|
Name |
Accession |
Description |
Interval |
E-value |
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
51-344 |
6.76e-145 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 410.56 E-value: 6.76e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:COG0190 3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:COG0190 82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLhtdgEHErpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:COG0190 162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:COG0190 232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
51-344 |
1.27e-122 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 354.32 E-value: 1.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESwvsLGNRR--PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVK---LKEQGivPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGK 208
Cdd:PRK14190 80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 209 NVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 289 GINYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14190 230 GVNRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
51-344 |
2.63e-110 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 323.02 E-value: 2.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK10792 83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK10792 163 VVVGASNIVGRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK10792 233 NRLED-----GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
51-344 |
1.09e-104 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 308.92 E-value: 1.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14186 82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDPvTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14186 232 HRLPSS-DGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
53-344 |
1.57e-99 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 295.52 E-value: 1.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14191 3 LLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14191 83 DLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14191 163 IGASNIVGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 222418558 293 VHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14191 233 LND-----GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEK 279
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
51-344 |
2.13e-99 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 295.06 E-value: 2.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRrPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14189 3 AQLIDGNALSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14189 82 IDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14189 162 VVIGRSNIVGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14189 232 NRDDA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-345 |
1.04e-98 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 293.79 E-value: 1.04e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 50 EAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLD 129
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 130 VTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKN 209
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 210 VVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVG 289
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 222418558 290 INYVHDP--VTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PRK14188 231 INRIPAPekGEGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRA 288
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
49-346 |
2.91e-94 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 282.08 E-value: 2.91e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 49 HEAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PRK14176 6 YESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGK 208
Cdd:PRK14176 86 ELIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 209 NVVVAGRSKNVGMPIA-MLLHTdgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVID 287
Cdd:PRK14176 166 NAVIVGHSNVVGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 222418558 288 VGINYVHDpvtgktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 346
Cdd:PRK14176 235 VGITKEED------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
51-344 |
7.83e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 275.86 E-value: 7.83e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK--------NATVTLTHSRT--RNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14179 232 NRDEN-----GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
52-344 |
2.15e-90 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 272.42 E-value: 2.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 52 IIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14184 2 LLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVV 211
Cdd:PRK14184 82 AELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 212 VAGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14184 162 VVGRSNIVGKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 222418558 292 YVHDpvtgktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14184 236 RTDD------GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
53-347 |
4.77e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 271.70 E-value: 4.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14185 3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14185 83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDGEherpGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 293 VHDPVTGKT-KLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKIIY 347
Cdd:PRK14185 237 VPDATRKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIY 292
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
52-339 |
1.26e-89 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 270.54 E-value: 1.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 52 IIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14174 2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRTGIQTFGKN 209
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 210 VVVAGRSKNVGMPIAMLLHtdgeHERPGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVG 289
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLML----QKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222418558 290 INYVHDPVTGK-TKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTL 339
Cdd:PRK14174 236 INRIEDPSTKSgYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
53-342 |
1.96e-89 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 270.11 E-value: 1.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGNRrPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14167 4 IIDGNAVAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14167 83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14167 163 VGRSDIVGKPMANLLIQKA----DGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 222418558 293 VHDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAA 342
Cdd:PRK14167 237 VDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
49-346 |
3.05e-89 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 269.84 E-value: 3.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 49 HEAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PLN02516 7 HVAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLD--QHSLIPATASAVWEIIKRTGIQTF 206
Cdd:PLN02516 87 SKVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 207 GKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPKEQLKIHTqlADIIIVAAGIPKLITSDMVKEGAAVI 286
Cdd:PLN02516 167 GKKAVVVGRSNIVGLPVSLLLLK--------ADATVTVVHSRTPDPESIVRE--ADIVIAAAGQAMMIKGDWIKPGAAVI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222418558 287 DVGINYVHDPvTGKT--KLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 346
Cdd:PLN02516 237 DVGTNAVSDP-SKKSgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
53-343 |
4.79e-88 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 266.31 E-value: 4.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14183 3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14183 83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14183 163 VGASNIVGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222418558 293 VHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14183 233 TED-----GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
51-343 |
2.25e-87 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 265.20 E-value: 2.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCL--DQHSLIPATASAVWEIIKRTGIQTFGK 208
Cdd:PRK14168 83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 209 NVVVAGRSKNVGMPIAMLLHTDGeherPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDV 288
Cdd:PRK14168 163 EVVVVGRSNIVGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 289 GINYV-HDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14168 237 GVNRVgTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
164-343 |
5.35e-85 |
|
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: 254.02 E-value: 5.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 164 PEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 243
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 244 IAHRYTPKeqLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPvtGKTKLVGDVDFEAVKKKAGFITPVP 323
Cdd:cd01080 73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
|
170 180
....*....|....*....|
gi 222418558 324 GGVGPMTVAMLLKNTLLAAK 343
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-345 |
1.15e-84 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 260.32 E-value: 1.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 2 TVPVRGFSLLRGRLG----RAPALGRSTapSVRAPGEPGSAFRGfrSSGVRHEAIIISGTEMAKHIQKEIQRGVESWVSL 77
Cdd:PLN02616 24 STPFNGTFLLRRCVGplrvRTTASGRGC--CINSSSSPSPVINA--DTGSEGGAKVIDGKAVAKKIRDEITIEVSRMKES 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 78 GNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERT 157
Cdd:PLN02616 100 IGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFISGFNNDPSVHGILVQLPLPSHMDEQN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 158 ICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeher 235
Cdd:PLN02616 180 ILNAVSIEKDVDGFHPLNIGRLAMRGREplFVPCTPKGCIELLHRYNVEIKGKRAVVIGRSNIVGMPAALLLQRE----- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 236 pggDATVTIAHRYT--PKEQlkihTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPVTGKT-KLVGDVDFEAV 312
Cdd:PLN02616 255 ---DATVSIVHSRTknPEEI----TREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDASSPRGyRLVGDVCYEEA 327
|
330 340 350
....*....|....*....|....*....|...
