|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
24-480 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 816.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226 13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226 93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 264 AGMIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALT 343
Cdd:PLN03226 253 GGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 344 ELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAH 423
Cdd:PLN03226 332 SKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAE 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034600887 424 FIHRGIELTLQIQSDTGVRatLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL 480
Cdd:PLN03226 412 FLHRAVTIALKIQKEHGKK--LKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGF 466
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
26-425 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 769.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 26 LKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYK 105
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 106 LDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQ 185
Cdd:pfam00464 81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 186 LEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG 265
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 266 MIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTEL 345
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 346 GYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 425
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
27-453 |
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: 632.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 27 KDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKL 106
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 107 DpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTdkkKISATSIFFESMPYKVNPDTGYINYDQL 186
Cdd:cd00378 81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 187 EENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGM 266
Cdd:cd00378 154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 267 IFYRKGvksvdpktgkeilyNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELG 346
Cdd:cd00378 234 ILTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 347 YKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 425
Cdd:cd00378 300 FKVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFI 379
|
410 420
....*....|....*....|....*...
gi 1034600887 426 HRGIeltlqiqSDTGVRATLKEFKERLA 453
Cdd:cd00378 380 ARAL-------KDAEDVAVAEEVRKEVA 400
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
21-479 |
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: 553.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 21 MLaQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:COG0112 1 ML-SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:COG0112 80 KELFGAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:COG0112 151 IDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 261 GCRAGMIFyrkgvksvdpkTGKEilynLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSE 340
Cdd:COG0112 231 GPRGGLIL-----------CNEE----LAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 341 ALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQ 419
Cdd:COG0112 296 ALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEME 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 420 KVAHFIHRGieltlqiqsdtgvratlkefkerLAGDKYQAAVQALREEVESFASLFPLPG 479
Cdd:COG0112 376 EIAELIADV-----------------------LDNPEDEAVLAEVREEVKELCKRFPLYP 412
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
24-480 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 816.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN03226 13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINY 183
Cdd:PLN03226 93 FRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMPYRLDESTGLIDY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 264 AGMIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALT 343
Cdd:PLN03226 253 GGMIFFRKGPKPPK-GQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 344 ELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAH 423
Cdd:PLN03226 332 SKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRGLVEKDFEKVAE 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034600887 424 FIHRGIELTLQIQSDTGVRatLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL 480
Cdd:PLN03226 412 FLHRAVTIALKIQKEHGKK--LKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGF 466
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
26-425 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 769.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 26 LKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYK 105
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 106 LDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQ 185
Cdd:pfam00464 81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 186 LEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG 265
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 266 MIFYRKGVKSVDpKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTEL 345
Cdd:pfam00464 241 MIFYRKGVKSVD-KTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 346 GYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 425
Cdd:pfam00464 320 GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
24-480 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 737.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PTZ00094 13 QSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDtGYINY 183
Cdd:PTZ00094 93 FGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLIDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 184 DQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCR 263
Cdd:PTZ00094 172 DKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 264 AGMIFYRKGVKSvdpktgkeilyNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALT 343
Cdd:PTZ00094 252 SGLIFYRKKVKP-----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 344 ELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAH 423
Cdd:PTZ00094 321 KRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVAD 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034600887 424 FIHRGIELTLQIQSDTGvrATLKEFKERLAGDKyqaAVQALREEVESFASLFPLPGL 480
Cdd:PTZ00094 401 FLDRAVKLAQEIQKQVG--KKLVDFKKALEKNP---ELQKLRQEVVEFASQFPFPGI 452
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
27-453 |
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: 632.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 27 KDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKL 106
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 107 DpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTdkkKISATSIFFESMPYKVNPDTGYINYDQL 186
Cdd:cd00378 81 E----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 187 EENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGM 266
Cdd:cd00378 154 EKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 267 IFYRKGvksvdpktgkeilyNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELG 346
Cdd:cd00378 234 ILTRKG--------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 347 YKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQKVAHFI 425
Cdd:cd00378 300 FKVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDpSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFI 379
|
410 420
....*....|....*....|....*...
