|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-285 |
0e+00 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 612.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK10792 1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK10792 81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKV 240
Cdd:PRK10792 161 NAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLEDGKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 556490405 241 VGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYHDV 285
Cdd:PRK10792 241 VGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
1-286 |
0e+00 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 513.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGkRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:COG0190 1 MMAQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:COG0190 80 ALIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKV 240
Cdd:COG0190 160 HAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGKL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 556490405 241 VGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYHDVE 286
Cdd:COG0190 240 VGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGLR 285
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-285 |
4.24e-134 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 380.90 E-value: 4.24e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGKrAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14190 1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGI-VPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK14190 80 ALIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKV 240
Cdd:PRK14190 160 HVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGKL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 556490405 241 VGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYHDV 285
Cdd:PRK14190 240 CGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-280 |
3.84e-129 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 368.25 E-value: 3.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGKRaPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14189 1 MTAQLIDGNALSKQLRAEAAQRAAALTARGHQ-PGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK14189 80 ARIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKV 240
Cdd:PRK14189 160 HAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAGKL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 556490405 241 VGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACE 280
Cdd:PRK14189 240 CGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAE 279
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-280 |
3.32e-128 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 366.01 E-value: 3.32e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 4 KIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELI 83
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 84 DTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVGD 243
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLVGD 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 556490405 244 VVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACE 280
Cdd:PRK14191 242 VDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-279 |
3.65e-127 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 363.51 E-value: 3.65e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 2 AAKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLE 81
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 82 LIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLN 161
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 162 AVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLES---- 237
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPApekg 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 556490405 238 ---GKVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQAC 279
Cdd:PRK14188 241 egkTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAA 285
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-278 |
8.41e-122 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 350.13 E-value: 8.41e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 3 AKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLEL 82
Cdd:PRK14186 2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 83 IDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNA 162
Cdd:PRK14186 82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 163 VVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLES----G 238
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSsdgkT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 556490405 239 KVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQA 278
Cdd:PRK14186 242 RLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLS 281
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-278 |
3.42e-118 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 340.60 E-value: 3.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 5 IIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELID 84
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 85 TLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAVV 164
Cdd:PRK14184 83 ELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 165 IGASNIVGRPMSMELLLAG----CTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGkV 240
Cdd:PRK14184 163 VGRSNIVGKPLALMLGAPGkfanATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG-L 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 556490405 241 VGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQA 278
Cdd:PRK14184 242 VGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-278 |
1.67e-113 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 328.71 E-value: 1.67e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 4 KIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELI 83
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 84 DTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14183 82 AMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVGD 243
Cdd:PRK14183 162 VVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDGRLVGD 241
|
250 260 270
....*....|....*....|....*....|....*
gi 556490405 244 VVYEDAAARASYITPVPGGVGPMTVATLIQNTLQA 278
Cdd:PRK14183 242 VDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKA 276
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-279 |
5.76e-113 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 327.09 E-value: 5.76e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 3 AKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLEL 82
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 83 IDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNA 162
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 163 VVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVG 242
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENGKLIG 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 556490405 243 DVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQAC 279
Cdd:PRK14179 242 DVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAA 278
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-280 |
1.88e-107 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 313.12 E-value: 1.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 5 IIDGKTIAQQVRSEVAEKVKARKVAGKRaPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELID 84
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSKGIE-SCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 85 TLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRL-CQRAPRLRPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14166 82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLnLGLESGFLPCTPLGVMKLLKAYEIDLEGKDAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVGD 243
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVGD 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 556490405 244 VVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACE 280
Cdd:PRK14166 242 VDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-281 |
8.53e-107 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 311.74 E-value: 8.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 4 KIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELI 83
Cdd:PRK14176 9 RIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 84 DTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14176 89 DSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRlESGKVVGD 243
Cdd:PRK14176 169 IVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITK-EEDKVYGD 247
|
250 260 270
....*....|....*....|....*....|....*...
