|
Name |
Accession |
Description |
Interval |
E-value |
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
1-294 |
1.57e-177 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 491.07 E-value: 1.57e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:COG0190 1 MMAQILDGKAVAAEIREELKERVAALKAK-GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:COG0190 80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTcig 240
Cdd:COG0190 160 HAVVVGRSNIVGKPLALLLLRR----NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGIN--- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:COG0190 233 RVEDGK--LVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGL 284
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-294 |
3.22e-167 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 464.87 E-value: 3.22e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKaKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14190 1 MMAVIIDGKEVAKEKREQLKEEVVKLK-EQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14190 80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNE----NATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPegkriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14190 236 NGK-----LCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-293 |
1.83e-131 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 374.41 E-value: 1.83e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14189 1 MTAQLIDGNALSKQLRAEAAQRAAALTAR-GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14189 80 ARIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIG 240
Cdd:PRK14189 160 HAVVIGRSNIVGKPMAMLLLQ----AGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVG---MN 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 YTPEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAG 293
Cdd:PRK14189 233 RDDAGK--LCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAA 283
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-294 |
9.44e-129 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 368.13 E-value: 9.44e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14188 2 ATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14188 82 IARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLqkapGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGY- 241
Cdd:PRK14188 162 VVIGRSNLVGKPMAQLLL----AANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAp 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499238903 242 -TPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14188 238 eKGEGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRAAGL 291
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-294 |
9.89e-122 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 349.84 E-value: 9.89e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 4 HIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLI 83
Cdd:PRK14184 2 LLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 84 ARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVV 163
Cdd:PRK14184 82 AELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 164 IVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYTP 243
Cdd:PRK14184 162 VVGRSNIVGKPLALMLGAPGKFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVG---INRTD 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499238903 244 EGkriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14184 239 DG---LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKERVGL 286
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-288 |
8.19e-121 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 347.67 E-value: 8.19e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK10792 1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK10792 81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIG 240
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLL----AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVG---IN 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499238903 241 YTPEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAA 288
Cdd:PRK10792 234 RLEDGK--LVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQAC 279
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-294 |
2.14e-117 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 339.54 E-value: 2.14e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14168 1 MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG--EPCFLPCTPHGVQELLIRSGIKIE 158
Cdd:PRK14168 81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGgdEVKFLPCTPAGIQEMLVRSGVETS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 159 GTHVVIVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTC 238
Cdd:PRK14168 161 GAEVVVVGRSNIVGKPIANMMTQKGPGANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499238903 239 IGYTPE-GKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14168 241 VGTNEStGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAKFHLSL 297
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-289 |
2.10e-116 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 336.35 E-value: 2.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14191 3 LLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14191 83 DLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYTPE 244
Cdd:PRK14191 163 IGASNIVGKPLAMLMLN----AGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIG---INRLND 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14191 236 GR--LVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-294 |
4.43e-115 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 333.32 E-value: 4.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG--EPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14174 83 DLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGhlDKCFVSCTPYGILELLGRYNIETKGKHC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCI--G 240
Cdd:PRK14174 163 VVVGRSNIVGKPMANLMLQKLKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIedP 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 YTPEGKRiLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14174 243 STKSGYR-LVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERVNNL 295
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-293 |
1.64e-114 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 331.59 E-value: 1.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14193 1 MTAIILDGKATADEIKADLAERVAALKEK-GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14193 80 AVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKAPgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PRK14193 160 HVVVIGRGVTVGRPIGLLLTRRSE--NATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 ytpEGKriLSGDVDfEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAG 293
Cdd:PRK14193 238 ---DGK--LVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-294 |
4.49e-114 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 330.97 E-value: 4.49e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 3 AHIINGTEIAAAIREEIRSEVTALkAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETL-EDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14167 81 IDELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGYT 242
