|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-359 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 733.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 1 QGSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAANVQPNSGSQANQGVFFAMLKPGDTIMGMSLAHGGH 80
Cdd:PRK00011 45 QGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 81 LTHGSPVNMSGKWFNVVSYGLN-ENEDIDYDAAEKLAQEHKPKLIVAGASAFALKIDFARMAQIAKSVGAYLMVDMAHYA 159
Cdd:PRK00011 125 LTHGSPVNFSGKLYNVVSYGVDeETGLIDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 160 GLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILMK-AEYEKQINSAIFPGIQGGPLMHVIAAKAVAFKEALSPEFKAY 238
Cdd:PRK00011 205 GLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNdEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEY 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 239 QQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGAAHITVNKNAIPNDPEKPFVTSGVRLGSP 318
Cdd:PRK00011 285 AQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTP 364
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1359830406 319 AMTTRGFGPAEAEQVGNLIADVLENPEDAATLERVRAQVAE 359
Cdd:PRK00011 365 AITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEEVKE 405
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
1-359 |
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: 716.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 1 QGSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAANVQPNSGSQANQGVFFAMLKPGDTIMGMSLAHGGH 80
Cdd:COG0112 44 QGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 81 LTHGSPVNMSGKWFNVVSYGLN-ENEDIDYDAAEKLAQEHKPKLIVAGASAFALKIDFARMAQIAKSVGAYLMVDMAHYA 159
Cdd:COG0112 124 LTHGSPVNFSGKGYNVVSYGVDpETGLIDYDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 160 GLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILMKAEYEKQINSAIFPGIQGGPLMHVIAAKAVAFKEALSPEFKAYQ 239
Cdd:COG0112 204 GLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNEELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 240 QKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGAAHITVNKNAIPNDPEKPFVTSGVRLGSPA 319
Cdd:COG0112 284 KQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPA 363
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1359830406 320 MTTRGFGPAEAEQVGNLIADVLENPEDAATLERVRAQVAE 359
Cdd:COG0112 364 VTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEVKE 403
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
1-359 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 633.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 1 QGSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAANVQPNSGSQANQGVFFAMLKPGDTIMGMSLAHGGH 80
Cdd:PRK13034 48 QGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 81 LTHGSPVNMSGKWFNVVSYGLNE-NEDIDYDAAEKLAQEHKPKLIVAGASAFALKIDFARMAQIAKSVGAYLMVDMAHYA 159
Cdd:PRK13034 128 LTHGAKVSLSGKWYNAVQYGVDRlTGLIDYDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 160 GLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILMK-AEYEKQINSAIFPGIQGGPLMHVIAAKAVAFKEALSPEFKAY 238
Cdd:PRK13034 208 GLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNdEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTY 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 239 QQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGAAHITVNKNAIPNDPEKPFVTSGVRLGSP 318
Cdd:PRK13034 288 AKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTP 367
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1359830406 319 AMTTRGFGPAEAEQVGNLIADVLENPEDAATLERVRAQVAE 359
Cdd:PRK13034 368 AGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKEVKA 408
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
1-359 |
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: 594.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 1 QGSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAANVQPNSGSQANQGVFFAMLKPGDTIMGMSLAHGGH 80
Cdd:cd00378 39 MGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 81 LTHGSP--VNMSGKWFNVVSYGLN-ENEDIDYDAAEKLAQEHKPKLIVAGASAFALKIDFARMAQIAKSVGAYLMVDMAH 157
Cdd:cd00378 119 LTHGSFtkVSASGKLFESVPYGVDpETGLIDYDALEKMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 158 YAGLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILM-KAEYEKQINSAIFPGIQGGPLMHVIAAKAVAFKEALSPEFK 236
