NCBI Conserved Domain Search

Conserved domains on [gi|1828258322|ref|WP_167535177|]

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bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase [Mycolicibacterium monacense]

Protein Classification

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase( domain architecture ID 11487154)

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase reversibly catalyzes oxidation of 5,10-methylene-THF to 5,10-methenyl-THF and hydrolysis of 5,10-methenyl-THF to 10-formyl-THF

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PRK14193

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-284

0e+00

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 585.44 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14193    1 MTAIILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14193   81 VIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRRSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:PRK14193  161 VVVIGRGVTVGRPIGLLLTRRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDGK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1828258322 241 LVGDVAPDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALAR 284
Cdd:PRK14193  241 LVGDVHPDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284

Name

Accession

Description

Interval

E-value

PRK14193

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-284

0e+00

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 585.44 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14193    1 MTAIILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14193   81 VIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRRSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:PRK14193  161 VVVIGRGVTVGRPIGLLLTRRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDGK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1828258322 241 LVGDVAPDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALAR 284
Cdd:PRK14193  241 LVGDVHPDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284

FolD

COG0190

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...

1-283

1.51e-172

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 477.97 E-value: 1.51e-172

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:COG0190     1 MMAQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:COG0190    81 LIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:COG0190   161 AVVVGRSNIVGKPLALLLLRR--NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1828258322 241 LVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALA 283
Cdd:COG0190   239 LVGDVDfESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282

THF_DHG_CYH_C

pfam02882

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;

123-280

1.15e-83

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;

Pssm-ID: 427036 Cd Length: 160 Bit Score: 248.15 E-value: 1.15e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 123 HPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTR 202
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--NATVTVCHSKTKDLAEITR 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828258322 203 EADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKLVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:pfam02882  79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDfENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAK 157

NAD_bind_m-THF_DH_Cyclohyd

cd01080

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...

115-280

1.29e-77

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: 233.22 E-value: 1.29e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 115 PGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVIGRGVTVGRPLGLLLTRRseNATVTLCHTAT 194
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNR--NATVTVCHSKT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 195 RHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRD---DNGKLVGDVAPDVW-EVAGHVSPNPGGVGPLTRAF 270
Cdd:cd01080    79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVpdkSGGKLVGDVDFESAkEKASAITPVPGGVGPMTVAM 158

                         170
                  ....*....|
gi 1828258322 271 LLTNVVERAE 280
Cdd:cd01080   159 LMKNTVEAAK 168

AlaDh_PNT_C

smart01002

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...

158-231

1.60e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.

Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 40.95 E-value: 1.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  158 GAHVVVIGRGVTVGRPLGLLLtrrseNATVTLCHTATRHLPQFTREADIIVAAAGV-----PHMVTAEMV---RPGAAVI 229
Cdd:smart01002  43 GAEVTVLDVRPARLRQLESLL-----GARFTTLYSQAELLEEAVKEADLVIGAVLIpgakaPKLVTREMVksmKPGSVIV 117


                   ..
gi 1828258322  230 DV 231
Cdd:smart01002 118 DV 119

Name

Accession

Description

Interval

E-value

PRK14193

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-284

0e+00

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 585.44 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14193    1 MTAIILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14193   81 VIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRRSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:PRK14193  161 VVVIGRGVTVGRPIGLLLTRRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAGDGK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1828258322 241 LVGDVAPDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALAR 284
Cdd:PRK14193  241 LVGDVHPDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284

FolD

COG0190

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...

1-283

1.51e-172

5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 477.97 E-value: 1.51e-172

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:COG0190     1 MMAQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:COG0190    81 LIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:COG0190   161 AVVVGRSNIVGKPLALLLLRR--NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVEDGK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1828258322 241 LVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALA 283
Cdd:COG0190   239 LVGDVDfESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282

PRK14190

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-280

1.86e-130

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 371.65 E-value: 1.86e-130

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14190    1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14190   81 LIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRrsENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:PRK14190  161 VVVVGRSNIVGKPVGQLLLN--ENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLENGK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1828258322 241 LVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:PRK14190  239 LCGDVDFDnVKEKASYITPVPGGVGPMTITMLMHNTVELAK 279