Cdd:PRK14167 161 VVVGRSDIVGKPMANLLIQKADGGNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDAD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499238903 243 PEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14167 241 TEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASLQEGV 292
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-294 |
3.44e-110 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 320.86 E-value: 3.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14186 82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGyT 242
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLA----ANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLP-S 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499238903 243 PEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14186 237 SDGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRHGL 288
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-290 |
3.19e-109 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 318.23 E-value: 3.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYT 242
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK----NATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVG---MNRD 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499238903 243 PEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKR 290
Cdd:PRK14179 235 ENGK--LIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-293 |
1.29e-106 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 311.76 E-value: 1.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAkhgiVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14173 1 MAARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14173 77 ELIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLqkapGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PRK14173 157 EVVVVGRSNIVGKPLAALLL----REDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 yTPEGKRILSGDVDFEaVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAG 293
Cdd:PRK14173 233 -GNGGRDILTGDVHPE-VAEVAGALTPVPGGVGPMTVAMLMANTVIAALRRRG 283
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-292 |
3.73e-106 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 310.58 E-value: 3.73e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14176 90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTcigyTPE 244
Cdd:PRK14176 170 VGHSNVVGKPMAAMLLNR----NATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGIT----KEE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14176 242 DK--VYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-296 |
4.95e-104 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 304.92 E-value: 4.95e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14175 1 MVAKILDGKQIAKDYRQGLQDQVEALKEK-GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14175 80 NELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTtcig 240
Cdd:PRK14175 160 NAVVIGRSHIVGQPVSKLLLQ----KNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGN---- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499238903 241 yTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGLVK 296
Cdd:PRK14175 232 -TPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMRRGIDS 286
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-292 |
5.11e-100 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 294.81 E-value: 5.11e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14183 3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14183 83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYTPE 244
Cdd:PRK14183 163 VGASNIVGKPMAALLLN----ANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIG---INRTED 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14183 236 GR--LVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-291 |
6.98e-100 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 294.81 E-value: 6.98e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14185 3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14185 83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCI--GYT 242
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAYPGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVpdATR 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499238903 243 PEGKRiLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRA 291
Cdd:PRK14185 243 KSGFK-LTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKA 290
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-289 |
1.62e-98 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 290.53 E-value: 1.62e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14172 4 IINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14172 84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIgytpE 244
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNE----NATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV----N 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14172 236 GK--ITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK 278
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-292 |
1.78e-97 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 289.05 E-value: 1.78e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14194 2 MSAKLIDGKAAAARVLAQVREDVRTLKAA-GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14194 81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIg 240
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQ----AHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRI- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499238903 241 yTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14194 236 -DDDGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQA 286
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
3-291 |
7.91e-97 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 287.17 E-value: 7.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG--EPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PLN02516 89 VHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIG 240
Cdd:PLN02516 169 KAVVVGRSNIVGLPVSLLLLK----ADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVS 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 --YTPEGKRILsGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRA 291
Cdd:PLN02516 245 dpSKKSGYRLV-GDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRV 296
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-290 |
2.72e-96 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 288.06 E-value: 2.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 2 SAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLT 81
Cdd:PLN02616 72 GAKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 82 LIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCL--GEPCFLPCTPHGVQELLIRSGIKIEG 159
Cdd:PLN02616 152 FISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrgREPLFVPCTPKGCIELLHRYNVEIKG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 160 THVVIVGRSNLVGKPLAnILLQKapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCI 239
