|
Name |
Accession |
Description |
Interval |
E-value |
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
2-288 |
1.50e-143 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 404.78 E-value: 1.50e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 2 AKQIQKEIQQGVESWIALGnRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPR 81
Cdd:COG0190 12 AAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNV 161
Cdd:COG0190 91 VHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 162 GMPIAMLLhtdgeHERpggDATVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvtg 241
Cdd:COG0190 171 GKPLALLL-----LRR---NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVED---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720414576 242 kTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIA 288
Cdd:COG0190 237 -GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-285 |
3.36e-119 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 343.15 E-value: 3.36e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVEswiALGNRR--PHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNM 78
Cdd:PRK14190 11 VAKEKREQLKEEVV---KLKEQGivPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 79 DPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRS 158
Cdd:PRK14190 88 DPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHVVVVGRS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 159 KNVGMPIAMLLHTDgeherpggDATVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDp 238
Cdd:PRK14190 168 NIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLEN- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720414576 239 vtgkTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14190 237 ----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAK 279
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-286 |
1.43e-107 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 313.78 E-value: 1.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 2 AKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPR 81
Cdd:PRK10792 12 AQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLALIDELNADPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNV 161
Cdd:PRK10792 92 IDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNAVVVGASNIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 162 GMPIAMLLHTDGeherpggdATVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvtg 241
Cdd:PRK10792 172 GRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLED---- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720414576 242 kTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKN 286
Cdd:PRK10792 238 -GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-283 |
4.64e-107 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 312.77 E-value: 4.64e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14186 10 LAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEALIAQLNQDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14186 90 RVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKAVVVGRSIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDPvT 240
Cdd:PRK14186 170 VGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSS-D 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720414576 241 GKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLA 283
Cdd:PRK14186 239 GKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLS 281
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-286 |
1.95e-100 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 295.52 E-value: 1.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14191 9 LSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14191 89 NIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDGeherpggdATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvt 240
Cdd:PRK14191 169 VGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLND--- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720414576 241 gkTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKN 286
Cdd:PRK14191 236 --GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEK 279
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-288 |
5.56e-99 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 291.98 E-value: 5.56e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRrPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14189 11 LSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLARIDELNRDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14189 90 KIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSNI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDGeherpggdATVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvt 240
Cdd:PRK14189 170 VGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDA--- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720414576 241 gkTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIA 288
Cdd:PRK14189 237 --GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAA 282
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-288 |
5.17e-97 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 287.24 E-value: 5.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 2 AKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPR 81
Cdd:PRK14188 11 AADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALIARLNADPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNV 161
Cdd:PRK14188 91 IHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSNLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 162 GMPIAMLLHTDgeherpggDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYI--QDPV 239
Cdd:PRK14188 171 GKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIpaPEKG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720414576 240 TGKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIA 288
Cdd:PRK14188 241 EGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRAA 289
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-288 |
1.47e-92 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 275.53 E-value: 1.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14176 16 LAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14176 96 DVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIA-MLLHTdgeherpggDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpv 239
Cdd:PRK14176 176 VGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED-- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720414576 240 tgktKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIA 288
Cdd:PRK14176 243 ----KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-285 |
8.24e-91 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 270.86 E-value: 8.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14179 10 LAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDLIERYNQDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14179 90 TWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDgeherpggDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvt 240
Cdd:PRK14179 170 VGKPMAQLLLDK--------NATVTLTHSRT--RNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDEN--- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720414576 241 gkTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14179 237 --GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAAL 279
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
2-285 |
1.76e-90 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 270.11 E-value: 1.76e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 2 AKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPR 81
Cdd:PRK14184 10 AATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAELNARPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 82 VSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNV 161