gi 556490405 244 VVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEE 281
Cdd:PRK14176 248 VDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-280 |
1.11e-102 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 301.16 E-value: 1.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGkRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14193 1 MTAIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK14193 80 AVIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVT--HRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESG 238
Cdd:PRK14193 160 HVVVIGRGVTVGRPIGLLLTRRSENATVTlcHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 556490405 239 KVVGDvVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACE 280
Cdd:PRK14193 240 KLVGD-VHPDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAE 280
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-285 |
4.13e-101 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 297.50 E-value: 4.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 5 IIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELID 84
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 85 TLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRL-------CqraprLRPCTPRGIVTLLERYNIDT 157
Cdd:PRK14174 83 DLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLvmghldkC-----FVSCTPYGILELLGRYNIET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 158 YGLNAVVIGASNIVGRPMS----MELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGIN 233
Cdd:PRK14174 158 KGKHCVVVGRSNIVGKPMAnlmlQKLKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGIN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 556490405 234 RLE-----SG-KVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYHDV 285
Cdd:PRK14174 238 RIEdpstkSGyRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERVNNL 295
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-277 |
5.82e-99 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 291.54 E-value: 5.82e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 5 IIDGKTIAQQVRSEVAEKVKARKVAGKrAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELID 84
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAARGV-QTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 85 TLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRL-RPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14182 82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVGD 243
Cdd:PRK14182 162 VVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADGKLVGD 241
|
250 260 270
....*....|....*....|....*....|....
gi 556490405 244 VVYEDAAARASYITPVPGGVGPMTVATLIQNTLQ 277
Cdd:PRK14182 242 VEFAAAAARASAITPVPGGVGPMTRAMLLVNTVE 275
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-283 |
3.47e-98 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 290.21 E-value: 3.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGKRaPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14194 2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK14194 81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESG-- 238
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDDDgr 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 556490405 239 -KVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYH 283
Cdd:PRK14194 241 sRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQA 286
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-286 |
4.14e-98 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 292.29 E-value: 4.14e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 2 AAKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLE 81
Cdd:PLN02616 72 GAKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 82 LIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRA--PRLRPCTPRGIVTLLERYNIDTYG 159
Cdd:PLN02616 152 FISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGrePLFVPCTPKGCIELLHRYNVEIKG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 160 LNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESG- 238
Cdd:PLN02616 232 KRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDAs 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 556490405 239 -----KVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYHDVE 286
Cdd:PLN02616 312 sprgyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRIHNFQ 364
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-286 |
2.25e-97 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 288.21 E-value: 2.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 3 AKIIDGKTIAQQVRSEVAEKVKARKVAGKRaPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLEL 82
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDAGVT-PGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 83 IDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNA 162
Cdd:PRK14167 81 IDELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 163 VVIGASNIVGRPMSMELLLAG----CTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESG 238
Cdd:PRK14167 161 VVVGRSDIVGKPMANLLIQKAdggnATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDAD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 556490405 239 -----KVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYHDVE 286
Cdd:PRK14167 241 tekgyELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASLQEGVD 293
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-281 |
4.96e-97 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 286.93 E-value: 4.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 5 IIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELID 84
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 85 TLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPR-LRPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14180 83 QLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKcLESCTPKGIMTMLREYGIKTEGAYAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLEsGKVVGD 243
Cdd:PRK14180 163 VVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVD-GKIVGD 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 556490405 244 VVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEE 281
Cdd:PRK14180 242 VDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQE 279
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
3-276 |
1.24e-96 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 286.40 E-value: 1.24e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 3 AKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLEL 82
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 83 IDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQ--RAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PLN02516 89 VHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMkgREPLFLPCTPKGCLELLSRSGIPIKGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRL----- 235
Cdd:PLN02516 169 KAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVsdpsk 248
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 556490405 236 ESG-KVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTL 276
Cdd:PLN02516 249 KSGyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTV 290
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-278 |
5.25e-96 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 284.50 E-value: 5.25e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGkRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14175 1 MVAKILDGKQIAKDYRQGLQDQVEALKEKG-FTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK14175 80 NELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKV 240
