|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
13-430 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 733.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 13 MSAPLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAK 92
Cdd:PRK00011 2 FMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 93 ALFGAEFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNFSGKLYENGFYGVDPATHLIDMDAVRATA 172
Cdd:PRK00011 82 ELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 173 LEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVGK 252
Cdd:PRK00011 162 LEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 253 -QQYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLmapdvAKAGVSVVSGGTDVHLV 331
Cdd:PRK00011 242 dEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEAL-----AERGFRVVSGGTDNHLV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 332 LVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATAL-ATGSSVDV 410
Cdd:PRK00011 317 LVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLdNPDDEAVI 396
|
410 420
....*....|....*....|
gi 745755632 411 SALKDRATRLARAFPLYDGL 430
Cdd:PRK00011 397 EEVKEEVKELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
13-430 |
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: 729.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 13 MSAPLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAK 92
Cdd:COG0112 1 MLSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 93 ALFGAEFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNFSGKLYENGFYGVDPATHLIDMDAVRATA 172
Cdd:COG0112 81 ELFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 173 LEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVGK 252
Cdd:COG0112 161 LEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 253 QQYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLMApdvakAGVSVVSGGTDVHLVL 332
Cdd:COG0112 241 EELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAE-----RGFRVVSGGTDNHLVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 333 VDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATALATGSSVDV-S 411
Cdd:COG0112 316 VDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVlA 395
|
410
....*....|....*....
gi 745755632 412 ALKDRATRLARAFPLYDGL 430
Cdd:COG0112 396 EVREEVKELCKRFPLYPDL 414
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
18-420 |
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: 618.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 18 AEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAKALFGA 97
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 98 EFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMR--LNFSGKLYENGFYGVDPATHLIDMDAVRATALEF 175
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 176 RPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVG-KQQ 254
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 255 YAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLmapdvAKAGVSVVSGGTDVHLVLVD 334
Cdd:cd00378 241 LAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEAL-----KERGFKVVSGGTDNHLVLVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 335 LRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATAL-ATGSSVDVSAL 413
Cdd:cd00378 316 LRPKGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALkDAEDVAVAEEV 395
|
....*..
gi 745755632 414 KDRATRL 420
Cdd:cd00378 396 RKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
17-398 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 550.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 17 LAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAKALFG 96
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 97 AE----FANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNF-----SGKLYENGFYGVDPATHLIDMDA 167
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 168 VRATALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSG 247
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 248 LI--------VGKQ------QYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLMapd 313
Cdd:pfam00464 241 MIfyrkgvksVDKTgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALT--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 314 vaKAGVSVVSGGTDVHLVLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDpRPPMVTSGLRIGTPALATRGFGDTEFTE 393
Cdd:pfam00464 318 --ERGYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEK 394
|
....*
gi 745755632 394 VADII 398
Cdd:pfam00464 395 VAGFI 399
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
13-430 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 733.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 13 MSAPLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAK 92
Cdd:PRK00011 2 FMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 93 ALFGAEFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNFSGKLYENGFYGVDPATHLIDMDAVRATA 172
Cdd:PRK00011 82 ELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 173 LEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVGK 252
Cdd:PRK00011 162 LEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 253 -QQYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLmapdvAKAGVSVVSGGTDVHLV 331
Cdd:PRK00011 242 dEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEAL-----AERGFRVVSGGTDNHLV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 332 LVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATAL-ATGSSVDV 410
Cdd:PRK00011 317 LVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLdNPDDEAVI 396
|
410 420
....*....|....*....|
gi 745755632 411 SALKDRATRLARAFPLYDGL 430
Cdd:PRK00011 397 EEVKEEVKELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
13-430 |
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: 729.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 13 MSAPLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAK 92
Cdd:COG0112 1 MLSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 93 ALFGAEFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNFSGKLYENGFYGVDPATHLIDMDAVRATA 172
Cdd:COG0112 81 ELFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 173 LEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVGK 252
Cdd:COG0112 161 LEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 253 QQYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLMApdvakAGVSVVSGGTDVHLVL 332
Cdd:COG0112 241 EELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAE-----RGFRVVSGGTDNHLVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 333 VDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATALATGSSVDV-S 411
Cdd:COG0112 316 VDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVlA 395
|
410
....*....|....*....
gi 745755632 412 ALKDRATRLARAFPLYDGL 430
Cdd:COG0112 396 EVREEVKELCKRFPLYPDL 414
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
12-427 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 620.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 12 VMSAPLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRA 91
Cdd:PRK13034 4 FFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 92 KALFGAEFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNFSGKLYENGFYGVDPATHLIDMDAVRAT 171
Cdd:PRK13034 84 KQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 172 ALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVG 251
Cdd:PRK13034 164 AKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 252 K-QQYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLMapdvaKAGVSVVSGGTDVHL 330
Cdd:PRK13034 244 NdEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLK-----ERGYDLVSGGTDNHL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 331 VLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATAL-ATGSSVD 409
Cdd:PRK13034 319 LLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLdDLGNAAL 398
|
410
....*....|....*...