Cdd:PLN02616 232 KRAVVIGRSNIVGMPAA-LLLQR---EDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPV 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 240 --GYTPEGKRiLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKR 290
Cdd:PLN02616 308 edASSPRGYR-LVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-289 |
8.91e-96 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 283.84 E-value: 8.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSK-GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG-EPCFLPCTPHGVQELLIRSGIKIEGTHVV 163
Cdd:PRK14166 82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 164 IVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYTP 243
Cdd:PRK14166 162 IIGASNIVGRPMATMLLN----AGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVG---INRLE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499238903 244 EGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14166 235 SGK--IVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
11-290 |
2.39e-95 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 282.91 E-value: 2.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 11 IAAAIREEIRSEVTAlkakhgivPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIARLNADP 90
Cdd:PRK14181 12 ILATIKENISASSTA--------PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 91 KISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGE-PCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSN 169
Cdd:PRK14181 84 NIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 170 LVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGYTPEGKRIL 249
Cdd:PRK14181 164 IVGKPLAALLMQKHPDTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAANPKGYIL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499238903 250 SGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKR 290
Cdd:PRK14181 244 VGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLR 284
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-292 |
3.48e-95 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 282.60 E-value: 3.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 3 AHIINGTEIAAAIREEIRSEVTALkAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKL-AQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14169 80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGttcIGYT 242
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLMVN----HDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVG---ISRG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499238903 243 PEGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14169 233 ADGK--LLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRA 280
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-289 |
2.81e-94 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 279.81 E-value: 2.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTalkaKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEII----ESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVI 164
Cdd:PRK14178 78 RLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 165 VGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIgytpE 244
Cdd:PRK14178 158 VGRSIDVGRPMAALLLN----ADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV----N 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499238903 245 GKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14178 230 GK--LCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-293 |
9.09e-94 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 278.65 E-value: 9.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14192 1 MMALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14192 81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVgttciG 240
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLLN----ANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDA-----G 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 241 YTPEGKRILsGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAG 293
Cdd:PRK14192 232 FHPRDGGGV-GDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-294 |
5.85e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 269.39 E-value: 5.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 3 AHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14187 2 TNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEP--CFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14187 82 INELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKknCLIPCTPKGCLYLIKTITRNLSGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIg 240
Cdd:PRK14187 162 DAVVIGRSNIVGKPMACLLLGE----NCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSI- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499238903 241 yTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGL 294
Cdd:PRK14187 237 -EEGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAACNQKGI 289
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-289 |
1.85e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 268.00 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 1 MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLL 80
Cdd:PRK14177 1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 81 TLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGT 160
Cdd:PRK14177 81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 161 HVVIVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVgttciG 240
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTE----MNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDA-----G 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499238903 241 YTPEGkrilSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14177 232 YNPGN----VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-291 |
3.28e-89 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 269.52 E-value: 3.28e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 2 SAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLT 81
Cdd:PLN02897 55 KTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 82 LIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCL--GEPCFLPCTPHGVQELLIRSGIKIEG 159
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrgREPLFVSCTPKGCVELLIRSGVEIAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 160 THVVIVGRSNLVGKPLAnILLQKapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCI 239
Cdd:PLN02897 215 KNAVVIGRSNIVGLPMS-LLLQR---HDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPV 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 240 -GYTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRA 291
Cdd:PLN02897 291 eDSSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
116-289 |
5.51e-89 |
|
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.
Pssm-ID: 133448 Cd Length: 168 Bit Score: 262.49 E-value: 5.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 116 PDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQkapgANATVTICHS 195
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLN----RNATVTVCHS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 196 GTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGytPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPM 275
Cdd:cd01080 77 KTKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVP--DKSGGKLVGDVDFESAKEKASAITPVPGGVGPM 154
|
170
....*....|....
