|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
4-419 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 805.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 4 TNLDFLAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRA 83
Cdd:PRK00011 1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 84 KELFGAAHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSPVNVSGKWFEVCHYGVSQETEQLDYGQIREL 163
Cdd:PRK00011 81 KELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 164 ALKERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGGLILT 243
Cdd:PRK00011 161 ALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 244 NQSDLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRELKIVSGGTDNHVLLVDL 323
Cdd:PRK00011 241 NDEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 324 RSIGMTGKRADQLVSGVKITANKNTVPFDPESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNIIADRLLNREDEQVATQCR 403
Cdd:PRK00011 321 RSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVK 400
|
410
....*....|....*.
gi 332350376 404 QRVAQLCDRFPLYPHL 419
Cdd:PRK00011 401 EEVKELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
6-419 |
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: 785.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 6 LDFLAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKE 85
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 86 LFGAAHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSPVNVSGKWFEVCHYGVSQETEQLDYGQIRELAL 165
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 166 KERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGGLILTNQ 245
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 246 sDLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRELKIVSGGTDNHVLLVDLRS 325
Cdd:COG0112 242 -ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 326 IGMTGKRADQLVSGVKITANKNTVPFDPESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNIIADRLLNREDEQVATQCRQR 405
Cdd:COG0112 321 KGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREE 400
|
410
....*....|....
gi 332350376 406 VAQLCDRFPLYPHL 419
Cdd:COG0112 401 VKELCKRFPLYPDL 414
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
10-409 |
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: 648.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 10 AETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKELFGA 89
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 90 AHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSP--VNVSGKWFEVCHYGVSQETEQLDYGQIRELALKE 167
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 168 RPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGGLILTNQSD 247
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 248 LGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRELKIVSGGTDNHVLLVDLRSIG 327
Cdd:cd00378 241 LAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 328 MTGKRADQLVSGVKITANKNTVPFDPESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNIIADRLLNREDEQVATQCRQRVA 407
Cdd:cd00378 321 ITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVA 400
|
..
gi 332350376 408 QL 409
Cdd:cd00378 401 EL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
9-386 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 599.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 9 LAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKELFG 88
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 89 A----AHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSPVNV-----SGKWFEVCHYGVSQETEQLDYGQ 159
Cdd:pfam00464 81 LdpakWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 160 IRELALKERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGG 239
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 240 LILTNQS-------------DLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRE 306
Cdd:pfam00464 241 MIFYRKGvksvdktgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 307 LKIVSGGTDNHVLLVDLRSIGMTGKRADQLVSGVKITANKNTVPFDpESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNII 386
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
4-419 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 805.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 4 TNLDFLAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRA 83
Cdd:PRK00011 1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 84 KELFGAAHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSPVNVSGKWFEVCHYGVSQETEQLDYGQIREL 163
Cdd:PRK00011 81 KELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 164 ALKERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGGLILT 243
Cdd:PRK00011 161 ALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 244 NQSDLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRELKIVSGGTDNHVLLVDL 323
Cdd:PRK00011 241 NDEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 324 RSIGMTGKRADQLVSGVKITANKNTVPFDPESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNIIADRLLNREDEQVATQCR 403
Cdd:PRK00011 321 RSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVK 400
|
410
....*....|....*.
gi 332350376 404 QRVAQLCDRFPLYPHL 419
Cdd:PRK00011 401 EEVKELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
6-419 |
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: 785.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 6 LDFLAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKE 85
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 86 LFGAAHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSPVNVSGKWFEVCHYGVSQETEQLDYGQIRELAL 165
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 166 KERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGGLILTNQ 245
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 246 sDLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRELKIVSGGTDNHVLLVDLRS 325
Cdd:COG0112 242 -ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 326 IGMTGKRADQLVSGVKITANKNTVPFDPESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNIIADRLLNREDEQVATQCRQR 405
Cdd:COG0112 321 KGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREE 400
|
410
....*....|....
