|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-284 |
0e+00 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 551.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PRK14193 1 MTAIILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14193 81 VIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTRRSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGK 240
Cdd:PRK14193 161 VVVIGRGVTVGRPIGLLLTRRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDGK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 664524730 241 IVGDVHPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14193 241 LVGDVHPDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
1-284 |
2.44e-176 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 487.60 E-value: 2.44e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:COG0190 1 MMAQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:COG0190 81 LIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGK 240
Cdd:COG0190 161 AVVVGRSNIVGKPLALLLLRR--NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 664524730 241 IVGDVH-PDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:COG0190 239 LVGDVDfESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAG 283
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-284 |
2.34e-127 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 363.56 E-value: 2.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PRK14190 1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTRrsENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGK 240
Cdd:PRK14190 161 VVVVGRSNIVGKPVGQLLLN--ENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 664524730 241 IVGDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14190 239 LCGDVDFDnVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGG 283
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-284 |
1.05e-114 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 331.65 E-value: 1.05e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PRK14189 1 MTAQLIDGNALSKQLRAEAAQRAAALTARGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14189 81 RIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGK 240
Cdd:PRK14189 161 AVVIGRSNIVGKPMAMLLLQA--GATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAGK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 664524730 241 IVGDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14189 239 LCGDVDFAgVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAA 283
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-282 |
4.53e-114 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 329.96 E-value: 4.53e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERGV-TPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIE 79
Cdd:PRK10792 1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLrAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 80 AVVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGA 159
Cdd:PRK10792 81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 160 EVVVVGRGVTIGRPMP--LLLTRrsenATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNA 237
Cdd:PRK10792 161 NAVVVGASNIVGRPMSleLLLAG----CTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 664524730 238 EGKIVGDVHPDVA-EVAAWISPNPGGVGPMTRAQLLVNVVEAAERR 282
Cdd:PRK10792 237 DGKLVGDVEFETAaERASWITPVPGGVGPMTVATLLENTLQACEEY 282
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-284 |
1.87e-109 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 318.55 E-value: 1.87e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 2 TAQILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PRK14186 1 MALILDGKALAAEIEQRLQAQIESNLPKaGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14186 81 LIAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLtrRSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSR----N 236
Cdd:PRK14186 161 AVVVGRSILVGKPLALML--LAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRlpssD 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 664524730 237 AEGKIVGDV-HPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14186 239 GKTRLCGDVdFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRHG 287
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-284 |
1.72e-105 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 308.24 E-value: 1.72e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 4 QILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14184 2 LLLDGKATAATIREELKTEVAALTARhGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14184 82 AELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTRRSE--NATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGk 240
Cdd:PRK14184 162 VVGRSNIVGKPLALMLGAPGKfaNATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG- 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 664524730 241 IVGDV-HPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14184 241 LVGDCdFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKERVG 285
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-284 |
2.16e-102 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 300.72 E-value: 2.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 2 TAQILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAhGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTRrsENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSR----- 235
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLA--ANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRipape 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 664524730 236 NAEGK--IVGDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14188 239 KGEGKtrLVGDVAFAeAAEVAGAITPVPGGVGPMTIACLLANTLTAACRAAG 290
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-283 |
2.71e-100 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 295.14 E-value: 2.71e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 4 QILDGKATAAAIKSELTARVAALK-ERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTaQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKIV 242
Cdd:PRK14191 162 IIGASNIVGKPLAMLML--NAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 664524730 243 GDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRA 283
Cdd:PRK14191 240 GDVDFEnVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQ 281
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-284 |
2.44e-96 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 285.52 E-value: 2.44e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 3 AQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14167 82 DELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTRRSE--NATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSR----N 236
Cdd:PRK14167 162 VVGRSDIVGKPMANLLIQKADggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRvdadT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 664524730 237 AEG-KIVGDVHPDVA-EVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14167 242 EKGyELVGDVEFESAkEKASAITPVPGGVGPMTRAMLLYNTVKAASLQEG 291
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-283 |
9.32e-94 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 278.25 E-value: 9.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 4 QILDGKATAAAIKSELTARVAALK-ERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDELKlVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14183 82 AMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKIV 242
Cdd:PRK14183 162 VVGASNIVGKPMAALLLNA--NATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDGRLV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 664524730 243 GDV-HPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRA 283
Cdd:PRK14183 240 GDVdFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-284 |
1.02e-93 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 278.25 E-value: 1.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERgvtPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PRK14173 1 MAARELSGPPAAEAVYAELRARLAKLPFV---PHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14173 78 LIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTRrsENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSR--NAE 238
Cdd:PRK14173 158 VVVVGRSNIVGKPLAALLLR--EDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRvgGNG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 664524730 239 GK--IVGDVHPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14173 236 GRdiLTGDVHPEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALRRRG 283
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-283 |
1.61e-93 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 277.79 E-value: 1.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 3 AQILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAV 81