gi 222418558 313 KKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PLN02616 328 CKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
51-343 |
7.01e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 255.61 E-value: 7.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14175 3 AKILDGKQIAKDYRQGLQDQVEALKEKG-FTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14175 82 LNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGi 290
Cdd:PRK14175 162 VVIGRSHIVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 222418558 291 nyvhDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14175 231 ----NTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
51-344 |
8.12e-84 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 255.32 E-value: 8.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICS---ELilkPKDVSQEEL 127
Cdd:PRK14193 3 AIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSirrDL---PADATQEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 128 LDVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFG 207
Cdd:PRK14193 79 NAVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 208 KNVVVAGRSKNVGMPIAMLLhtdgehERPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVID 287
Cdd:PRK14193 159 AHVVVIGRGVTVGRPIGLLL------TRRSENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 222418558 288 VGINYVhdpvtGKTKLVGDVDfEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14193 231 VGVSRA-----GDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
53-343 |
1.59e-83 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 254.57 E-value: 1.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSKG-IESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS-LIPATASAVWEIIKRTGIQTFGKNVV 211
Cdd:PRK14166 82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 212 VAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 222418558 292 YVHdpvtgKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14166 232 RLE-----SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
51-342 |
4.03e-82 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 251.29 E-value: 4.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSlgnrRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14173 3 ARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14173 79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHtdgeherpGGDATVTIAHRYTPkeQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14173 159 VVVGRSNIVGKPLAALLL--------REDATVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 222418558 291 NYVHDPvTGKTKLVGDVDFEaVKKKAGFITPVPGGVGPMTVAMLLKNTLLAA 342
Cdd:PRK14173 229 NRVGGN-GGRDILTGDVHPE-VAEVAGALTPVPGGVGPMTVAMLMANTVIAA 278
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
53-345 |
1.95e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 249.61 E-value: 1.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14170 4 IIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14170 83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14170 163 IGRSNIVGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 222418558 293 VHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PRK14170 233 DEN-----NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRI 280
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-342 |
4.91e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 248.59 E-value: 4.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 50 EAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLD 129
Cdd:PRK14187 1 ETNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 130 VTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRTGIQTFG 207
Cdd:PRK14187 81 KINELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQkkNCLIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 208 KNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVID 287
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLL--------GENCTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 222418558 288 VGINYVHdpVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAA 342
Cdd:PRK14187 231 VGINSIE--EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
172-344 |
9.11e-81 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 243.14 E-value: 9.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 172 HIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPk 251
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 252 eQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVhdpvtGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTV 331
Cdd:pfam02882 72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRV-----GNGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
|
170
....*....|...
gi 222418558 332 AMLLKNTLLAAKK 344
Cdd:pfam02882 146 AMLLQNTVEAAKR 158
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
52-337 |
1.22e-79 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 244.69 E-value: 1.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 52 IIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVV 211
Cdd:PRK14172 83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 212 VAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTS 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 222418558 292 YVHDpvtgktKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKN 337
Cdd:PRK14172 233 SVNG------KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
53-347 |
5.97e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 240.63 E-value: 5.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRL--CLDQhSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14171 84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 222418558 291 NYVhdpvtGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKIIY 347
Cdd:PRK14171 233 NRI-----SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLY 284
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
49-345 |
2.05e-77 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 241.02 E-value: 2.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 49 HEAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELL 128
Cdd:PLN02897 54 QKTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQIL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 129 DVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRTGIQTF 206
Cdd:PLN02897 134 SALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREplFVSCTPKGCVELLIRSGVEIA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 207 GKNVVVAGRSKNVGMPIAMLLHtdgEHerpggDATVTIAHRYTPK-EQLkihTQLADIIIVAAGIPKLITSDMVKEGAAV 285
Cdd:PLN02897 214 GKNAVVIGRSNIVGLPMSLLLQ---RH-----DATVSTVHAFTKDpEQI---TRKADIVIAAAGIPNLVRGSWLKPGAVV 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222418558 286 IDVGINYVHDPVTG-KTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PLN02897 283 IDVGTTPVEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
52-345 |
1.12e-76 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 237.24 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 52 IIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14180 2 ILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCL-DQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14180 162 VVVGASNVVGKPVSQLLLN--------AKATVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 222418558 291 NYVhdpvtgKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKI 345
Cdd:PRK14180 232 NHV------DGKIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQEL 280
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
51-344 |
1.68e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 236.77 E-value: 1.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQD-VTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14169 80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLhtdgeherPGGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGI 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 222418558 291 NYVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14169 230 SRGAD-----GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
82-343 |
4.22e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 235.51 E-value: 4.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 82 PHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNG 161
Cdd:PRK14178 27 PRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPLPKGVDTERVIAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 162 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDAT 241
Cdd:PRK14178 107 ILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLN--------ADAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 242 VTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgktKLVGDVDFEAVKKKAGFITP 321
Cdd:PRK14178 179 VTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNG------KLCGDVDFDAVKEIAGAITP 250
|
250 260
....*....|....*....|..