gi 332350376 406 VAQLCDRFPLYPHL 419
Cdd:COG0112 401 VKELCKRFPLYPDL 414
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
7-416 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 705.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 7 DFLAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKEL 86
Cdd:PRK13034 7 DSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 87 FGAAHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSPVNVSGKWFEVCHYGVSQETEQLDYGQIRELALK 166
Cdd:PRK13034 87 FGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAKE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 167 ERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGGLILTNQS 246
Cdd:PRK13034 167 HKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 247 DLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRELKIVSGGTDNHVLLVDLRSI 326
Cdd:PRK13034 247 EIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRPK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 327 GMTGKRADQLVSGVKITANKNTVPFDPESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNIIADRLLNREDEQVATQCRQRV 406
Cdd:PRK13034 327 GLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKEV 406
|
410
....*....|
gi 332350376 407 AQLCDRFPLY 416
Cdd:PRK13034 407 KALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
10-409 |
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: 648.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 10 AETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKELFGA 89
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 90 AHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSP--VNVSGKWFEVCHYGVSQETEQLDYGQIRELALKE 167
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 168 RPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGGLILTNQSD 247
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 248 LGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRELKIVSGGTDNHVLLVDLRSIG 327
Cdd:cd00378 241 LAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 328 MTGKRADQLVSGVKITANKNTVPFDPESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNIIADRLLNREDEQVATQCRQRVA 407
Cdd:cd00378 321 ITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVA 400
|
..
gi 332350376 408 QL 409
Cdd:cd00378 401 EL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
9-386 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 599.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 9 LAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKELFG 88
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 89 A----AHANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGSPVNV-----SGKWFEVCHYGVSQETEQLDYGQ 159
Cdd:pfam00464 81 LdpakWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 160 IRELALKERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRGG 239
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 240 LILTNQS-------------DLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRE 306
Cdd:pfam00464 241 MIFYRKGvksvdktgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 307 LKIVSGGTDNHVLLVDLRSIGMTGKRADQLVSGVKITANKNTVPFDpESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNII 386
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
1-386 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 511.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 1 MTQTNLDFLAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAI 80
Cdd:PTZ00094 7 LVLPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 81 DRAKELFGAAH----ANVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHG-----SPVNVSGKWFEVCHYGVSQE 151
Cdd:PTZ00094 87 KRALEAFGLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 152 TEqLDYGQIRELALKERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHK 231
Cdd:PTZ00094 167 GL-IDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 232 TLRGPRGGLILTNQ---SDLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQNRELK 308
Cdd:PTZ00094 246 SLRGPRSGLIFYRKkvkPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYD 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332350376 309 IVSGGTDNHVLLVDLRSIGMTGKRADQLVSGVKITANKNTVPFDpESPFVTSGLRLGSPAMTTRGMGVAEFTEIGNII 386
Cdd:PTZ00094 326 LVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGD-KSALNPSGVRLGTPALTTRGAKEKDFKFVADFL 402
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
3-422 |
4.32e-180 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 511.12 E-value: 4.32e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 3 QTNLDFLAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDR 82
Cdd:PRK13580 24 LAALDVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 83 AKELFGAAHANVQPHSGAQANFAVFLALL------------------------------KPGD-KIMGMDLSHGGHLTHG 131
Cdd:PRK13580 104 AKELFGAEHAYVQPHSGADANLVAFWAILahkvespaleklgaktvndlteedwealraELGNqRLLGMSLDSGGHLTHG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 132 SPVNVSGKWFEVCHYGVSQETEQLDYGQIRELALKERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVA 211
Cdd:PRK13580 184 FRPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 212 ----TGHHpNPLPHCHVVTTTTHKTLRGPRGGLILTnQSDLGKKFDKAVfPGTQGGPLEHVIAGKAVAFGEALTPAFKTY 287
Cdd:PRK13580 264 gkvfTGDE-DPVPHADIVTTTTHKTLRGPRGGLVLA-KKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKY 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 288 SAQVIENAKALATALQNRELKIVSGGTDNHVLLVDLRSIGMTGKRADQLVSGVKITANKNTVPFDPESPFVTSGLRLGSP 367
Cdd:PRK13580 341 AQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTP 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332350376 368 AMTTRGMGVAEFTEIGNIIADRLLNRE----------------DEQVATQCRQRVAQLCDRFPLYPHLTIP 422
Cdd:PRK13580 421 ALTTLGMGSDEMDEVAELIVKVLSNTTpgttaegapskakyelDEGVAQEVRARVAELLARFPLYPEIDLE 491
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
9-386 |
1.79e-163 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 468.31 E-value: 1.79e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 9 LAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKELFG 88
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 89 AAHA----NVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHG--------SPVNVsgkWFEVCHYGVSQETEQLD 156
Cdd:PLN03226 95 LDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgkkiSATSI---YFESMPYRLDESTGLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 157 YGQIRELALKERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGP 236
Cdd:PLN03226 172 YDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 237 RGGLIL-------------TNQSDLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALATALQ 303
Cdd:PLN03226 252 RGGMIFfrkgpkppkgqgeGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 304 NRELKIVSGGTDNHVLLVDLRSIGMTGKRADQLVSGVKITANKNTVPFDpESPFVTSGLRLGSPAMTTRGMGVAEFTEIG 383
Cdd:PLN03226 332 SKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDFEKVA 410
|
...