Cdd:PRK14175 160 NAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGKL 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 556490405 241 VGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQA 278
Cdd:PRK14175 240 KGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLA 277
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
124-283 |
8.52e-95 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 276.27 E-value: 8.52e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 124 HPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENA 203
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITREA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 204 DLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYH 283
Cdd:pfam02882 81 DIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKRQL 160
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-280 |
1.47e-94 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 280.56 E-value: 1.47e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVaekvKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14173 1 MAARELSGPPAAEAVYAEL----RARLAKLPFVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK14173 77 ELIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRL--ESG 238
Cdd:PRK14173 157 EVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVggNGG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 556490405 239 K--VVGDVVYEdAAARASYITPVPGGVGPMTVATLIQNTLQACE 280
Cdd:PRK14173 237 RdiLTGDVHPE-VAEVAGALTPVPGGVGPMTVAMLMANTVIAAL 279
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-281 |
4.44e-94 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 279.14 E-value: 4.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 3 AKIIDGKTIAQQVRSEVAEKVKARKVAGKrAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLEL 82
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQDV-TPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 83 IDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNA 162
Cdd:PRK14169 80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 163 VVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVG 242
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGKLLG 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 556490405 243 DVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEE 281
Cdd:PRK14169 240 DVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-278 |
1.06e-93 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 278.64 E-value: 1.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 4 KIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELI 83
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 84 DTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14185 82 RELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAG----CTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESG- 238
Cdd:PRK14185 162 VLGRSNIVGKPMAQLMMQKAypgdCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDAt 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 556490405 239 -----KVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQA 278
Cdd:PRK14185 242 rksgfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLA 286
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-278 |
1.40e-93 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 277.88 E-value: 1.40e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 5 IIDGKTIAQQvRSEVaekVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELID 84
Cdd:PRK14178 2 ILDGKAVSEK-RLEL---LKEEIIESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 85 TLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAVV 164
Cdd:PRK14178 78 RLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 165 IGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLEsGKVVGDV 244
Cdd:PRK14178 158 VGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVN-GKLCGDV 236
|
250 260 270
....*....|....*....|....*....|....
gi 556490405 245 VYEDAAARASYITPVPGGVGPMTVATLIQNTLQA 278
Cdd:PRK14178 237 DFDAVKEIAGAITPVPGGVGPMTIATLMENTFDA 270
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-282 |
1.46e-93 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 278.01 E-value: 1.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14177 1 MSPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK14177 81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINrleSGKv 240
Cdd:PRK14177 161 NAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN---PGN- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 556490405 241 VGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEY 282
Cdd:PRK14177 237 VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEH 278
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-281 |
3.65e-93 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 276.66 E-value: 3.65e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 4 KIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELI 83
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 84 DTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14172 83 EELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLEsGKVVGD 243
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVN-GKITGD 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 556490405 244 VVYEDAAARASYITPVPGGVGPMTVATLIQNtlqACEE 281
Cdd:PRK14172 242 VNFDKVIDKASYITPVPGGVGSLTTTLLIKN---VCEA 276
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
3-284 |
2.76e-91 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 274.53 E-value: 2.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 3 AKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLEL 82
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 83 IDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRA--PRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PLN02897 136 LRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGrePLFVSCTPKGCVELLIRSGVEIAGK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESG-- 238
Cdd:PLN02897 216 NAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSsc 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 556490405 239 ----KVVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYHD 284
Cdd:PLN02897 296 efgyRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRIFL 345
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
116-280 |
9.59e-90 |
|
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: 264.03 E-value: 9.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 116 PDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKN 195
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 196 LRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLE---SGKVVGDVVYEDAAARASYITPVPGGVGPMTVATLI 272
Cdd:cd01080 81 LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPdksGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAMLM 160
|
....*...
gi 556490405 273 QNTLQACE 280
Cdd:cd01080 161 KNTVEAAK 168
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-287 |
1.64e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 268.23 E-value: 1.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 5 IIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELID 84