gi 745755632 410 VSALKDRATRLARAFPLY 427
Cdd:PRK13034 399 EQRVRKEVKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
18-420 |
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: 618.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 18 AEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAKALFGA 97
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 98 EFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMR--LNFSGKLYENGFYGVDPATHLIDMDAVRATALEF 175
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 176 RPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVG-KQQ 254
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 255 YAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLmapdvAKAGVSVVSGGTDVHLVLVD 334
Cdd:cd00378 241 LAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEAL-----KERGFKVVSGGTDNHLVLVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 335 LRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATAL-ATGSSVDVSAL 413
Cdd:cd00378 316 LRPKGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALkDAEDVAVAEEV 395
|
....*..
gi 745755632 414 KDRATRL 420
Cdd:cd00378 396 RKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
17-398 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 550.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 17 LAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAKALFG 96
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 97 AE----FANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNF-----SGKLYENGFYGVDPATHLIDMDA 167
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 168 VRATALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSG 247
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 248 LI--------VGKQ------QYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLMapd 313
Cdd:pfam00464 241 MIfyrkgvksVDKTgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALT--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 314 vaKAGVSVVSGGTDVHLVLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDpRPPMVTSGLRIGTPALATRGFGDTEFTE 393
Cdd:pfam00464 318 --ERGYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEK 394
|
....*
gi 745755632 394 VADII 398
Cdd:pfam00464 395 VAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
8-426 |
2.64e-172 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 490.26 E-value: 2.64e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 8 RTTAVMSAPLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLA 87
Cdd:PTZ00094 6 NLVLPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 88 RDRAKALFG---AEF-ANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGM-----RLNFSGKLYENGFYGVDP 158
Cdd:PTZ00094 86 QKRALEAFGldpEEWgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFytakkKVSATSIYFESLPYQVNE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 159 aTHLIDMDAVRATALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVH 238
Cdd:PTZ00094 166 -KGLIDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 239 KTLGGGRSGLIV----GKQQYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLMapdv 314
Cdd:PTZ00094 245 KSLRGPRSGLIFyrkkVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALE---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 315 aKAGVSVVSGGTDVHLVLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRpPMVTSGLRIGTPALATRGFGDTEFTEV 394
Cdd:PTZ00094 321 -KRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKS-ALNPSGVRLGTPALTTRGAKEKDFKFV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 745755632 395 ADIIATALATGSSV-------------------DVSALKDRATRLARAFPL 426
Cdd:PTZ00094 399 ADFLDRAVKLAQEIqkqvgkklvdfkkaleknpELQKLRQEVVEFASQFPF 449
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
6-431 |
7.24e-163 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 467.98 E-value: 7.24e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 6 DARTTAVMSA--PLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVV 83
Cdd:PRK13580 17 NLASTAYLAAldVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 84 ENLARDRAKALFGAEFANVQPHSGAQAN-----AAVLHALMSPG--------------------------ERLLGLDLAN 132
Cdd:PRK13580 97 EWEAAEHAKELFGAEHAYVQPHSGADANlvafwAILAHKVESPAleklgaktvndlteedwealraelgnQRLLGMSLDS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 133 GGHLTHGMRLNFSGKLYENGFYGVDPATHLIDMDAVRATALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMA 212
Cdd:PRK13580 177 GGHLTHGFRPNISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 213 HFAGLVAAGL---HPSPVPHADVVSTTVHKTLGGGRSGLIVGKQQYAKAINSAVfPGQQGGPLMHVIAGKAVALKIAATP 289
Cdd:PRK13580 257 HFAGLVAGKVftgDEDPVPHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 290 EFADRQRRTLSGARIIADRLMapdvaKAGVSVVSGGTDVHLVLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPM 369
Cdd:PRK13580 336 EFQKYAQQVVDNARALAEGFL-----KRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAW 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 745755632 370 VTSGLRIGTPALATRGFGDTEFTEVADIIATAL--------ATGSSVDVSA---------LKDRATRLARAFPLYDGLE 431
Cdd:PRK13580 411 YTSGIRLGTPALTTLGMGSDEMDEVAELIVKVLsnttpgttAEGAPSKAKYeldegvaqeVRARVAELLARFPLYPEID 489
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
15-425 |
1.13e-158 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 456.75 E-value: 1.13e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 15 APLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAKAL 94
Cdd:PLN03226 13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 95 FGAEFA----NVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRlNFSGKL------YENGFYGVDPATHLID 164
Cdd:PLN03226 93 FRLDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQ-TDGKKIsatsiyFESMPYRLDESTGLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 165 MDAVRATALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGG 244
Cdd:PLN03226 172 YDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 245 RSGLI--------VGKQQ------YAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLM 310
Cdd:PLN03226 252 RGGMIffrkgpkpPKGQGegavydYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 311 apdvaKAGVSVVSGGTDVHLVLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDpRPPMVTSGLRIGTPALATRGFGDTE 390
Cdd:PLN03226 332 -----SKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKD 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 745755632 391 FTEVADIIATAL--------ATGSSV--------------DVSALKDRATRLARAFP 425
Cdd:PLN03226 406 FEKVAEFLHRAVtialkiqkEHGKKLkdfkkglesndfskDIEALRAEVEEFATSFP 462
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
6-408 |
5.38e-110 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 336.01 E-value: 5.38e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 6 DARTTAVMS---APLAEVDPDIAELLAKELGRQRDTLEMIASENFAPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDV 82
Cdd:PLN02271 115 ESRRAAVRAwgnQPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 83 VENLARDRAKALFGAEFA----NVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNfSGK-------LYEN 151
Cdd:PLN02271 195 IERLCCERALAAFGLDSEkwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTP-GGKkvsgasiFFES 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 152 GFYGVDPATHLIDMDAVRATALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHAD 231
Cdd:PLN02271 274 LPYKVNPQTGYIDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 232 VVSTTVHKTLGGGRSGLIVGKQ--------------------QYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEF 291
Cdd:PLN02271 354 IVTSTTHKSLRGPRGGIIFYRKgpklrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEY 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 292 ADRQRRTLSGARIIADRLMapdvaKAGVSVVSGGTDVHLVLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDpRPPMVT 371
Cdd:PLN02271 434 KAYMQQVKKNAQALASALL-----RRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGD-NGTISP 507
|
410 420 430
....*....|....*....|....*....|....*..