gi 499238903 276 TIIMLMLNTLTAAK 289
Cdd:cd01080 155 TVAMLMKNTVEAAK 168
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-289 |
7.34e-89 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 266.51 E-value: 7.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCL-GEPCFLPCTPHGVQELLIRSGIKIEGTHVV 163
Cdd:PRK14180 83 QLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 164 IVGRSNLVGKPLANILLQkapgANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIgytp 243
Cdd:PRK14180 163 VVGASNVVGKPVSQLLLN----AKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHV---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499238903 244 EGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:PRK14180 235 DGK--IVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQ 278
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-292 |
7.55e-89 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 266.50 E-value: 7.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 5 IINGTEIAAAIREEIRSEVTALKAKhGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIA 84
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR-GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 85 RLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCF-LPCTPHGVQELLIRSGIKIEGTHVV 163
Cdd:PRK14182 82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 164 IVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGytp 243
Cdd:PRK14182 162 VVGRSNIVGKPMAMMLLER----HATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLA--- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499238903 244 EGKriLSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAA 292
Cdd:PRK14182 235 DGK--LVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTA 281
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-290 |
1.59e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 265.40 E-value: 1.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 3 AHIINGTEIAAAIREEIRSEVTALkAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTL 82
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAEL-VKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 83 IARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14170 81 VEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTtcigyT 242
Cdd:PRK14170 161 VVIGRSNIVGKPVAQLLLNE----NATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGM-----D 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499238903 243 PEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKR 290
Cdd:PRK14170 232 RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
124-292 |
3.93e-88 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 259.71 E-value: 3.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 124 HPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLI 203
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA----NATVTVCHSKTKDLAEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 204 TSQADILVSAMGKPKFITADMVRQGAVVIDVGTtcigyTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLN 283
Cdd:pfam02882 77 TREADIVVVAVGKPELIKADWIKPGAVVIDVGI-----NRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQN 151
|
....*....
gi 499238903 284 TLTAAKRAA 292
Cdd:pfam02882 152 TVEAAKRQL 160
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-295 |
9.62e-86 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 258.73 E-value: 9.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 4 HIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLI 83
Cdd:PRK14171 3 NIIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 84 ARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLG-EPCFLPCTPHGVQELLIRSGIKIEGTHV 162
Cdd:PRK14171 83 NELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGiSQGFIPCTALGCLAVIKKYEPNLTGKNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 163 VIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGyt 242
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE----NCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRIS-- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 243 peGKRILsGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGLV 295
Cdd:PRK14171 237 --GNKII-GDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLYTL 286
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
6-121 |
3.83e-58 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 181.83 E-value: 3.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 6 INGTEIAAAIREEIRSEVTALKAkHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIAR 85
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKA-GGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 499238903 86 LNADPKISGILVQVPLPVQISENLVLNAINPDKDVD 121
Cdd:pfam00763 80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
136-289 |
6.97e-24 |
|
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133451 Cd Length: 140 Bit Score: 94.50 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 136 PCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQKapgaNATVTICHSGTKNLPLITSQADILVSAMG 215
Cdd:cd05212 5 PLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRD----GATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499238903 216 KPKFITADMVRQGAVVIDVGTTcigytpegkrILSGDVdfeaVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAK 289
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPT----------KLSGDD----VKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
116-285 |
5.33e-13 |
|
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 66.30 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 116 PDKDVDGFHPVNVGRMCLGE---------PCFLPCTP---------HGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLAN 177
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYHNIrfldpenrkKSILPCTPlaivkilefLGIYNKILPYGNRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499238903 178 IL-----------------LQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKF-ITADMVRQGAVVIDVgttci 239
Cdd:cd01079 81 LLandgarvysvdingiqvFTRGESIRHEKHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINF----- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499238903 240 gytpegkrilSGDVDFEA-VKEKAFAITPVpkgVGPMTIIMLMLNTL 285
Cdd:cd01079 156 ----------ASIKNFEPsVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
187-234 |
4.67e-04 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 39.80 E-value: 4.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499238903 187 NATVTICHSGTKNLPLITSQADILVSAM-----GKPKFITADMVRQ---GAVVIDV 234
Cdd:smart01002 64 GARFTTLYSQAELLEEAVKEADLVIGAVlipgaKAPKLVTREMVKSmkpGSVIVDV 119
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
190-234 |
7.65e-03 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 37.38 E-value: 7.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499238903 190 VTICHSGTKNLPLITSQADILVSAM----GK-PKFITADMVRQ---GAVVIDV 234
Cdd:cd05305 215 VTTLYSNPANLEEALKEADLVIGAVlipgAKaPKLVTEEMVKTmkpGSVIVDV 267
|
|
|