gi 332350376 384 NII 386
Cdd:PLN03226 411 EFL 413
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
9-391 |
7.87e-124 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 371.06 E-value: 7.87e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 9 LAETDPTIATYLGQELQRQREHLELIASENFTSPAVMAAQGSVLTNKYAEGLPGKRYYGGCEFIDKVEQVAIDRAKELFG 88
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 89 AAHA----NVQPHSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHG----SPVNVSGK--WFEVCHYGVSQETEQLDYG 158
Cdd:PLN02271 209 LDSEkwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyytpGGKKVSGAsiFFESLPYKVNPQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 159 QIRELALKERPKLIICGYSAYPRIIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTHKTLRGPRG 238
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 239 GLIL-------------------TNQSDLGKKFDKAVFPGTQGGPLEHVIAGKAVAFGEALTPAFKTYSAQVIENAKALA 299
Cdd:PLN02271 369 GIIFyrkgpklrkqgmllshgddNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 300 TALQNRELKIVSGGTDNHVLLVDLRSIGMTGKRADQLVSGVKITANKNTVpFDPESPFVTSGLRLGSPAMTTRGMGVAEF 379
Cdd:PLN02271 449 SALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSRGCLESDF 527
|
410
....*....|..
gi 332350376 380 teigNIIADRLL 391
Cdd:PLN02271 528 ----ETIADFLL 535
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
76-244 |
3.01e-15 |
|
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: 73.19 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 76 EQVAIDRAKELF--GAAHANVQPhSGAQANFAVFLALLKPGDKIMGMDLSHGGHLTHGspVNVSGkwFEVCHYGVSQETE 153
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVA--AELAG--AKPVPVPVDDAGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 154 QLDYGQI-RELALKERPKLIICGYSAYPR--IIDFEKFRAIADEVGAYLMADMAHIAGLVATGHHPNPLPHCHVVTTTTH 230
Cdd:cd01494 77 GGLDVAIlEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 332350376 231 KTLRGPRGGLILTN 244
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
92-208 |
1.21e-05 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 46.91 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 92 ANVQPHSGAQAN-FAVFLALLKPGDKIMGMDLSHGGHLTHgspVNVSG-KWFEVCHYgvSQETEQLDYGQIRElALKERP 169
Cdd:pfam00155 64 AAVVFGSGAGANiEALIFLLANPGDAILVPAPTYASYIRI---ARLAGgEVVRYPLY--DSNDFHLDFDALEA-ALKEKP 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 332350376 170 KLII-------CGySAYPRIiDFEKFRAIADEVGAYLMADMAHIAG 208
Cdd:pfam00155 138 KVVLhtsphnpTG-TVATLE-ELEKLLDLAKEHNILLLVDEAYAGF 181
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
85-202 |
1.64e-05 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 46.81 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 85 ELFGAAHANVQPhSGAQANFAVFLALLKPGDKI-MGMDLSHGGH--LTHGSPvnvsgkwfevcHYGVSQE-TEQLDYGQI 160
Cdd:cd00614 51 ALEGGEAALAFS-SGMAAISTVLLALLKAGDHVvASDDLYGGTYrlFERLLP-----------KLGIEVTfVDPDDPEAL 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 332350376 161 RElALKERPKLIicgYSAYP-----RIIDFEKFRAIADEVGAYLMAD 202
Cdd:cd00614 119 EA-AIKPETKLV---YVESPtnptlKVVDIEAIAELAHEHGALLVVD 161
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
98-220 |
1.22e-04 |
|
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: 43.87 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332350376 98 SGA-QANFAVFLALLKPGDKIMGMDLSHGGHLTHgspVNVSGkwFEVCHYGVSQETEQLDYGQIRELALKERPKLIICGY 176
Cdd:cd00609 66 NGAqEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAG--AEVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYLNN 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 332350376 177 SAYP--RIIDFEKFRAIAD---EVGAYLMADMAHiAGLVATGHHPNPLP 220
Cdd:cd00609 141 PNNPtgAVLSEEELEELAElakKHGILIISDEAY-AELVYDGEPPPALA 188
|
|
| |