gi 745755632 372 SGLRIGTPALATRGFGDTEFTEVADIIATALATGSSV 408
Cdd:PLN02271 508 GGVRIGTPAMTSRGCLESDFETIADFLLRAAQIASAV 544
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
84-252 |
3.49e-18 |
|
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: 81.66 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 84 ENLARDRAKALF--GAEFANVQPhSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNFsGKLYengFYGVDPATH 161
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAG-AKPV---PVPVDDAGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 162 -LIDMDAVRATALEFRPKVIIAGWSAYPR--VLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVH 238
Cdd:cd01494 77 gGLDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 745755632 239 KTLGGGRSGLIVGK 252
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| PRK07811 |
PRK07811 |
cystathionine gamma-synthase; Provisional |
35-243 |
3.62e-03 |
|
cystathionine gamma-synthase; Provisional
Pssm-ID: 236104 [Multi-domain] Cd Length: 388 Bit Score: 39.24 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 35 QRDTLEMIASENFAPRAVLQAQ------GSVLTNKYA------EGLPGRRyyGGCEHVDVV--------ENLArdrakAL 94
Cdd:PRK07811 1 SEDMSDHHANQGFATRAIHAGYepdpatGAVNPPIYAsstfaqDGVGGLR--GGYEYARTGnptrtaleEQLA-----AL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 95 FGAEFANVQPhSGAQANAAVLHALMSPGERLLGLDLANGGhlTHgmRLnFSgKLYENGFYGVDPAtHLIDMDAVRAtALE 174
Cdd:PRK07811 74 EGGAYGRAFS-SGMAATDCLLRAVLRPGDHIVIPNDAYGG--TF--RL-ID-KVFTRWGVEYTPV-DLSDLDAVRA-AIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 175 FRPKVIiagWSAYP-----RVLDFAAFRSIADEVGAKLLVDMAhFAglvaaglhpSPVPH------ADVV--STTvhKTL 241
Cdd:PRK07811 145 PRTKLI---WVETPtnpllSITDIAALAELAHDAGAKVVVDNT-FA---------SPYLQqplalgADVVvhSTT--KYI 209
|
..
gi 745755632 242 GG 243
Cdd:PRK07811 210 GG 211
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
156-213 |
4.09e-03 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 39.28 E-value: 4.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 745755632 156 VDPATHLIDMDAVRAtALEFRPKVII----AGWSAyprvlDFAAFRSIADEVGAKLLVDMAH 213
Cdd:COG0399 99 IDPDTYNIDPEALEA-AITPRTKAIIpvhlYGQPA-----DMDAIMAIAKKHGLKVIEDAAQ 154
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
80-252 |
5.53e-03 |
|
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: 38.72 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 80 VDVVEnlarDRAKALFGAEFANVQPhSGAQANAAVLHALMSPGERLLGLDLANGGhlTHGMRLNFSGKL-YENGFygVDP 158
Cdd:cd00614 42 VDALE----KKLAALEGGEAALAFS-SGMAAISTVLLALLKAGDHVVASDDLYGG--TYRLFERLLPKLgIEVTF--VDP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 745755632 159 AthliDMDAVRAtALEFRPKVIiagWSAYP-----RVLDFAAFRSIADEVGAKLLVDmahfaGLVAAGLHPSPVPH-ADV 232
Cdd:cd00614 113 D----DPEALEA-AIKPETKLV---YVESPtnptlKVVDIEAIAELAHEHGALLVVD-----NTFATPYLQRPLELgADI 179
|
170 180
....*....|....*....|....*
gi 745755632 233 V--STTvhKTLGGGR---SGLIVGK 252
Cdd:cd00614 180 VvhSAT--KYIGGHSdviAGVVVGS 202
|
|
| |