Cdd:PRK14184 90 IDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNIV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 162 GMPIAMLLHTDGeherPGGDATVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvtg 241
Cdd:PRK14184 170 GKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDD---- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720414576 242 ktKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14184 240 --GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWK 281
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-281 |
4.99e-90 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 269.38 E-value: 4.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 4 QIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPRVS 83
Cdd:PRK14174 12 DLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 84 GILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNV 161
Cdd:PRK14174 92 GILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSNIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 162 GMPIAMLLHtdgeHERPGGDATVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDPVTG 241
Cdd:PRK14174 172 GKPMANLML----QKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIEDPSTK 245
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720414576 242 K-TKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTL 281
Cdd:PRK14174 246 SgYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-289 |
5.02e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 269.39 E-value: 5.02e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14185 9 ISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVRELNQDD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14185 89 DVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDGEherpGGDATVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDPVT 240
Cdd:PRK14185 169 VGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDATR 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720414576 241 GKT-KLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIAY 289
Cdd:PRK14185 243 KSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIY 292
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-288 |
5.81e-88 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 263.61 E-value: 5.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14183 9 LSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIAMMNNNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14183 89 NIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCVVGASNI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDGeherpggdATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvt 240
Cdd:PRK14183 169 VGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTED--- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720414576 241 gkTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIA 288
Cdd:PRK14183 236 --GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
106-285 |
3.08e-87 |
|
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: 257.48 E-value: 3.08e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 106 PEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDATVT 185
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 186 IAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDPvtGKTKLVGDVDFEAVKKKASFITPVP 265
Cdd:cd01080 73 VCHSKTK--NLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148
|
170 180
....*....|....*....|
gi 1720414576 266 GGVGPMTVAMLLKNTLLAAK 285
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-284 |
1.71e-86 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 260.48 E-value: 1.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESwIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14167 10 VAAQIRDDLTDAIET-LEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14167 89 DVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDGeherPGGDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDPVT 240
Cdd:PRK14167 169 VGKPMANLLIQKA----DGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDADTE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720414576 241 GKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAA 284
Cdd:PRK14167 243 KGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-286 |
9.17e-85 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 255.72 E-value: 9.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGnRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14166 9 LSAKIKEELKEKNQFLKSKG-IESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINTLNHDD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS-LIPATASAVWEIIKRAGIETFGKNVVVAGRSK 159
Cdd:PRK14166 88 SVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESgFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 160 NVGMPIAMLLHTDGeherpggdATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQdpv 239
Cdd:PRK14166 168 IVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLE--- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720414576 240 tgKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKN 286
Cdd:PRK14166 235 --SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKN 279
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-285 |
2.09e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 255.19 E-value: 2.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 3 KQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPRV 82
Cdd:PRK14168 13 EEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLALIDKYNNDDSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 83 SGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCL--DQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14168 93 HGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGAEVVVVGRSNI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDGeherPGGDATVTIAHryTPREQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYI-QDPV 239
Cdd:PRK14168 173 VGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVgTNES 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720414576 240 TGKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14168 247 TGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
1-285 |
3.47e-84 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 254.82 E-value: 3.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PLN02516 17 IAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLD--QHSLIPATASAVWEIIKRAGIETFGKNVVVAGRS 158
Cdd:PLN02516 97 DVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 159 KNVGMPIAMLLHTdgeherpgGDATVTIAHRYTPREQlkAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDP 238
Cdd:PLN02516 177 NIVGLPVSLLLLK--------ADATVTVVHSRTPDPE--SIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSDP 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720414576 239 vTGKT--KLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PLN02516 247 -SKKSgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAK 294
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
23-284 |
4.50e-84 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 253.98 E-value: 4.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 23 RPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICN 102
Cdd:PRK14173 29 VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLELIARLNADPEVDGILVQLPLPPHIDFQRVLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 103 GIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGDA 182
Cdd:PRK14173 109 AIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEVVVVGRSNIVGKPLAALLL--------REDA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 183 TVTIAHRYTPreQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDPvTGKTKLVGDVDFEaVKKKASFIT 262
Cdd:PRK14173 181 TVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGGN-GGRDILTGDVHPE-VAEVAGALT 256
|
250 260
....*....|....*....|..