PRK14189

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

1-284

5.20e-114

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 329.73 E-value: 5.20e-114

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14189    1 MTAQLIDGNALSKQLRAEAAQRAAALTARGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14189   81 RIDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:PRK14189  161 AVVIGRSNIVGKPMAMLLLQA--GATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDAGK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1828258322 241 LVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALAR 284
Cdd:PRK14189  239 LCGDVDFAgVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAA 283

PRK14186

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-278

7.94e-109

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 317.01 E-value: 7.94e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   3 AITLDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDAT 81
Cdd:PRK14186    2 ALILDGKALAAEIEQRLQAQIESNLPKaGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  82 IDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHV 161
Cdd:PRK14186   82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 162 VVIGRGVTVGRPLGLLLtrRSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSR----DD 237
Cdd:PRK14186  162 VVVGRSILVGKPLALML--LAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRlpssDG 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1828258322 238 NGKLVGDV-APDVWEVAGHVSPNPGGVGPLTRAFLLTNVVER 278
Cdd:PRK14186  240 KTRLCGDVdFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLS 281

PRK10792

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-282

1.26e-106

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 311.08 E-value: 1.26e-106

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQG-RTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELD 79
Cdd:PRK10792    1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGlRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  80 ATIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGA 159
Cdd:PRK10792   81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 160 HVVVIGRGVTVGRP--LGLLLTRrsenATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDD 237
Cdd:PRK10792  161 NAVVVGASNIVGRPmsLELLLAG----CTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLE 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1828258322 238 NGKLVGDVAPDV-WEVAGHVSPNPGGVGPLTRAFLLTNVVERAEAL 282
Cdd:PRK10792  237 DGKLVGDVEFETaAERASWITPVPGGVGPMTVATLLENTLQACEEY 282

PRK14184

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-277

1.25e-101

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 298.61 E-value: 1.25e-101

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDE 84
Cdd:PRK14184    4 LDGKATAATIREELKTEVAALTARhGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  85 LNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14184   84 LNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVVV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTRRSE--NATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGkLV 242
Cdd:PRK14184  164 GRSNIVGKPLALMLGAPGKfaNATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG-LV 242

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1828258322 243 GDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVE 277
Cdd:PRK14184  243 GDCDFEgLSDVASAITPVPGGVGPMTIAQLLVNTVQ 278

PRK14191

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-284

3.10e-99

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 292.44 E-value: 3.10e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAALT-EQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDE 84
Cdd:PRK14191    4 LDGKALSYKIEKDLKNKIQILTaQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIKD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  85 LNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14191   84 LNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVVII 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKLVGD 244
Cdd:PRK14191  164 GASNIVGKPLAMLML--NAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDGRLVGD 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1828258322 245 VAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALAR 284
Cdd:PRK14191  242 VDFEnVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQR 282

PRK14188

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-283

8.04e-97

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 286.47 E-value: 8.04e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAAL-TEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDE 84
Cdd:PRK14188    5 IDGKAFAADVRATVAAEVARLkAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALIAR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  85 LNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14188   85 LNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLNAVVI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTRrsENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSR-------DD 237
Cdd:PRK14188  165 GRSNLVGKPMAQLLLA--ANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRipapekgEG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1828258322 238 NGKLVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALA 283
Cdd:PRK14188  243 KTRLVGDVAFAeAAEVAGAITPVPGGVGPMTIACLLANTLTAACRAA 289

PRK14179

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

3-279

2.83e-96

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 284.72 E-value: 2.83e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   3 AITLDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDAT 81
Cdd:PRK14179    2 TEIIDGKALAQKMQAELAEKVAKLKEEkGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  82 IDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHV 161
Cdd:PRK14179   82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 162 VVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKL 241
Cdd:PRK14179  162 VVIGRSNIVGKPMAQLLLDK--NATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRDENGKL 239

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1828258322 242 VGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERA 279
Cdd:PRK14179  240 IGDVDFDeVAEVASYITPVPGGVGPMTITMLMEQTYQAA 278

PRK14176

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-280

6.02e-94

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 279.00 E-value: 6.02e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAAL-TEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDE 84
Cdd:PRK14176   11 IDGKALAKKIEAEVRSGVERLkSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  85 LNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14176   91 LNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVIV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDnGKLVGD 244
Cdd:PRK14176  171 GHSNVVGKPMAAMLLNR--NATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEE-DKVYGD 247

