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Conserved domains on  [gi|22547189|ref|NP_683718|]
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serine hydroxymethyltransferase, cytosolic isoform 2 [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)

CATH:  3.90.1150.10|3.40.640.10
EC:  2.1.2.1
Gene Ontology:  GO:0004372|GO:0030170|GO:0070905|GO:0008270|GO:0019264|GO:0048027
PubMed:  12686103|2201683|10800595|10673430

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 22547189   24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  264 AGMIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTE 305
Cdd:PLN03226 253 GGMIFFRKGPkppkgqgegavydyedkinfavfpglqggphnhtiaalAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  306 LGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHF 385
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22547189  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 22547189   24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  264 AGMIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTE 305
Cdd:PLN03226 253 GGMIFFRKGPkppkgqgegavydyedkinfavfpglqggphnhtiaalAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  306 LGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHF 385
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22547189  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 22547189    26 LKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYK 105
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189   106 LDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQ 185
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189   186 LEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG 265
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189   266 MIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTELG 307
Cdd:pfam00464 241 MIFYRKGVksvdktgkeilyelekkinsavfpglqggphnhviaakAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22547189   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 22547189  27 KDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKL 106
Cdd:cd00378   1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 107 DpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTdkkKISATSIFFESMPYKVNPDTGYINYDQL 186
Cdd:cd00378  81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 187 EENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGM 266
Cdd:cd00378 154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 267 IFYRK-------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL 321
Cdd:cd00378 234 ILTRKgelakkinsavfpglqggphlhviaAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVL 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 322 VDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIeltlqiqSDT 400
Cdd:cd00378 314 VDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARAL-------KDA 386

                       410
                ....*....|....
gi 22547189 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 22547189  21 MLaQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:COG0112   1 ML-SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:COG0112  80 KELFGAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:COG0112 151 IDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLR 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 261 GCRAGMIFYRK------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSD 316
Cdd:COG0112 231 GPRGGLILCNEelakkidsavfpglqggplmhviaAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTD 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 317 NHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGieltlq 395
Cdd:COG0112 311 NHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADV------ 384

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 22547189 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 22547189   24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226  13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226  93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  264 AGMIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTE 305
Cdd:PLN03226 253 GGMIFFRKGPkppkgqgegavydyedkinfavfpglqggphnhtiaalAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  306 LGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHF 385
Cdd:PLN03226 333 KGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22547189  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 22547189    26 LKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYK 105
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189   106 LDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQ 185
Cdd:pfam00464  81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189   186 LEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG 265
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189   266 MIFYRKGV--------------------------------------AVALKQAMTLEFKVYQHQVVANCRALSEALTELG 307
Cdd:pfam00464 241 MIFYRKGVksvdktgkeilyelekkinsavfpglqggphnhviaakAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22547189   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 22547189   24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PTZ00094  13 QSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDtGYINY 183
Cdd:PTZ00094  93 FGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLIDY 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PTZ00094 172 DKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPR 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  264 AGMIFYRK----------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGS 315
Cdd:PTZ00094 252 SGLIFYRKkvkpdienkineavfpglqggphnhqiaAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGT 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  316 DNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIELTLQ 395
Cdd:PTZ00094 332 DNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVKLAQE 411

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 22547189  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 22547189  27 KDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKL 106
Cdd:cd00378   1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 107 DpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTdkkKISATSIFFESMPYKVNPDTGYINYDQL 186
Cdd:cd00378  81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 187 EENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGM 266
Cdd:cd00378 154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 267 IFYRK-------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL 321
Cdd:cd00378 234 ILTRKgelakkinsavfpglqggphlhviaAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVL 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 322 VDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIeltlqiqSDT 400
Cdd:cd00378 314 VDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARAL-------KDA 386

                       410
                ....*....|....
gi 22547189 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 22547189  21 MLaQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:COG0112   1 ML-SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:COG0112  80 KELFGAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:COG0112 151 IDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLR 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 261 GCRAGMIFYRK------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSD 316
Cdd:COG0112 231 GPRGGLILCNEelakkidsavfpglqggplmhviaAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTD 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 317 NHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGieltlq 395
Cdd:COG0112 311 NHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADV------ 384

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 22547189 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 22547189   21 MLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:PRK00011   1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:PRK00011  81 KELFGAE----YANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:PRK00011 152 IDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLR 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  261 GCRAGMIFYRK-------------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGS 315
Cdd:PRK00011 232 GPRGGLILTNDeelakkinsavfpgiqggplmhviaAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGT 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  316 DNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIhrgieltl 394
Cdd:PRK00011 312 DNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELI-------- 383

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 22547189  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 22547189   24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN02271 127 QPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAA 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMT-DKKKISATSIFFESMPYKVNPDTGYIN 182
Cdd:PLN02271 207 FGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTpGGKKVSGASIFFESLPYKVNPQTGYID 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  183 YDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGC 262
Cdd:PLN02271 287 YDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGP 366

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  263 RAGMIFYRKG--------------------------------------------VAVALKQAMTLEFKVYQHQVVANCRA 298
Cdd:PLN02271 367 RGGIIFYRKGpklrkqgmllshgddnshydfeekinfavfpslqggphnnhiaaLAIALKQVATPEYKAYMQQVKKNAQA 446

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  299 LSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKD 378
Cdd:PLN02271 447 LASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESD 526

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22547189  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 22547189   23 AQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQ 102
Cdd:PRK13034   6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  103 AYkldpQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGYIN 182
Cdd:PRK13034  86 LF----GCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLID 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  183 YDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGC 262
Cdd:PRK13034 157 YDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  263 RAGMI------FYRK-------------------GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDN 317
Cdd:PRK13034 237 RGGMIltndeeIAKKinsavfpglqggplmhviaAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDN 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  318 HLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIhrgieltLQI 396
Cdd:PRK13034 317 HLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEFREIANWI-------LDV 389

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 22547189  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 22547189   37 IKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCwgvnVQ 116
Cdd:PRK13580  41 IRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAY----VQ 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  117 PYSGSPANFAVYTAL---------VEPHG----------------------RIMGLDLPDGGHLTHGFmtdKKKISatSI 165
Cdd:PRK13580 117 PHSGADANLVAFWAIlahkvespaLEKLGaktvndlteedwealraelgnqRLLGMSLDSGGHLTHGF---RPNIS--GK 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  166 FFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVV---- 241
Cdd:PRK13580 192 MFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFtgde 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  242 -PSPFEHchVVTTTTHKTLRGCRAGMI--------FYRKGV---------------AVALKQAMTLEFKVYQHQVVANCR 297
Cdd:PRK13580 272 dPVPHAD--IVTTTTHKTLRGPRGGLVlakkeyadAVDKGCplvlggplphvmaakAVALAEARTPEFQKYAQQVVDNAR 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189  298 ALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRS-ALRPSGLRLGTPALTSRGLLE 376
Cdd:PRK13580 350 ALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNgAWYTSGIRLGTPALTTLGMGS 429

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22547189  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 22547189  92 LETLCQKRALQAYKldPQCWGVNVQPySGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHgfmtdkkkiSATSIFFESMP 171
Cdd:cd01494   1 KLEELEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVP 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22547189 172 YKVNPDTGY-INYDQLEENARLFHPKLIIAGTSCYSRNLEYA--RLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHC 248
Cdd:cd01494  69 VPVDDAGYGgLDVAILEELKAKPNVALIVITPNTTSGGVLVPlkEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGA 148

                       170       180
                ....*....|....*....|..
gi 22547189 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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