gi 1720414576 263 PVPGGVGPMTVAMLLKNTLLAA 284
Cdd:PRK14173 257 PVPGGVGPMTVAMLMANTVIAA 278
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
2-288 |
3.48e-83 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 251.47 E-value: 3.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 2 AKQIQKEIQQGVESWIALGnRRPHLSIILVGDNPASHTYVRNKIKAASAVGICS---ELiikPKNVSQEELLDITDQLNM 78
Cdd:PRK14193 12 ADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSirrDL---PADATQEELNAVIDELNA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 79 DPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRS 158
Cdd:PRK14193 88 DPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHVVVIGRG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 159 KNVGMPIAMLLhtdgehERPGGDATVTIAHryTPREQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIqdp 238
Cdd:PRK14193 168 VTVGRPIGLLL------TRRSENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRA--- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720414576 239 vtGKTKLVGDVDfEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIA 288
Cdd:PRK14193 237 --GDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRA 283
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-285 |
3.78e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 251.76 E-value: 3.78e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 3 KQIQKEIQQG----VESWIALGnRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNM 78
Cdd:PRK14175 9 KQIAKDYRQGlqdqVEALKEKG-FTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 79 DPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRS 158
Cdd:PRK14175 88 DDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNAVVIGRS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 159 KNVGMPIAMLLHTdgeherpgGDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGinyiqDP 238
Cdd:PRK14175 168 HIVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG-----NT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720414576 239 VTGKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14175 233 PDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
1-287 |
4.37e-83 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 254.16 E-value: 4.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PLN02616 81 VAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFISGFNNDP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRAGIETFGKNVVVAGRS 158
Cdd:PLN02616 161 SVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREplFVPCTPKGCIELLHRYNVEIKGKRAVVIGRS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 159 KNVGMPIAMLLHTDgeherpggDATVTIAHRYT--PREQlkahTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQ 236
Cdd:PLN02616 241 NIVGMPAALLLQRE--------DATVSIVHSRTknPEEI----TREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVE 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720414576 237 DPVTGKT-KLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNI 287
Cdd:PLN02616 309 DASSPRGyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
114-285 |
1.68e-82 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 245.45 E-value: 1.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 114 HIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDgeherpggDATVTIAHRYTPr 193
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 194 eQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIqdpvtGKTKLVGDVDFEAVKKKASFITPVPGGVGPMTV 273
Cdd:pfam02882 72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRV-----GNGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
|
170
....*....|..
gi 1720414576 274 AMLLKNTLLAAK 285
Cdd:pfam02882 146 AMLLQNTVEAAK 157
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
24-286 |
1.04e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 240.50 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 24 PHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14187 33 PCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQLPVPNHIDKNLIINT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 104 IAPEKDVDGFHIINIGRLCLDQ--HSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHtdgeherpGGD 181
Cdd:PRK14187 113 IDPEKDVDGFHNENVGRLFTGQkkNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLL--------GEN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 182 ATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQdpVTGKTKLVGDVDFEAVKKKASFI 261
Cdd:PRK14187 185 CTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIE--EGGVKKFVGDVDFAEVKKKASAI 260
|
250 260
....*....|....*....|....*
gi 1720414576 262 TPVPGGVGPMTVAMLLKNTLLAAKN 286
Cdd:PRK14187 261 TPVPGGVGPMTIAFLMVNTVIAACN 285
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-285 |
6.75e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 238.31 E-value: 6.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESwIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14169 9 VSKKILADLKQTVAK-LAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKVAELNHDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14169 88 DVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVVIVGRSNI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLhtdgeherPGGDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvt 240
Cdd:PRK14169 168 VGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGAD--- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720414576 241 gkTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14169 235 --GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAK 277
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-289 |
7.41e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 235.62 E-value: 7.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14171 10 LANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINELNLDN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRL--CLDQhSLIPATASAVWEIIKRAGIETFGKNVVVAGRS 158
Cdd:PRK14171 90 EISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNVVIIGRS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 159 KNVGMPIAMLLHTDgeherpggDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIqdp 238
Cdd:PRK14171 169 NIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI--- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1720414576 239 vtGKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIAY 289
Cdd:PRK14171 236 --SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFKDSLY 284
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
24-286 |
1.27e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 234.74 E-value: 1.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 24 PHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14178 27 PRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPLPKGVDTERVIAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 104 IAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDAT 183
Cdd:PRK14178 107 ILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLN--------ADAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 184 VTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvtgktKLVGDVDFEAVKKKASFITP 263
Cdd:PRK14178 179 VTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNG------KLCGDVDFDAVKEIAGAITP 250
|
250 260
....*....|....*....|...