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEkGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 82 VRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEV 161
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 162 VVVGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKI 241
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK--NATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENGKL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 664524730 242 VGDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRA 283
Cdd:PRK14179 240 IGDVDFDeVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSL 282
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-281 |
2.21e-92 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 275.15 E-value: 2.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 5 ILDGKATAAAIKSELTARVAALK-ERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVR 83
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERLKsNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 84 ELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVVV 163
Cdd:PRK14176 90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 164 VGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNaEGKIVG 243
Cdd:PRK14176 170 VGHSNVVGKPMAAMLLNR--NATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKE-EDKVYG 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 664524730 244 DVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAER 281
Cdd:PRK14176 247 DVDFEnVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-282 |
1.60e-90 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 269.97 E-value: 1.60e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 5 ILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVRE 84
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 85 LNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLN-EPAPLPCTPHGILTLLRRHGVEIKGAEVVV 163
Cdd:PRK14166 83 LNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 164 VGRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKIVG 243
Cdd:PRK14166 163 IGASNIVGRPMATMLL--NAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 664524730 244 DVH-PDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERR 282
Cdd:PRK14166 241 DVDfEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNR 280
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-284 |
2.27e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 264.40 E-value: 2.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 5 ILDGKATAAaikSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVRE 84
Cdd:PRK14178 2 ILDGKAVSE---KRLELLKEEIIESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 85 LNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVVVV 164
Cdd:PRK14178 79 LNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 165 GRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRnAEGKIVGD 244
Cdd:PRK14178 159 GRSIDVGRPMAALLL--NADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQ-VNGKLCGD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 664524730 245 VHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14178 236 VDFDaVKEIAGAITPVPGGVGPMTIATLMENTFDAAKMRCC 276
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
2-281 |
4.51e-88 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 264.45 E-value: 4.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 2 TAQILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PLN02516 8 VAQIIDGKAIAKAIRSEIAEEVAQLSEKhGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLN--EPAPLPCTPHGILTLLRRHGVEIKG 158
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 159 AEVVVVGRGVTIGRPMPLLLTRrsENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGV----- 233
Cdd:PLN02516 168 KKAVVVGRSNIVGLPVSLLLLK--ADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTnavsd 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 664524730 234 -SRNAEGKIVGDV-HPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAER 281
Cdd:PLN02516 246 pSKKSGYRLVGDVdFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-283 |
5.16e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 263.73 E-value: 5.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 3 AQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14169 81 AELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKIV 242
Cdd:PRK14169 161 IVGRSNIVGRPLAGLMV--NHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGKLL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 664524730 243 GDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRA 283
Cdd:PRK14169 239 GDVDEAaVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRA 280
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-284 |
3.82e-86 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 259.01 E-value: 3.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIE 79
Cdd:PRK14192 1 MMALVLDGKALAKQIEEELSVRVEALKAKtGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 80 AVVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGA 159
Cdd:PRK14192 81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 160 EVVVVGRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEG 239
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLL--NANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGG 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 664524730 240 KiVGDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14192 239 G-VGDIELQgIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-281 |
8.10e-86 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 258.60 E-value: 8.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 4 QILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14174 2 LIIDGKKVSLDLKNELKTRVEAYRAKtGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLN--EPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGhlDKCFVSCTPYGILELLGRYNIETKGKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTR--RSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGV----- 233
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLMLQklKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGInried 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 664524730 234 -SRNAEGKIVGDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAER 281
Cdd:PRK14174 242 pSTKSGYRLVGDVDYEgVSAKASAITPVPGGVGPMTIAMLLKNTLQSFER 291
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-279 |
9.29e-85 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 255.96 E-value: 9.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIE 79
Cdd:PRK14168 1 MSAKIIKGTEIREEILEEIRGEVAELKEKyGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 80 AVVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVL--NEPAPLPCTPHGILTLLRRHGVEIK 157
Cdd:PRK14168 81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 158 GAEVVVVGRGVTIGRPMPLLLTRR--SENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSR 235
Cdd:PRK14168 161 GAEVVVVGRSNIVGKPIANMMTQKgpGANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 664524730 236 ----NAEGKIV--GDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAA 279
Cdd:PRK14168 241 vgtnESTGKAIlsGDVDFDaVKEIAGKITPVPGGVGPMTIAMLMRNTLKSA 291
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-283 |
2.72e-84 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 254.18 E-value: 2.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 5 ILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVRE 84
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAARGVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 85 LNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPA-PLPCTPHGILTLLRRHGVEIKGAEVVV 163
Cdd:PRK14182 83 LNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGvPRPCTPAGVMRMLDEARVDPKGKRALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 164 VGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKIVG 243
Cdd:PRK14182 163 VGRSNIVGKPMAMMLLER--HATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADGKLVG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 664524730 244 DV-HPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRA 283
Cdd:PRK14182 241 DVeFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTA 281
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
123-283 |
4.10e-84 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 249.30 E-value: 4.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 123 HPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVVVVGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLR 202
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--NATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 203 RADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKIVGDVH-PDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAER 281
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDfENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKR 158
|
..