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1828258322 245 VAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:PRK14176  248 VDFEnVIKKASLITPVPGGVGPLTIAMLMKHVLMCAE 284

PRK14167

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-285

1.16e-93

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 278.58 E-value: 1.16e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDEL 85
Cdd:PRK14167    5 IDGNAVAAQIRDDLTDAIETLEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDEL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  86 NANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVIG 165
Cdd:PRK14167   85 NADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVVVG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 166 RGVTVGRPLGLLLTRRSE--NATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSR--DDNGK- 240
Cdd:PRK14167  165 RSDIVGKPMANLLIQKADggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRvdADTEKg 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1828258322 241 --LVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVeRAEALARG 285
Cdd:PRK14167  245 yeLVGDVEFEsAKEKASAITPVPGGVGPMTRAMLLYNTV-KAASLQEG 291

PRK14173

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-280

3.72e-92

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 274.40 E-value: 3.72e-92

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEqgrTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14173    1 MAARELSGPPAAEAVYAELRARLAKLPF---VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14173   78 LIARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRrsENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSR--DDN 238
Cdd:PRK14173  158 VVVVGRSNIVGKPLAALLLR--EDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRvgGNG 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1828258322 239 GK--LVGDVAPDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:PRK14173  236 GRdiLTGDVHPEVAEVAGALTPVPGGVGPMTVAMLMANTVIAAL 279

PRK14174

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

4-282

3.52e-90

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 269.77 E-value: 3.52e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   4 ITLDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATI 82
Cdd:PRK14174    2 LIIDGKKVSLDLKNELKTRVEAYRAKtGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  83 DELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLN--EPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14174   82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGhlDKCFVSCTPYGILELLGRYNIETKGKH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTR--RSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDN 238
Cdd:PRK14174  162 CVVVGRSNIVGKPMANLMLQklKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIED 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1828258322 239 G------KLVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVV---ERAEAL 282
Cdd:PRK14174  242 PstksgyRLVGDVDYEgVSAKASAITPVPGGVGPMTIAMLLKNTLqsfERVNNL 295

PRK14169

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-285

1.07e-89

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 267.97 E-value: 1.07e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   3 AITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATI 82
Cdd:PRK14169    1 ATRLDGRAVSKKILADLKQTVAKLAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  83 DELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVV 162
Cdd:PRK14169   81 AELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 163 VIGRGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKLV 242
Cdd:PRK14169  161 IVGRSNIVGRPLAGLMV--NHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGKLL 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1828258322 243 GDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALARG 285
Cdd:PRK14169  239 GDVDEAaVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRANG 282

PRK14183

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-283

1.78e-87

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 262.46 E-value: 1.78e-87

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAAL-TEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDE 84
Cdd:PRK14183    4 LDGKALSDKIKENVKKEVDELkLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIAM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  85 LNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14183   84 MNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCVV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKLVGD 244
Cdd:PRK14183  164 GASNIVGKPMAALLLNA--NATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDGRLVGD 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1828258322 245 VA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALA 283
Cdd:PRK14183  242 VDfENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281

PRK14166

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-280

2.12e-86

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 259.57 E-value: 2.12e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDEL 85
Cdd:PRK14166    4 LDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINTL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  86 NANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLN-EPAPLPCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14166   84 NHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAVII 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKLVGD 244
Cdd:PRK14166  164 GASNIVGRPMATMLL--NAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVGD 241

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1828258322 245 VA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:PRK14166  242 VDfEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278

PRK14178

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-279

2.54e-86

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 259.39 E-value: 2.54e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVaalTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDEL 85
Cdd:PRK14178    3 LDGKAVSEKRLELLKEEI---IESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  86 NANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVIG 165
Cdd:PRK14178   80 NEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 166 RGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRdDNGKLVGDV 245
Cdd:PRK14178  160 RSIDVGRPMAALLL--NADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQ-VNGKLCGDV 236

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1828258322 246 APD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERA 279
Cdd:PRK14178  237 DFDaVKEIAGAITPVPGGVGPMTIATLMENTFDAA 271