gi 1720414576 264 VPGGVGPMTVAMLLKNTLLAAKN 286
Cdd:PRK14178 251 VPGGVGPMTIATLMENTFDAAKM 273
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-287 |
1.62e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 234.58 E-value: 1.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGnRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14170 10 LAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14170 89 TIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDgeherpggDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvt 240
Cdd:PRK14170 169 VGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDEN--- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720414576 241 gkTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNI 287
Cdd:PRK14170 236 --NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRI 280
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
3-287 |
3.75e-76 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 235.62 E-value: 3.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 3 KQIQKEIQQGVESWI-----ALGnRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLN 77
Cdd:PLN02897 62 NVIAEEIRTKIASEVrkmkkAVG-KVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSALRKFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 78 MDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHS--LIPATASAVWEIIKRAGIETFGKNVVVA 155
Cdd:PLN02897 141 EDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREplFVSCTPKGCVELLIRSGVEIAGKNAVVI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 156 GRSKNVGMPIAMLLHtdgEHerpggDATVTIAHRYTPR-EQLkahTQLADIIIVAAGIPRLITADMVREGAAVIDVGINY 234
Cdd:PLN02897 221 GRSNIVGLPMSLLLQ---RH-----DATVSTVHAFTKDpEQI---TRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTP 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1720414576 235 IQDPVTG-KTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNI 287
Cdd:PLN02897 290 VEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
23-285 |
7.26e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 233.58 E-value: 7.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 23 RPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICN 102
Cdd:PRK14194 33 EPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIAELNADPSVNGILLQLPLPAHIDEARVLQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 103 GIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDA 182
Cdd:PRK14194 113 AINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHAVVIGRSNIVGKPMAALLLQ--------AHC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 183 TVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvTGKTKLVGDVDFEAVKKKASFIT 262
Cdd:PRK14194 185 SVTVVHSRS--TDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDD--DGRSRLVGDVDFDSALPVVSAIT 260
|
250 260
....*....|....*....|...
gi 1720414576 263 PVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14194 261 PVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-279 |
1.14e-75 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 232.36 E-value: 1.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14172 10 VALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIEELNKDN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14172 90 NVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTDgeherpggDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvt 240
Cdd:PRK14172 170 VGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNG--- 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720414576 241 gktKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKN 279
Cdd:PRK14172 237 ---KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
24-287 |
1.77e-75 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 231.84 E-value: 1.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 24 PHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICNG 103
Cdd:PRK14180 32 PKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPLPAHINKNNVIYS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 104 IAPEKDVDGFHIINIGRLCL-DQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTdgeherpgGDA 182
Cdd:PRK14180 112 IKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVGKPVSQLLLN--------AKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 183 TVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpvtgktKLVGDVDFEAVKKKASFIT 262
Cdd:PRK14180 184 TVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDG------KIVGDVDFAAVKDKVAAIT 255
|
250 260
....*....|....*....|....*
gi 1720414576 263 PVPGGVGPMTVAMLLKNTLLAAKNI 287
Cdd:PRK14180 256 PVPGGVGPMTITELLYNTFQCAQEL 280
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-285 |
6.18e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 230.63 E-value: 6.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14177 11 LSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDKLNLDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14177 91 NVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVVVGRSPI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINyiqdpvT 240
Cdd:PRK14177 171 LGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN------P 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720414576 241 GKtklVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14177 235 GN---VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
9-280 |
1.21e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 219.73 E-value: 1.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 9 IQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDPRVSGILVQ 88
Cdd:PRK14181 12 ILATIKENISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGILVQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 89 LPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQ-HSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAM 167
Cdd:PRK14181 92 LPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 168 LLHtdgeHERPGGDATVTIAHryTPREQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDPVTGKTKLVG 247
Cdd:PRK14181 172 LLM----QKHPDTNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAANPKGYILVG 245
|
250 260 270
....*....|....*....|....*....|...