gi 664524730 282 RA 283
Cdd:pfam02882 159 QL 160
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
3-281 |
1.09e-83 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 255.70 E-value: 1.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 3 AQILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAV 81
Cdd:PLN02616 73 AKVIDGKAVAKKIRDEITIEVSRMKESiGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 82 VRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVL--NEPAPLPCTPHGILTLLRRHGVEIKGA 159
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrgREPLFVPCTPKGCIELLHRYNVEIKGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 160 EVVVVGRGVTIGRPMPLLLTRrsENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGV-----S 234
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQR--EDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGInpvedA 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 664524730 235 RNAEG-KIVGDV-HPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAER 281
Cdd:PLN02616 311 SSPRGyRLVGDVcYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-284 |
4.73e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 251.37 E-value: 4.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PRK14175 1 MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14175 81 ELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGK 240
Cdd:PRK14175 161 AVVIGRSHIVGQPVSKLLLQK--NASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 664524730 241 IVGDV-HPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14175 239 LKGDVdYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMRRG 283
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-281 |
1.60e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 247.43 E-value: 1.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 4 QILDGKATAAAIKSELTARVAALKERG-VTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAKGgKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14185 82 RELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTRRSE--NATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEG- 239
Cdd:PRK14185 162 VLGRSNIVGKPMAQLMMQKAYpgDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDAt 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 664524730 240 -----KIVGDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEAAER 281
Cdd:PRK14185 242 rksgfKLTGDVKFDeVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKK 289
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-278 |
4.62e-81 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 245.85 E-value: 4.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 4 QILDGKATAAAIKSELTARVAALKERG-VTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGlSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14172 83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSrNAEGKIV 242
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLL--NENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTS-SVNGKIT 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 664524730 243 GDVHPD-VAEVAAWISPNPGGVGPMTRAQLLVNVVEA 278
Cdd:PRK14172 240 GDVNFDkVIDKASYITPVPGGVGSLTTTLLIKNVCEA 276
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-281 |
8.01e-80 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 244.87 E-value: 8.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 2 TAQILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PLN02897 55 KTVVIDGNVIAEEIRTKIASEVRKMKKAvGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVL--NEPAPLPCTPHGILTLLRRHGVEIKG 158
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrgREPLFVSCTPKGCVELLIRSGVEIAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 159 AEVVVVGRGVTIGRPMPLLLTRrsENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGV----- 233
Cdd:PLN02897 215 KNAVVIGRSNIVGLPMSLLLQR--HDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTtpved 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 664524730 234 -SRNAEGKIVGDV-HPDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAER 281
Cdd:PLN02897 293 sSCEFGYRLVGDVcYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKR 342
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
115-280 |
2.43e-78 |
|
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: 234.76 E-value: 2.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 115 PDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVVVVGRGVTIGRPMPLLLTRRseNATVTQCHTGT 194
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNR--NATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 195 RDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSR---NAEGKIVGDVHPD-VAEVAAWISPNPGGVGPMTRAQ 270
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRvpdKSGGKLVGDVDFEsAKEKASAITPVPGGVGPMTVAM 158
|
170
....*....|
gi 664524730 271 LLVNVVEAAE 280
Cdd:cd01080 159 LMKNTVEAAK 168
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-281 |
2.79e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 231.50 E-value: 2.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 3 AQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVV 82
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 83 RELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14170 82 EELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKIV 242
Cdd:PRK14170 162 VIGRSNIVGKPVAQLLL--NENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLC 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 664524730 243 GDVH-PDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAER 281
Cdd:PRK14170 240 GDVDfDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-278 |