gi 1034600887 426 HRGIeltlqiqSDTGVRATLKEFKERLA 453
Cdd:cd00378 380 ARAL-------KDAEDVAVAEEVRKEVA 400
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
21-479 |
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: 553.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 21 MLaQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:COG0112 1 ML-SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:COG0112 80 KELFGAE----HANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:COG0112 151 IDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 261 GCRAGMIFyrkgvksvdpkTGKEilynLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSE 340
Cdd:COG0112 231 GPRGGLIL-----------CNEE----LAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 341 ALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQ 419
Cdd:COG0112 296 ALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDpRSPFVTSGIRIGTPAVTTRGMKEAEME 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 420 KVAHFIHRGieltlqiqsdtgvratlkefkerLAGDKYQAAVQALREEVESFASLFPLPG 479
Cdd:COG0112 376 EIAELIADV-----------------------LDNPEDEAVLAEVREEVKELCKRFPLYP 412
|
|
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
21-479 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 552.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 21 MLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRA 100
Cdd:PRK00011 1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 101 LQAYKLDpqcwGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGY 180
Cdd:PRK00011 81 KELFGAE----YANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 181 INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLR 260
Cdd:PRK00011 152 IDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 261 GCRAGMIFyrkgvkSVDPKTGKEilynleslINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSE 340
Cdd:PRK00011 232 GPRGGLIL------TNDEELAKK--------INSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 341 ALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDFQ 419
Cdd:PRK00011 298 ALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDpRSPFVTSGIRIGTPAITTRGFKEAEMK 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 420 KVAHFIhrgieltlqiqsdtgvratlkefKERLAGDKYQAAVQALREEVESFASLFPLPG 479
Cdd:PRK00011 378 EIAELI-----------------------ADVLDNPDDEAVIEEVKEEVKELCKRFPLYK 414
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
24-479 |
0e+00 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 542.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 24 QPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQA 103
Cdd:PLN02271 127 QPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 104 YKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMT-DKKKISATSIFFESMPYKVNPDTGYIN 182
Cdd:PLN02271 207 FGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTpGGKKVSGASIFFESLPYKVNPQTGYID 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 183 YDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGC 262
Cdd:PLN02271 287 YDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 263 RAGMIFYRKGVKSVDP-----KTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRA 337
Cdd:PLN02271 367 RGGIIFYRKGPKLRKQgmllsHGDDNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQA 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 338 LSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKD 417
Cdd:PLN02271 447 LASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGDNGTISPGGVRIGTPAMTSRGCLESD 526
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034600887 418 FQKVAHFIHRGIELTLQIQSDTGvratlKEFKERLAGDKYQAAVQALREEVESFASLFPLPG 479
Cdd:PLN02271 527 FETIADFLLRAAQIASAVQREHG-----KLQKEFLKGLQNNKDIVELRNRVEAFASQFAMPG 583
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
23-478 |
1.61e-170 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 486.39 E-value: 1.61e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 23 AQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQ 102
Cdd:PRK13034 6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 103 AYkldpQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGfmtdkKKISATSIFFESMPYKVNPDTGYIN 182
Cdd:PRK13034 86 LF----GCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 183 YDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGC 262
Cdd:PRK13034 157 YDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 263 RAGMifyrkgvksvdpktgkeILYNLESL---INSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALS 339
Cdd:PRK13034 237 RGGM-----------------ILTNDEEIakkINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 340 EALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGD-RSALRPSGLRLGTPALTSRGLLEKDF 418
Cdd:PRK13034 300 EVLKERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDtESPFVTSGIRIGTPAGTTRGFGEAEF 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034600887 419 QKVAHFIhrgieltLQIQSDTGvratlkefkerlagdkyQAAVQA-LREEVESFASLFPLP 478
Cdd:PRK13034 380 REIANWI-------LDVLDDLG-----------------NAALEQrVRKEVKALCSRFPIY 416
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
37-480 |
6.74e-111 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 337.01 E-value: 6.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 37 IKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCwgvnVQ 116
Cdd:PRK13580 41 IRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAY----VQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 117 PYSGSPANFAVYTAL---------VEPHG----------------------RIMGLDLPDGGHLTHGFmtdKKKISatSI 165
Cdd:PRK13580 117 PHSGADANLVAFWAIlahkvespaLEKLGaktvndlteedwealraelgnqRLLGMSLDSGGHLTHGF---RPNIS--GK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 166 FFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVV---- 241
Cdd:PRK13580 192 MFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFtgde 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 242 -PSPFEHchVVTTTTHKTLRGCRAGMIFyrkgvksvdpkTGKEilynLESLINSAVfPGLQGGPHNHAIAGVAVALKQAM 320
Cdd:PRK13580 272 dPVPHAD--IVTTTTHKTLRGPRGGLVL-----------AKKE----YADAVDKGC-PLVLGGPLPHVMAAKAVALAEAR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 321 TLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRS-ALRPS 399
Cdd:PRK13580 334 TPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNgAWYTS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 400 GLRLGTPALTSRGLLEKDFQKVAHFIHRgieltlqIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPL-P 478
Cdd:PRK13580 414 GIRLGTPALTTLGMGSDEMDEVAELIVK-------VLSNTTPGTTAEGAPSKAKYELDEGVAQEVRARVAELLARFPLyP 486
|
..
gi 1034600887 479 GL 480
Cdd:PRK13580 487 EI 488
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
92-270 |
6.53e-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: 112.09 E-value: 6.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 92 LETLCQKRALQAYKldPQCWGVNVQPySGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHgfmtdkkkiSATSIFFESMP 171
Cdd:cd01494 1 KLEELEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 172 YKVNPDTGY-INYDQLEENARLFHPKLIIAGTSCYSRNLEYA--RLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHC 248
Cdd:cd01494 69 VPVDDAGYGgLDVAILEELKAKPNVALIVITPNTTSGGVLVPlkEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGA 148
|
170 180
....*....|....*....|..
gi 1034600887 249 HVVTTTTHKTLRGCRAGMIFYR 270
Cdd:cd01494 149 DVVTFSLHKNLGGEGGGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
171-404 |
1.78e-03 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 40.40 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 171 PYKVNPDTGYINYDQLEENARLFHPKLII-------AGTsCYSRNlEYARLRKIADENGAYLMADMAHiSGLVAAGVVPS 243
Cdd:cd00609 109 PVPLDEEGGFLLDLELLEAAKTPKTKLLYlnnpnnpTGA-VLSEE-ELEELAELAKKHGILIISDEAY-AELVYDGEPPP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 244 PFEhcHVVTTTTHKTLRGC---------RAGMIFYRKgvksvdpktgKEILYNLESLInsavfPGLQGGPHNHAIAGVAV 314
Cdd:cd00609 186 ALA--LLDAYERVIVLRSFsktfglpglRIGYLIAPP----------EELLERLKKLL-----PYTTSGPSTLSQAAAAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034600887 315 ALKQAMTlEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLrSKGTDGGRAEKVLEACSIACNKntcPGDRS 394
Cdd:cd00609 249 ALDDGEE-HLEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDL-PEGDDEEFLERLLLEAGVVVRP---GSAFG 323
|
250
....*....|
gi 1034600887 395 ALRPSGLRLG 404
Cdd:cd00609 324 EGGEGFVRLS 333
|
|
|