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 85 TLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLC--QRAPRLRPCTPRGIVTLLERYNIDTYGLNA 162
Cdd:PRK14187 84 ELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFtgQKKNCLIPCTPKGCLYLIKTITRNLSGSDA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 163 VVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESG---K 239
Cdd:PRK14187 164 VVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGgvkK 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 556490405 240 VVGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEEYHDVED 287
Cdd:PRK14187 244 FVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAACNQKGIDD 291
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-281 |
2.71e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 267.10 E-value: 2.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14192 1 MMALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGL 160
Cdd:PRK14192 81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 161 NAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKv 240
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGGG- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 556490405 241 VGDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACEE 281
Cdd:PRK14192 240 VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEK 280
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-278 |
1.04e-87 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 263.36 E-value: 1.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 5 IIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELID 84
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 85 TLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPR-LRPCTPRGIVTLLERYNIDTYGLNAV 163
Cdd:PRK14171 84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQgFIPCTALGCLAVIKKYEPNLTGKNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 164 VIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVGD 243
Cdd:PRK14171 164 IIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGNKIIGD 243
|
250 260 270
....*....|....*....|....*....|....*
gi 556490405 244 VVYEDAAARASYITPVPGGVGPMTVATLIQNTLQA 278
Cdd:PRK14171 244 VDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-278 |
5.60e-87 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 261.73 E-value: 5.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 1 MAAKIIDGKTIAQQVRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELL 80
Cdd:PRK14168 1 MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 81 ELIDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLC--QRAPRLRPCTPRGIVTLLERYNIDTY 158
Cdd:PRK14168 81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMigGDEVKFLPCTPAGIQEMLVRSGVETS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 159 GLNAVVIGASNIVGRPMSMELLLAG----CTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINR 234
Cdd:PRK14168 161 GAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 556490405 235 L----ESGKVV--GDVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQA 278
Cdd:PRK14168 241 VgtneSTGKAIlsGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKS 290
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-280 |
7.60e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 253.46 E-value: 7.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 3 AKIIDGKTIAQQVRSEVAEKVKARKVAGKRaPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLEL 82
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKEGKK-PGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 83 IDTLNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTYGLNA 162
Cdd:PRK14170 81 VEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 163 VVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGKVVG 242
Cdd:PRK14170 161 VVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCG 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 556490405 243 DVVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACE 280
Cdd:PRK14170 241 DVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAK 278
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
15-275 |
9.11e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 237.84 E-value: 9.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 15 VRSEVAEKVKARKVAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELIDTLNADKEIDG 94
Cdd:PRK14181 8 AAEHILATIKENISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 95 ILVQLPLPAGIDNVKVLERIAPDKDVDGFHPYNVGR-LCQRAPRLRPCTPRGIVTLLERYNIDTYGLNAVVIGASNIVGR 173
Cdd:PRK14181 88 ILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKlLLGETDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 174 PMSMELLL----AGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGEWIKEGAIVVDVGINRLESGK-----VVGDV 244
Cdd:PRK14181 168 PLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAANpkgyiLVGDV 247
|
250 260 270
....*....|....*....|....*....|.
gi 556490405 245 VYEDAAARASYITPVPGGVGPMTVATLIQNT 275
Cdd:PRK14181 248 DFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
6-121 |
4.57e-63 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 194.16 E-value: 4.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 6 IDGKTIAQQVRSEVAEKVKARKvAGKRAPGLAVVLVGSNPASQIYVGSKRKACEEVGFVSRSYDLPETTSEAELLELIDT 85
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALK-AGGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 556490405 86 LNADKEIDGILVQLPLPAGIDNVKVLERIAPDKDVD 121
Cdd:pfam00763 80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
140-280 |
3.65e-31 |
|
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: 113.37 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 140 PCTPRGIV-------TLLERYNIDTYGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGK 212
Cdd:cd05212 2 PCTPLFVSpvakavkELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSPK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556490405 213 PGFIPGEWIKEGAIVVDVGINRLesgkvvgdvVYEDAAARASYITPVPGGVGPMTVATLIQNTLQACE 280
Cdd:cd05212 82 PEKVPTEWIKPGATVINCSPTKL---------SGDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
116-283 |
2.62e-12 |
|
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: 64.37 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 116 PDKDVDGFHPYNVGRLCQ---------RAPRLRPCTPRGIVTLLE---------RYNIDTYGLNAVVIGASNIVGRPMSM 177
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYHnirfldpenRKKSILPCTPLAIVKILEflgiynkilPYGNRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 178 elLLAGCTTTV-------THRFTKN-----LRHHVEN-----------ADLLIVAVGKPGF-IPGEWIKEGAIVVDV-GI 232
Cdd:cd01079 81 --LLANDGARVysvdingIQVFTRGesirhEKHHVTDeeamtldclsqSDVVITGVPSPNYkVPTELLKDGAICINFaSI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556490405 233 NRLEsgkvvgdvvyEDAAARASYITPVpggVGPMTVATLIQNTLQACEEYH 283
Cdd:cd01079 159 KNFE----------PSVKEKASIYVPS---IGKVTIAMLLRNLLRLYHNQH 196
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
170-229 |
2.91e-03 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 38.49 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556490405 170 IVGRPMSMELLLAGCTTTVTHRFTKNLRHHV--------------ENADLLI-----------VAVGKPGFIPGewIKEG 224
Cdd:PRK11559 12 IMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIaagaetastakavaEQCDVIItmlpnsphvkeVALGENGIIEG--AKPG 89
|
....*
gi 556490405 225 AIVVD 229
Cdd:PRK11559 90 TVVID 94
|
|
|