGDKyqaAVQALREEVESFASLFPLPGL 441
Cdd:PTZ00094  412 IQKQVG--KKLVDFKKALEKNP---ELQKLRQEVVEFASQFPFPGI 452
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
27-414 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: 583.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  27 KDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKL 106
Cdd:cd00378     1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 107 DpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTdkkKISATSIFFESMPYKVNPDTGYINYDQL 186
Cdd:cd00378    81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 187 EENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGM 266
Cdd:cd00378   154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 267 IFYRK-------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL 321
Cdd:cd00378   234 ILTRKgelakkinsavfpglqggphlhviaAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 322 VDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIeltlqiqSDT 400
Cdd:cd00378   314 VDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARAL-------KDA 386
                         410
                  ....*....|....
gi 1034600889 401 GVRATLKEFKERLA 414
Cdd:cd00378   387 EDVAVAEEVRKEVA 400
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
21-440 6.78e-179

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: 505.72  E-value: 6.78e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  21 MLaQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:COG0112     1 ML-SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:COG0112    80 KELFGAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:COG0112   151 IDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLR 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 261 GCRAGMIFYRK------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSD 316
Cdd:COG0112   231 GPRGGLILCNEelakkidsavfpglqggplmhviaAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTD 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 317 NHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGieltlq 395
Cdd:COG0112   311 NHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADV------ 384
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1034600889 396 iqsdtgvratlkefkerLAGDKYQAAVQALREEVESFASLFPLPG 440
Cdd:COG0112   385 -----------------LDNPEDEAVLAEVREEVKELCKRFPLYP 412
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
21-440 2.67e-178

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 504.22  E-value: 2.67e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  21 MLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:PRK00011    1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:PRK00011   81 KELFGAE----YANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:PRK00011  152 IDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 261 GCRAGMIFYRK-------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGS 315
Cdd:PRK00011  232 GPRGGLILTNDeelakkinsavfpgiqggplmhviaAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 316 DNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIhrgieltl 394
Cdd:PRK00011  312 DNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELI-------- 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1034600889 395 qiqsdtgvratlkefKERLAGDKYQAAVQALREEVESFASLFPLPG 440
Cdd:PRK00011  384 ---------------ADVLDNPDDEAVIEEVKEEVKELCKRFPLYK 414
PLN02271 PLN02271
serine hydroxymethyltransferase
24-440 2.86e-170

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 490.47  E-value: 2.86e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN02271  127 QPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAA 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMT-DKKKISATSIFFESMPYKVNPDTGYIN 182
Cdd:PLN02271  207 FGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTpGGKKVSGASIFFESLPYKVNPQTGYID 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 183 YDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGC 262
Cdd:PLN02271  287 YDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGP 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 263 RAGMIFYRKG--------------------------------------------VAVALKQAMTLEFKVYQHQVVANCRA 298
Cdd:PLN02271  367 RGGIIFYRKGpklrkqgmllshgddnshydfeekinfavfpslqggphnnhiaaLAIALKQVATPEYKAYMQQVKKNAQA 446
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 299 LSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKD 378
Cdd:PLN02271  447 LASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESD 526
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034600889 379 FQKVAHFIHRGIELTLQIQSDTGvratlKEFKERLAGDKYQAAVQALREEVESFASLFPLPG 440
Cdd:PLN02271  527 FETIADFLLRAAQIASAVQREHG-----KLQKEFLKGLQNNKDIVELRNRVEAFASQFAMPG 583
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
23-439 5.91e-155

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 445.17  E-value: 5.91e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  23 AQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQ 102
Cdd:PRK13034    6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 103 AYkldpQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGYIN 182
Cdd:PRK13034   86 LF----GCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 183 YDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGC 262
Cdd:PRK13034  157 YDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 263 RAGMI------FYRK-------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDN 317
Cdd:PRK13034  237 RGGMIltndeeIAKKinsavfpglqggplmhviaAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 318 HLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIhrgieltLQI 396
Cdd:PRK13034  317 HLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEFREIANWI-------LDV 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1034600889 397 QSDTGvratlkefkerlagdkyQAAVQA-LREEVESFASLFPLP 439
Cdd:PRK13034  390 LDDLG-----------------NAALEQrVRKEVKALCSRFPIY 416
PRK13580 PRK13580
glycine hydroxymethyltransferase;
37-441 5.72e-106

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 322.76  E-value: 5.72e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  37 IKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCwgvnVQ 116
Cdd:PRK13580   41 IRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAY----VQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 117 PYSGSPANFAVYTAL---------VEPHG----------------------RIMGLDLPDGGHLTHGFmtdKKKISatSI 165
Cdd:PRK13580  117 PHSGADANLVAFWAIlahkvespaLEKLGaktvndlteedwealraelgnqRLLGMSLDSGGHLTHGF---RPNIS--GK 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 166 FFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVV---- 241
Cdd:PRK13580  192 MFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFtgde 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 242 -PSPFEHchVVTTTTHKTLRGCRAGMI--------FYRKGV---------------AVALKQAMTLEFKVYQHQVVANCR 297
Cdd:PRK13580  272 dPVPHAD--IVTTTTHKTLRGPRGGLVlakkeyadAVDKGCplvlggplphvmaakAVALAEARTPEFQKYAQQVVDNAR 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 298 ALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRS-ALRPSGLRLGTPALTSRGLLE 376
Cdd:PRK13580  350 ALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNgAWYTSGIRLGTPALTTLGMGS 429
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034600889 377 KDFQKVAHFIHRgieltlqIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPL-PGL 441
Cdd:PRK13580  430 DEMDEVAELIVK-------VLSNTTPGTTAEGAPSKAKYELDEGVAQEVRARVAELLARFPLyPEI 488
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
92-270 2.54e-29

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: 112.48  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889  92 LETLCQKRALQAYKldPQCWGVNVQPySGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHgfmtdkkkiSATSIFFESMP 171
Cdd:cd01494     1 KLEELEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600889 172 YKVNPDTGY-INYDQLEENARLFHPKLIIAGTSCYSRNLEYA--RLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHC 248
Cdd:cd01494    69 VPVDDAGYGgLDVAILEELKAKPNVALIVITPNTTSGGVLVPlkEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGA 148
                         170       180
                  ....*....|....*....|..
gi 1034600889 249 HVVTTTTHKTLRGCRAGMIFYR 270
Cdd:cd01494   149 DVVTFSLHKNLGGEGGGVVIVK 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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