Cdd:cd00378 199 VAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 237 AYQQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGAAHITVNKNAIPNDPEKPFVTSGVRLG 316
Cdd:cd00378 279 AYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIG 358
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1359830406 317 SPAMTTRGFGPAEAEQVGNLIADVLENPEDAATLERVRAQVAE 359
Cdd:cd00378 359 TPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAE 401
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
1-337 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 542.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 1 QGSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEA----ANVQPNSGSQANQGVFFAMLKPGDTIMGMSLA 76
Cdd:pfam00464 40 LGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDPakwgVNVQPLSGSPANLAVYTALLEPGDRIMGLDLP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 77 HGGHLTHGSPVNM-----SGKWFNVVSYGLN-ENEDIDYDAAEKLAQEHKPKLIVAGASAFALKIDFARMAQIAKSVGAY 150
Cdd:pfam00464 120 HGGHLTHGYPVNSkkisaSSKFFESMPYGVDpETGYIDYDQLEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 151 LMVDMAHYAGLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILMKA--------------EYEKQINSAIFPGIQGGPL 216
Cdd:pfam00464 200 LMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIFYRKgvksvdktgkeilyELEKKINSAVFPGLQGGPH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 217 MHVIAAKAVAFKEALSPEFKAYQQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGAAHITVN 296
Cdd:pfam00464 280 NHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITAN 359
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1359830406 297 KNAIPNDpEKPFVTSGVRLGSPAMTTRGFGPAEAEQVGNLI 337
Cdd:pfam00464 360 KNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
2-342 |
2.16e-162 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 462.14 E-value: 2.16e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 2 GSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEA----ANVQPNSGSQANQGVFFAMLKPGDTIMGMSLAH 77
Cdd:PTZ00094 55 GSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFGLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 78 GGHLTHG-----SPVNMSGKWFNVVSYGLNENEDIDYDAAEKLAQEHKPKLIVAGASAFALKIDFARMAQIAKSVGAYLM 152
Cdd:PTZ00094 135 GGHLTHGfytakKKVSATSIYFESLPYQVNEKGLIDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLM 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 153 VDMAHYAGLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVIL----MKAEYEKQINSAIFPGIQGGPLMHVIAAKAVAFK 228
Cdd:PTZ00094 215 ADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSGLIFyrkkVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 229 EALSPEFKAYQQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGAAHITVNKNAIPNDPEKpF 308
Cdd:PTZ00094 295 EVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSA-L 373
|
330 340 350
....*....|....*....|....*....|....
gi 1359830406 309 VTSGVRLGSPAMTTRGFGPAEAEQVGNLIADVLE 342
Cdd:PTZ00094 374 NPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVK 407
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
2-359 |
1.29e-158 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 453.73 E-value: 1.29e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 2 GSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAANVQPNSGSQANQGVFFAML----------KPGDT-- 69
Cdd:PRK13580 70 GNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQPHSGADANLVAFWAILahkvespaleKLGAKtv 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 70 -------------------IMGMSLAHGGHLTHGSPVNMSGKWFNVVSYGLN-ENEDIDYDAAEKLAQEHKPKLIVAGAS 129
Cdd:PRK13580 150 ndlteedwealraelgnqrLLGMSLDSGGHLTHGFRPNISGKMFHQRSYGVDpDTGLLDYDEIAALAREFKPLILVAGYS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 130 AFALKIDFARMAQIAKSVGAYLMVDMAHYAGLIAAGVYP---NPVPHADFVTTTTHKSLRGPRGGVILMKAEYEKQINSA 206
Cdd:PRK13580 230 AYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 207 IfPGIQGGPLMHVIAAKAVAFKEALSPEFKAYQQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEA 286
Cdd:PRK13580 310 C-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAES 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 287 ALGAAHITVNKNAIPNDPEKPFVTSGVRLGSPAMTTRGFGPAEAEQVGNLIADVLENPE----------------DAATL 350
Cdd:PRK13580 389 ALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVKVLSNTTpgttaegapskakyelDEGVA 468
|
....*....