PRK14192

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-284

1.61e-85

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 257.47 E-value: 1.61e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELD 79
Cdd:PRK14192    1 MMALVLDGKALAKQIEEELSVRVEALKAKtGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  80 ATIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGA 159
Cdd:PRK14192   81 AKIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 160 HVVVIGRGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNG 239
Cdd:PRK14192  161 HAVVVGRSAILGKPMAMMLL--NANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGG 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1828258322 240 KlVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALAR 284
Cdd:PRK14192  239 G-VGDIELQgIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283

PLN02516

methylenetetrahydrofolate dehydrogenase (NADP+)

3-281

1.17e-84

methylenetetrahydrofolate dehydrogenase (NADP+)

Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 255.97 E-value: 1.17e-84

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   3 AITLDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDAT 81
Cdd:PLN02516    9 AQIIDGKAIAKAIRSEIAEEVAQLSEKhGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  82 IDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLN--EPAPLPCTPRGIVHLLRRYEVEIAGA 159
Cdd:PLN02516   89 VHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGK 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 160 HVVVIGRGVTVGRPLGLLLTRrsENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGV------ 233
Cdd:PLN02516  169 KAVVVGRSNIVGLPVSLLLLK--ADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTnavsdp 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1828258322 234 SRDDNGKLVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEA 281
Cdd:PLN02516  247 SKKSGYRLVGDVDfAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295

THF_DHG_CYH_C

pfam02882

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;

123-280

1.15e-83

Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;

Pssm-ID: 427036 Cd Length: 160 Bit Score: 248.15 E-value: 1.15e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 123 HPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTR 202
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--NATVTVCHSKTKDLAEITR 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828258322 203 EADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKLVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:pfam02882  79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGDVDfENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAK 157

PRK14172

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

1-277

8.87e-82

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 247.77 E-value: 8.87e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAItLDGKATRDEIFVDLKERVAALTEQG-RTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELD 79
Cdd:PRK14172    1 MGQI-INGKEVALKIKEEIKNFVEERKENGlSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  80 ATIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGA 159
Cdd:PRK14172   80 NEIEELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 160 HVVVIGRGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSrDDNG 239
Cdd:PRK14172  160 EVVVIGRSNIVGKPVAQLLL--NENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTS-SVNG 236

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1828258322 240 KLVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVE 277
Cdd:PRK14172  237 KITGDVNFDkVIDKASYITPVPGGVGSLTTTLLIKNVCE 275

PLN02616

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

2-280

1.00e-81

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 250.69 E-value: 1.00e-81

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   2 GAITLDGKAT----RDEIFVDLKERVAALteqGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAE 77
Cdd:PLN02616   72 GAKVIDGKAVakkiRDEITIEVSRMKESI---GVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  78 LDATIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVL--NEPAPLPCTPRGIVHLLRRYEVE 155
Cdd:PLN02616  149 VLKFISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMrgREPLFVPCTPKGCIELLHRYNVE 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 156 IAGAHVVVIGRGVTVGRPLGLLLTRrsENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVS- 234
Cdd:PLN02616  229 IKGKRAVVIGRSNIVGMPAALLLQR--EDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINp 306

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1828258322 235 -RDDNG----KLVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:PLN02616  307 vEDASSprgyRLVGDVCyEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAK 358

PRK14175

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-285

1.69e-80

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 244.83 E-value: 1.69e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14175    1 MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14175   81 ELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:PRK14175  161 AVVIGRSHIVGQPVSKLLLQK--NASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1828258322 241 LVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVeRAEALARG 285
Cdd:PRK14175  239 LKGDVDYDaVKEIAGAITPVPGGVGPLTITMVLNNTL-LAEKMRRG 283

PRK14171

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-277

1.20e-79

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 242.56 E-value: 1.20e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDE 84
Cdd:PRK14171    5 IDGKALANEILADLKLEIQELKSQtNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  85 LNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLN-EPAPLPCTPRGIVHLLRRYEVEIAGAHVVV 163
Cdd:PRK14171   85 LNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGiSQGFIPCTALGCLAVIKKYEPNLTGKNVVI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 164 IGRGVTVGRPLGLLLTRrsENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKLVG 243
Cdd:PRK14171  165 IGRSNIVGKPLSALLLK--ENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGNKIIG 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1828258322 244 DVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVE 277
Cdd:PRK14171  243 DVDfENVKSKVKYITPVPGGIGPMTIAFLLKNTVK 277