7.33e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 230.23 E-value: 7.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 5 ILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVR 83
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQtNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 84 ELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLN-EPAPLPCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14171 84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGiSQGFIPCTALGCLAVIKKYEPNLTGKNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTRrsENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEGKIV 242
Cdd:PRK14171 164 IIGRSNIVGKPLSALLLK--ENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGNKII 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 664524730 243 GDVH-PDVAEVAAWISPNPGGVGPMTRAQLLVNVVEA 278
Cdd:PRK14171 242 GDVDfENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-284 |
1.04e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 230.10 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 5 ILDGKATAAAIKSELTARVAALK-ERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVR 83
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKrQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 84 ELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAP--LPCTPHGILTLLRRHGVEIKGAEV 161
Cdd:PRK14187 84 ELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNclIPCTPKGCLYLIKTITRNLSGSDA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 162 VVVGRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAEG-- 239
Cdd:PRK14187 164 VVIGRSNIVGKPMACLLL--GENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGgv 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 664524730 240 -KIVGDVH-PDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAERRAG 284
Cdd:PRK14187 242 kKFVGDVDfAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAACNQKG 288
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-283 |
2.21e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 227.04 E-value: 2.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEA 80
Cdd:PRK14194 2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 81 VVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGAE 160
Cdd:PRK14194 82 LIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 161 VVVVGRGVTIGRPMPLLLTRrsENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSR---NA 237
Cdd:PRK14194 162 AVVIGRSNIVGKPMAALLLQ--AHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRiddDG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 664524730 238 EGKIVGDVHPDVA-EVAAWISPNPGGVGPMTRAQLLVNVVEAAERRA 283
Cdd:PRK14194 240 RSRLVGDVDFDSAlPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQA 286
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-279 |
1.49e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 219.07 E-value: 1.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 1 MTAQILDGKATAAAIKSELTARVAALKERGV-TPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIE 79
Cdd:PRK14177 1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKrIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 80 AVVRELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPLPCTPHGILTLLRRHGVEIKGA 159
Cdd:PRK14177 81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 160 EVVVVGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSRNAeg 239
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTEM--NATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGN-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 664524730 240 kiVGDVHPDVA-EVAAWISPNPGGVGPMTRAQLLVNVVEAA 279
Cdd:PRK14177 237 --VGDIEISKAkDKSSFYTPVPGGVGPMTIAVLLLQTLYSF 275
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-280 |
1.64e-70 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 219.13 E-value: 1.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 5 ILDGKATAAAIKSELTARVAALKER-GVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVR 83
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHtAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 84 ELNEDPDCTGYIVQLPLPRGIDENRILELMDPDKDADGLHPMNLGRLVLNEPAPL-PCTPHGILTLLRRHGVEIKGAEVV 162
Cdd:PRK14180 83 QLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLeSCTPKGIMTMLREYGIKTEGAYAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 163 VVGRGVTIGRPMPLLLTrrSENATVTQCHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSrNAEGKIV 242
Cdd:PRK14180 163 VVGASNVVGKPVSQLLL--NAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGIN-HVDGKIV 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 664524730 243 GDVH-PDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAE 280
Cdd:PRK14180 240 GDVDfAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQ 278
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
33-281 |
3.97e-63 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 200.47 E-value: 3.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 33 PGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVRELNEDPDCTGYIVQLPLPRGIDENRILEL 112
Cdd:PRK14181 27 PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGILVQLPLPKHLDAQAILQA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 113 MDPDKDADGLHPMNLGRLVLNEPAPL-PCTPHGILTLLRRHGVEIKGAEVVVVGRGVTIGRPMPLLLTRR--SENATVTQ 189
Cdd:PRK14181 107 ISPDKDVDGLHPVNMGKLLLGETDGFiPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLMQKhpDTNATVTL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 190 CHTGTRDLAAHLRRADIVVAAAGSPHLVRAEDVKPGAAVLDVGVSR----NAEGKI-VGDVH-PDVAEVAAWISPNPGGV 263
Cdd:PRK14181 187 LHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRvpaaNPKGYIlVGDVDfNNVVPKCRAITPVPGGV 266
|
250
....*....|....*...