gi 1359830406 351 ERVRAQVAE 359
Cdd:PRK13580 469 QEVRARVAE 477
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
2-337 |
4.44e-144 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 416.30 E-value: 4.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 2 GSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAA----NVQPNSGSQANQGVFFAMLKPGDTIMGMSLAH 77
Cdd:PLN03226 55 GSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFRLDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 78 GGHLTHG-----SPVNMSGKWFNVVSYGLNENED-IDYDAAEKLAQEHKPKLIVAGASAFALKIDFARMAQIAKSVGAYL 151
Cdd:PLN03226 135 GGHLSHGyqtdgKKISATSIYFESMPYRLDESTGlIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 152 MVDMAHYAGLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILMK--------------AEYEKQINSAIFPGIQGGPLM 217
Cdd:PLN03226 215 MCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMIFFRkgpkppkgqgegavYDYEDKINFAVFPGLQGGPHN 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 218 HVIAAKAVAFKEALSPEFKAYQQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGAAHITVNK 297
Cdd:PLN03226 295 HTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNK 374
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1359830406 298 NAIPNDpEKPFVTSGVRLGSPAMTTRGFGPAEAEQVGNLI 337
Cdd:PLN03226 375 NAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDFEKVAEFL 413
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
2-341 |
5.62e-104 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 317.52 E-value: 5.62e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 2 GSQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAA----NVQPNSGSQANQGVFFAMLKPGDTIMGMSLAH 77
Cdd:PLN02271 169 GSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSEkwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 78 GGHLTHG--SP----VNMSGKWFNVVSYGLNENED-IDYDAAEKLAQEHKPKLIVAGASAFALKIDFARMAQIAKSVGAY 150
Cdd:PLN02271 249 GGHMSHGyyTPggkkVSGASIFFESLPYKVNPQTGyIDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 151 LMVDMAHYAGLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILMKA--------------------EYEKQINSAIFPG 210
Cdd:PLN02271 329 LMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIFYRKgpklrkqgmllshgddnshyDFEEKINFAVFPS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 211 IQGGPLMHVIAAKAVAFKEALSPEFKAYQQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGA 290
Cdd:PLN02271 409 LQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEM 488
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1359830406 291 AHITVNKNAIPNDpEKPFVTSGVRLGSPAMTTRGFGPAEAEqvgnLIADVL 341
Cdd:PLN02271 489 CHITLNKTAIFGD-NGTISPGGVRIGTPAMTSRGCLESDFE----TIADFL 534
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
29-196 |
1.34e-22 |
|
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: 92.83 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 29 EQLAIDRVKQLF--GAEAANVQPnSGSQANQGVFFAMLKPGDTIMGMSLAHGGHLTHGspVNMSGKWFNVVSYGLNENED 106
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVA--AELAGAKPVPVPVDDAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 107 IDYDAAEKLAQEHKPKLIVA--GASAFALKIDFARMAQIAKSVGAYLMVDMAHYAGLIAAGVYPNPVPHADFVTTTTHKS 184
Cdd:cd01494 79 LDVAILEELKAKPNVALIVItpNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKN 158
|
170
....*....|..
gi 1359830406 185 LRGPRGGVILMK 196
Cdd:cd01494 159 LGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
45-277 |
1.07e-11 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 65.40 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 45 ANVQPNSGSQAN-QGVFFAMLKPGDTIMGMSLAHGGHLTHgspVNMSGkwFNVVSYGLNENED--IDYDAAEKLAQEhKP 121
Cdd:pfam00155 64 AAVVFGSGAGANiEALIFLLANPGDAILVPAPTYASYIRI---ARLAG--GEVVRYPLYDSNDfhLDFDALEAALKE-KP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 122 KLIVAG------ASAFALKiDFARMAQIAKSVGAYLMVDMAH----YAGLIAAGVYPNPVPHAD-FVTTTTHKS--LRGP 188
Cdd:pfam00155 138 KVVLHTsphnptGTVATLE-ELEKLLDLAKEHNILLLVDEAYagfvFGSPDAVATRALLAEGPNlLVVGSFSKAfgLAGW 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 189 RGGVILMKAEYEKQINSAIFPGIQGGPLMHvIAAKAVAFKEALSPEFKAYQQKVVENARVLAETLVKRGLRIVSGrtESH 268