gi 1720414576 248 DVDFEAVKKKASFITPVPGGVGPMTVAMLLKNT 280
Cdd:PRK14181 246 DVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-288 |
8.28e-68 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 212.19 E-value: 8.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGnRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14182 9 IAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLI-PATASAVWEIIKRAGIETFGKNVVVAGRSK 159
Cdd:PRK14182 88 AVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPrPCTPAGVMRMLDEARVDPKGKRALVVGRSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 160 NVGMPIAMLLhtdgeHERpggDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINYIQDpv 239
Cdd:PRK14182 168 IVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLAD-- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720414576 240 tgkTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNIA 288
Cdd:PRK14182 236 ---GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTA 281
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-285 |
1.54e-67 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 211.63 E-value: 1.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGNRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:PRK14192 11 LAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKN 160
Cdd:PRK14192 91 DVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 161 VGMPIAMLLHTdgeherpgGDATVTIAHRYTprEQLKAHTQLADIIIVAAGIPRLITADMVREGAAVIDVGINyiqdPVT 240
Cdd:PRK14192 171 LGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFH----PRD 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720414576 241 GKTklVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:PRK14192 237 GGG--VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAE 279
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
1-111 |
2.15e-51 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 164.50 E-value: 2.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 1 MAKQIQKEIQQGVESWIALGnRRPHLSIILVGDNPASHTYVRNKIKAASAVGICSELIIKPKNVSQEELLDITDQLNMDP 80
Cdd:pfam00763 6 IAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADP 84
|
90 100 110
....*....|....*....|....*....|.
gi 1720414576 81 RVSGILVQLPLPDHVDERTICNGIAPEKDVD 111
Cdd:pfam00763 85 SVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
129-285 |
2.36e-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: 90.26 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 129 IPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDGeherpggdATVTIAHRYTPREQLKAHTqlADIIIV 208
Cdd:cd05212 8 VSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDG--------ATVYSCDWKTIQLQSKVHD--ADVVVV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720414576 209 AAGIPRLITADMVREGAAVIDVGINYIQDpvtgktklvgdvdfEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAK 285
Cdd:cd05212 78 GSPKPEKVPTEWIKPGATVINCSPTKLSG--------------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
106-281 |
4.83e-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: 57.82 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 106 PEKDVDGFHIINIGRLC-----LD----QHSLIPATASAVWEIIKRAGI---------ETFGKNVVVAGRSKNVGMPIAM 167
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 168 LLHTDGEH----ERPGGDA-TVTIAHRYTP----REQLKAHTQLADIIIVAAGIPRL---ITADMVREGAAVIDVGinyi 235
Cdd:cd01079 81 LLANDGARvysvDINGIQVfTRGESIRHEKhhvtDEEAMTLDCLSQSDVVITGVPSPnykVPTELLKDGAICINFA---- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720414576 236 qdpvtgktklvGDVDFEA-VKKKASFITPVpggVGPMTVAMLLKNTL 281
Cdd:cd01079 157 -----------SIKNFEPsVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| NAD_bind_amino_acid_DH |
cd05191 |
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ... |
131-231 |
6.95e-03 |
|
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate 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: 133449 [Multi-domain] Cd Length: 86 Bit Score: 35.05 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414576 131 ATASAVWEIIKRAGIETF----GKNVVVAGRsKNVGMPIAMLLHTDGEherpggdATVTIAHRytpreqlkahtqlaDII 206
Cdd:cd05191 1 ATAAGAVALLKAAGKVTNkslkGKTVVVLGA-GEVGKGIAKLLADEGG-------KKVVLCDR--------------DIL 58
|
90 100
....*....|....*....|....*...
gi 1720414576 207 IVAAGIPRLITADMV---REGAAVIDVG 231
Cdd:cd05191 59 VTATPAGVPVLEEATakiNEGAVVIDLA 86
|
|
|