PRK14185

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-274

1.74e-79

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 242.43 E-value: 1.74e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAALTEQG-RTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDE 84
Cdd:PRK14185    4 IDGKAISAQIKQEIAAEVAEIVAKGgKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVRE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  85 LNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14185   84 LNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTRRSE--NATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSR------D 236
Cdd:PRK14185  164 GRSNIVGKPMAQLMMQKAYpgDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRvpdatrK 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1828258322 237 DNGKLVGDVAPDvwEVA---GHVSPNPGGVGPLTRAFLLTN 274
Cdd:PRK14185  244 SGFKLTGDVKFD--EVApkcSYITPVPGGVGPMTIVSLMKN 282

PRK14168

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-281

4.51e-79

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 241.32 E-value: 4.51e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELD 79
Cdd:PRK14168    1 MSAKIIKGTEIREEILEEIRGEVAELKEKyGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  80 ATIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVL--NEPAPLPCTPRGIVHLLRRYEVEIA 157
Cdd:PRK14168   81 ALIDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 158 GAHVVVIGRGVTVGRPLGLLLTRR--SENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSR 235
Cdd:PRK14168  161 GAEVVVVGRSNIVGKPIANMMTQKgpGANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1828258322 236 ----DDNGK--LVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEA 281
Cdd:PRK14168  241 vgtnESTGKaiLSGDVDFDaVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAKF 293

PRK14182

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

6-284

7.55e-78

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 238.00 E-value: 7.55e-78

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDEL 85
Cdd:PRK14182    4 IDGKQIAAKVKGEVATEVRALAARGVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  86 NANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPA-PLPCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14182   84 NADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGvPRPCTPAGVMRMLDEARVDPKGKRALVV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGKLVGD 244
Cdd:PRK14182  164 GRSNIVGKPMAMMLLER--HATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADGKLVGD 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1828258322 245 VA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALAR 284
Cdd:PRK14182  242 VEfAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTAR 282

NAD_bind_m-THF_DH_Cyclohyd

cd01080

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...

115-280

1.29e-77

Pssm-ID: 133448 Cd Length: 168 Bit Score: 233.22 E-value: 1.29e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 115 PGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAHVVVIGRGVTVGRPLGLLLTRRseNATVTLCHTAT 194
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNR--NATVTVCHSKT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 195 RHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRD---DNGKLVGDVAPDVW-EVAGHVSPNPGGVGPLTRAF 270
Cdd:cd01080    79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVpdkSGGKLVGDVDFESAkEKASAITPVPGGVGPMTVAM 158

                         170
                  ....*....|
gi 1828258322 271 LLTNVVERAE 280
Cdd:cd01080   159 LMKNTVEAAK 168

PRK14194

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-281

1.32e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 235.12 E-value: 1.32e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14194    2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14194   82 LIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTRrsENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSR-DDNG 239
Cdd:PRK14194  162 AVVIGRSNIVGKPMAALLLQ--AHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRiDDDG 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1828258322 240 K--LVGDVAPD-VWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEA 281
Cdd:PRK14194  240 RsrLVGDVDFDsALPVVSAITPVPGGVGPMTIAFLMKNTVTAARL 284

PLN02897

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

3-280

4.14e-76

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 235.62 E-value: 4.14e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   3 AITLDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDAT 81
Cdd:PLN02897   56 TVVIDGNVIAEEIRTKIASEVRKMKKAvGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  82 IDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVL--NEPAPLPCTPRGIVHLLRRYEVEIAGA 159
Cdd:PLN02897  136 LRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMrgREPLFVSCTPKGCVELLIRSGVEIAGK 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 160 HVVVIGRGVTVGRPLGLLLTRrsENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGV------ 233
Cdd:PLN02897  216 NAVVIGRSNIVGLPMSLLLQR--HDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTtpveds 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1828258322 234 SRDDNGKLVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:PLN02897  294 SCEFGYRLVGDVCyEEALGVASAITPVPGGVGPMTITMLLCNTLDAAK 341