gi 664524730 264 GPMTRAQLLVNVVEAAER 281
Cdd:PRK14181 267 GPMTVAMLMRNTWESYLR 284
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
6-120 |
1.04e-58 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 182.99 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 6 LDGKATAAAIKSELTARVAALKERGVTPGLGTVLVGDDPGSQKYVAGKHRDCAQVGIASIQRELPATATQEEIEAVVREL 85
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAGGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKL 80
|
90 100 110
....*....|....*....|....*....|....*
gi 664524730 86 NEDPDCTGYIVQLPLPRGIDENRILELMDPDKDAD 120
Cdd:pfam00763 81 NADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
138-280 |
2.35e-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: 95.27 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 138 LPCTPHGI-------LTLLRRHGVEIKGAEVVVVGRGVTIGRPMPLLLTRRseNATVTQCHTGTRDLAAHLRRADIVVAA 210
Cdd:cd05212 1 GPCTPLFVspvakavKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRD--GATVYSCDWKTIQLQSKVHDADVVVVG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 211 AGSPHLVRAEDVKPGAAVLDVGVSRNAegkivGDvhpDVAEVAAWISPNPGGVGPMTRAQLLVNVVEAAE 280
Cdd:cd05212 79 SPKPEKVPTEWIKPGATVINCSPTKLS-----GD---DVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
115-276 |
6.79e-11 |
|
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: 60.13 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 115 PDKDADGLHPMNLGRLVLNE---------PAPLPCTPHGILTLLRRHGV---------EIKGAEVVVVGRGVTIGRPMPL 176
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYHNIrfldpenrkKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 177 LLTrrSENATV-------TQCHT---GTRDLAAHLRR-----------ADIVVAAAGSPHL-VRAEDVKPGAAVLDVGVS 234
Cdd:cd01079 81 LLA--NDGARVysvdingIQVFTrgeSIRHEKHHVTDeeamtldclsqSDVVITGVPSPNYkVPTELLKDGAICINFASI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 664524730 235 RNAEgkivgdvhPDVAEVAAWISPNpggVGPMTRAQLLVNVV 276
Cdd:cd01079 159 KNFE--------PSVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| COG5322 |
COG5322 |
Predicted amino acid dehydrogenase [General function prediction only]; |
149-249 |
5.30e-09 |
|
Predicted amino acid dehydrogenase [General function prediction only];
Pssm-ID: 444114 [Multi-domain] Cd Length: 362 Bit Score: 56.39 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664524730 149 LRRHGVEIKGAEVVVVGRGVTIGRPMPLLLTRRSENATVTQCHTG-------------------TRDLAAHLRRADIVVA 209
Cdd:COG5322 142 AERMGIDLKKATVAVVGATGSIGSVCARLLAREVKRLTLVARNLErleelaeeilrnpggkvtiTTDIDEALREADIVVT 221
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 664524730 210 AAGSPH-LVRAEDVKPGAAVLDVGVSRNAEGKiVGDVHPDV 249
Cdd:COG5322 222 VTSAVGaIIDPEDLKPGAVVCDVARPRDVSRR-VAEKRPDV 261
|
|
| HemA |
COG0373 |
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
196-252 |
4.26e-04 |
|
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440142 [Multi-domain] Cd Length: 425 Bit Score: 41.25 E-value: 4.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664524730 196 DLAAHLRRADIVVAAAGSPH-LVRAEDVKPGAA--------VLDVGVSRnaegkivgDVHPDVAEV 252
Cdd:COG0373 235 ELPEALAEADIVISSTGAPHpVITKEMVERALKkrrhrplfLIDLAVPR--------DIEPEVGEL 292
|
|
| hemA |
PRK00045 |
glutamyl-tRNA reductase; Reviewed |
196-252 |
5.53e-04 |
|
glutamyl-tRNA reductase; Reviewed
Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 40.94 E-value: 5.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664524730 196 DLAAHLRRADIVVAAAGSPHLV-RAEDVKPGAA--------VLDVGVSRnaegkivgDVHPDVAEV 252
Cdd:PRK00045 235 ELPEALAEADIVISSTGAPHPIiGKGMVERALKarrhrpllLVDLAVPR--------DIEPEVGEL 292
|
|
|