gi 222418558 322 VPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14178 251 VPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-343 |
2.88e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 231.02 E-value: 2.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 50 EAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLD 129
Cdd:PRK14177 2 SPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 130 VTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKN 209
Cdd:PRK14177 82 VIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 210 VVVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVG 289
Cdd:PRK14177 162 AVVVGRSPILGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 222418558 290 INYVHdpvtgktklVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14177 232 YNPGN---------VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
53-343 |
1.41e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 229.73 E-value: 1.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14194 6 LIDGKAAAARVLAQVREDVRTLKAAG-IEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVV 212
Cdd:PRK14194 85 ELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 213 AGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINY 292
Cdd:PRK14194 165 IGRSNIVGKPMAALLLQ--------AHCSVTVVH--SRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINR 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222418558 293 VHDpvTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:PRK14194 235 IDD--DGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
52-338 |
3.82e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 223.20 E-value: 3.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 52 IIISGTEMAKHIQKEIQRGVESwvslGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVT 131
Cdd:PRK14181 1 MLLKGAPAAEHILATIKENISA----SSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 132 DQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ-HSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHtdgeHERPGGDATVTIAHryTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14181 157 AIVGRSNIVGKPLAALLM----QKHPDTNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGT 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 222418558 291 NYVHDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNT 338
Cdd:PRK14181 231 SRVPAANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
51-346 |
3.89e-67 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 212.78 E-value: 3.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 51 AIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDV 130
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 131 TDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNV 210
Cdd:PRK14192 83 IEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 211 VVAGRSKNVGMPIAMLLHTdgeherpgGDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGI 290
Cdd:PRK14192 163 VVVGRSAILGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGF 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 222418558 291 nyvHDPVTGKtklVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKII 346
Cdd:PRK14192 233 ---HPRDGGG---VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
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|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
53-344 |
5.57e-64 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 204.49 E-value: 5.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 53 IISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTD 132
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 133 QLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLI-PATASAVWEIIKRTGIQTFGKNVV 211
Cdd:PRK14182 82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPrPCTPAGVMRMLDEARVDPKGKRAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 212 VAGRSKNVGMPIAMLLhtdgeHERpggDATVTIAHRYTpkEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGIN 291
Cdd:PRK14182 162 VVGRSNIVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 222418558 292 YVHDpvtgkTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKK 344
Cdd:PRK14182 232 RLAD-----GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
54-169 |
7.41e-54 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 172.59 E-value: 7.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 54 ISGTEMAKHIQKEIQRGVESWVSLGnRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQ 133
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 222418558 134 LNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVD 169
Cdd:pfam00763 80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
187-343 |
1.35e-22 |
|
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: 91.80 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 187 IPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPKEQLKIHTqlADIIIV 266
Cdd:cd05212 8 VSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDG--------ATVYSCDWKTIQLQSKVHD--ADVVVV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222418558 267 AAGIPKLITSDMVKEGAAVIDVGINYVHDpvtgktklvgdvdfEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAK 343
Cdd:cd05212 78 GSPKPEKVPTEWIKPGATVINCSPTKLSG--------------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
164-339 |
2.16e-10 |
|
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: 59.36 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 164 PEKDVDGFHIINIGRLC-----LD----QHSLIPATASAVWEIIKRTGI---------QTFGKNVVVAGRSKNVGMPIAM 225
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222418558 226 LLHTDGE-------------HERPGGDATVTIAHRYTPKEQLKIhtQLADIIIVAAGIPKL-ITSDMVKEGAAVIDVGin 291
Cdd:cd01079 81 LLANDGArvysvdingiqvfTRGESIRHEKHHVTDEEAMTLDCL--SQSDVVITGVPSPNYkVPTELLKDGAICINFA-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 222418558 292 yvhdpvtgktklvGDVDFEA-VKKKAGFITPVpggVGPMTVAMLLKNTL 339
Cdd:cd01079 157 -------------SIKNFEPsVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
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|