Cdd:pfam00155 217 RVGYILGNAAVISQLRKLARPFYSSTHLQA-AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPS--QAG 293
|
250
....*....|
gi 1359830406 269 -VMLVDLRAK 277
Cdd:pfam00155 294 fFLLTGLDPE 303
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
29-269 |
1.74e-10 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 61.61 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 29 EQLAidrvkQLFGAEAANVQpNSGSQANQGVFFAMLKPGDTIMGMSLAH-----GGHLTHGspvnmsgkwfNVVSYGLNe 103
Cdd:COG0156 89 EELA-----EFLGKEAALLF-SSGYAANLGVISALAGRGDLIFSDELNHasiidGARLSGA----------KVVRFRHN- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 104 nediDYDAAEKL---AQEHKPKLIVA-------GASAfalkiDFARMAQIAKSVGAYLMVDMAHyagliAAGVY-PN--P 170
Cdd:COG0156 152 ----DMDDLERLlkkARAARRKLIVTdgvfsmdGDIA-----PLPEIVELAEKYGALLYVDDAH-----GTGVLgETgrG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 171 VPHA-------DFVTTTTHKSLrGPRGGVILMKAEY-EKQINSA---IFpgiQGGPLMHVIAAKAVAFKeaLSPEFKAYQ 239
Cdd:COG0156 218 LVEHfgledrvDIIMGTLSKAL-GSSGGFVAGSKELiDYLRNRArpfIF---STALPPAVAAAALAALE--ILREEPELR 291
|
250 260 270
....*....|....*....|....*....|
gi 1359830406 240 QKVVENARVLAETLVKRGLRIvsGRTESHV 269
Cdd:COG0156 292 ERLWENIAYFREGLKELGFDL--GPSESPI 319
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
29-268 |
2.53e-10 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 61.04 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 29 EQLAidrvkQLFGAEAANVQpNSGSQANQGVFFAMLKPGDTIMGMSLAHG----GHLTHGSPVnmsgkwfnvVSYGLNen 104
Cdd:cd06454 53 EELA-----EFHGKEAALVF-SSGYAANDGVLSTLAGKGDLIISDSLNHAsiidGIRLSGAKK---------RIFKHN-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 105 ediDYDAAEKLAQE----HKPKLIVAgASAFALKIDFA---RMAQIAKSVGAYLMVDMAHYAGLI---AAGV-YPNPVPH 173
Cdd:cd06454 116 ---DMEDLEKLLREarrpYGKKLIVT-EGVYSMDGDIAplpELVDLAKKYGAILFVDEAHSVGVYgphGRGVeEFGGLTD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 174 A-DFVTTTTHKSLrGPRGGVILMKAEY-EKQINSA---IFpgiQGGPLMHVIAAKAVAFKEALSpeFKAYQQKVVENARV 248
Cdd:cd06454 192 DvDIIMGTLGKAF-GAVGGYIAGSKELiDYLRSYArgfIF---STSLPPAVAAAALAALEVLQG--GPERRERLQENVRY 265
|
250 260
....*....|....*....|
gi 1359830406 249 LAETLVKRGLRIVSgrTESH 268
Cdd:cd06454 266 LRRGLKELGFPVGG--SPSH 283
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
38-208 |
2.98e-09 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 57.26 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 38 QLFGAEAANVQPNSGSQANQGVFFAMLKPGDTIMGM-----SLAHGGHLTHGSPVNMSGKWfnvvSYGLNENEDID-YDA 111
Cdd:cd00615 70 RAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDrnchkSVINGLVLSGAVPVYLKPER----NPYYGIAGGIPpETF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 112 AEKLAQEHKPKLIVA------GASAfalkiDFARMAQIAKSVGAYLMVDMAHYAGLIAAGVYPNPVPH--ADFVTTTTHK 183
Cdd:cd00615 146 KKALIEHPDAKAAVItnptyyGICY-----NLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSSAAMagADIVVQSTHK 220
|
170 180
....*....|....*....|....*...
gi 1359830406 184 SLRGPR-GGVILMKAEY--EKQINSAIF 208
Cdd:cd00615 221 TLPALTqGSMIHVKGDLvnPDRVNEALN 248
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
17-276 |
3.91e-09 |
|
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: 57.35 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 17 RYYGGCEYVDVVEQLAiDRVKQLFG--AEAANVQPNSGS-QANQGVFFAMLKPGDTIMGMSLAHGGHLTHgspVNMSGkw 93
Cdd:cd00609 31 GYYPDPGLPELREAIA-EWLGRRGGvdVPPEEIVVTNGAqEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAG-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 94 FNVVSYGLNENEDIDYD-AAEKLAQEHKPKLIV-------AGAsAFALKiDFARMAQIAKSVGAYLMVDMAhYAGLIAAG 165
Cdd:cd00609 105 AEVVPVPLDEEGGFLLDlELLEAAKTPKTKLLYlnnpnnpTGA-VLSEE-ELEELAELAKKHGILIISDEA-YAELVYDG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 166 VYPNPVPHAD-----FVTTTTHKSLRGP--RGG-VILMKAEYEKQINSAIfPGIQGGPLMHVIAAKAVAFKEALSpEFKA 237
Cdd:cd00609 182 EPPPALALLDayervIVLRSFSKTFGLPglRIGyLIAPPEELLERLKKLL-PYTTSGPSTLSQAAAAAALDDGEE-HLEE 259
|
250 260 270
....*....|....*....|....*....|....*....
gi 1359830406 238 YQQKVVENARVLAETLVKRGLRIVSGRTESHVMLVDLRA 276
Cdd:cd00609 260 LRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDLPE 298
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
61-198 |
2.24e-08 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 55.15 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 61 FAMLKPGDTIMgMSlahggHLTHGS---PVNMSGKWFNV-VSY-GLNENEDIDYDAAEKLAQEhKPKLI-VAGAS-AFAL 133
Cdd:COG0520 97 LGRLKPGDEIL-IT-----EMEHHSnivPWQELAERTGAeVRViPLDEDGELDLEALEALLTP-RTKLVaVTHVSnVTGT 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1359830406 134 KIDFARMAQIAKSVGAYLMVDMAHYAGLIAAGVYPNpvpHADFVTTTTHKsLRGPRG-GVILMKAE 198
Cdd:COG0520 170 VNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQAL---GCDFYAFSGHK-LYGPTGiGVLYGKRE 231
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
23-269 |
3.16e-08 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 54.78 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 23 EYVDVVEQLAidrvkQLFGAEAANVQpNSGSQANQGVFFAMLKPGDTIMGMSLAH-----GGHLthgSPVnmsgkwfNVV 97
Cdd:PRK05958 85 AHEALEEELA-----EWFGAERALLF-SSGYAANLAVLTALAGKGDLIVSDKLNHaslidGARL---SRA-------RVR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 98 SYGLNenediDYDAAEKLAQE--HKPKLIVA-------GASAfalkiDFARMAQIAKSVGAYLMVDMAHyagliAAGVY- 167
Cdd:PRK05958 149 RYPHN-----DVDALEALLAKwrAGRALIVTesvfsmdGDLA-----PLAELVALARRHGAWLLVDEAH-----GTGVLg 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 168 ---------------PNPVphadfVTTTTHKSLrGPRGGVILMKAEY-EKQINSA---IF----PgiqggPLMHVIAAKA 224
Cdd:PRK05958 214 pqgrglaaeaglagePDVI-----LVGTLGKAL-GSSGAAVLGSETLiDYLINRArpfIFttalP-----PAQAAAARAA 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1359830406 225 VafkeALSPEFKAYQQKVVENARVLAETLVKRGLRIVsgRTESHV 269
Cdd:PRK05958 283 L----RILRREPERRERLAALIARLRAGLRALGFQLM--DSQSAI 321
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
29-185 |
8.83e-06 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 47.41 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 29 EQLAidrvKQLFGAEAANVQPNSGSQANQGVFFAMLKPGDTI-----MGMSLAHGGHLTHGSPVNMSGKWFNVvsYGLNE 103
Cdd:COG1982 72 QELA----AEAFGADRTFFLVNGTSSGNKAMILAVCGPGDKVlvprnCHKSVIHGLILSGAIPVYLNPEIDNE--LGIIG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 104 NedIDYDAAEKLAQEH-KPKLIVA------GASAfalkiDFARMAQIAKSVGAYLMVDMAHYAGL----------IAAGv 166
Cdd:COG1982 146 G--ITPEAVEEALIEHpDAKAVLItnptyyGVCY-----DLKAIAELAHEHGIPVLVDEAHGAHFgfhpdlprsaMEAG- 217
|
170
....*....|....*....
gi 1359830406 167 ypnpvphADFVTTTTHKSL 185
Cdd:COG1982 218 -------ADLVVQSTHKTL 229
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
100-214 |
5.05e-05 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 44.76 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 100 GLNENEDIDYDAAEKLAQEhKPKLI-VAGAS-AFALKIDFARMAQIAKSVGAYLMVDMAHyagliAAGVYPNPVPH--AD 175
Cdd:cd06453 120 PVDDDGQLDLEALEKLLTE-RTKLVaVTHVSnVLGTINPVKEIGEIAHEAGVPVLVDGAQ-----SAGHMPVDVQDlgCD 193
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1359830406 176 FVTTTTHKSLrGPRG-GVILMKAEYEKqinsAIFPGIQGG 214
Cdd:cd06453 194 FLAFSGHKML-GPTGiGVLYGKEELLE----EMPPYGGGG 228
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
34-202 |
1.33e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 39.89 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 34 DRVKQLFGAEAANVQPnSGSQANQGVFFAMLKPGDTIMGMSLAH------GGHLTHGS--PVNMSGKwfnvvsyglnENE 105
Cdd:pfam01212 39 DRVAELFGKEAALFVP-SGTAANQLALMAHCQRGDEVICGEPAHihfdetGGHAELGGvqPRPLDGD----------EAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359830406 106 DIDYDAAEKLAQEH------KPKLIV-------AGASAFALKiDFARMAQIAKSVGAYLMVDMAHYA------GLIAAGV 166
Cdd:pfam01212 108 NMDLEDLEAAIREVgadifpPTGLISlenthnsAGGQVVSLE-NLREIAALAREHGIPVHLDGARFAnaavalGVIVKEI 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 1359830406 167 YpnpvPHADFVTTTTHKSLRGPRGGVILMKAEYEKQ 202
Cdd:pfam01212 187 T----SYADSVTMCLSKGLGAPVGSVLAGSDDFIAK 218
|
|
| |