PRK14170

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-282

7.59e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 232.66 E-value: 7.59e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAItLDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDA 80
Cdd:PRK14170    1 MGEI-IDGKKLAKEIQEKVTREVAELVKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  81 TIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGAH 160
Cdd:PRK14170   80 VVEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 161 VVVIGRGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDDNGK 240
Cdd:PRK14170  160 AVVIGRSNIVGKPVAQLLL--NENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNK 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1828258322 241 LVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEAL 282
Cdd:PRK14170  238 LCGDVDfDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRI 280

PRK14181

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

6-277

1.96e-74

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 229.36 E-value: 1.96e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAAlteQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDEL 85
Cdd:PRK14181    3 LKGAPAAEHILATIKENISA---SSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  86 NANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPL-PCTPRGIVHLLRRYEVEIAGAHVVVI 164
Cdd:PRK14181   80 NNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETDGFiPCTPAGIIELLKYYEIPLHGRHVAIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 165 GRGVTVGRPLGLLLTRR--SENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSR--DDNGK 240
Cdd:PRK14181  160 GRSNIVGKPLAALLMQKhpDTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRvpAANPK 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1828258322 241 ---LVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVE 277
Cdd:PRK14181  240 gyiLVGDVDfNNVVPKCRAITPVPGGVGPMTVAMLMRNTWE 280

PRK14187

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

3-276

1.61e-73

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 227.02 E-value: 1.61e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   3 AITLDGKATRDEIFVDLKERVAALTEQ-GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDAT 81
Cdd:PRK14187    2 TNIIDGKKIANDITEILATCIDDLKRQhNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  82 IDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAP--LPCTPRGIVHLLRRYEVEIAGA 159
Cdd:PRK14187   82 INELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNclIPCTPKGCLYLIKTITRNLSGS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 160 HVVVIGRGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVG---VSRD 236
Cdd:PRK14187  162 DAVVIGRSNIVGKPMACLLL--GENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGinsIEEG 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1828258322 237 DNGKLVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVV 276
Cdd:PRK14187  240 GVKKFVGDVDfAEVKKKASAITPVPGGVGPMTIAFLMVNTV 280

PRK14177

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

1-272

2.81e-70

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 218.69 E-value: 2.81e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   1 MGAITLDGKATRDEIFVDLKERVA-ALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELD 79
Cdd:PRK14177    1 MSPILLDGKKLSEKIRNEIRETIEeRKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  80 ATIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYEVEIAGA 159
Cdd:PRK14177   81 GVIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 160 HVVVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVsrddNG 239
Cdd:PRK14177  161 NAVVVGRSPILGKPMAMLLTEM--NATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGY----NP 234

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1828258322 240 KLVGDVapDVWEVAGHVS---PNPGGVGPLTRAFLL 272
Cdd:PRK14177  235 GNVGDI--EISKAKDKSSfytPVPGGVGPMTIAVLL 268

PRK14180

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...

4-284

6.49e-67

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional

Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 209.89 E-value: 6.49e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   4 ITLDGKAtrdeIFVDLKERVAALTEQ-----GRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAEL 78
Cdd:PRK14180    2 ILIDGKS----LSKDLKERLATQVQEykhhtAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  79 DATIDELNANPECTGYIVQLPLPKHLDENAALERIDPGKDADGLHPTNLGRLVLNEPAPL-PCTPRGIVHLLRRYEVEIA 157
Cdd:PRK14180   78 LELIDQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLeSCTPKGIMTMLREYGIKTE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 158 GAHVVVIGRGVTVGRPLGLLLTrrSENATVTLCHTATRHLPQFTREADIIVAAAGVPHMVTAEMVRPGAAVIDVGVSRDD 237
Cdd:PRK14180  158 GAYAVVVGASNVVGKPVSQLLL--NAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVD 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1828258322 238 nGKLVGDVA-PDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAEALAR 284
Cdd:PRK14180  236 -GKIVGDVDfAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELNR 282

THF_DHG_CYH

pfam00763

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;

6-120

2.06e-58

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;

Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 182.22 E-value: 2.06e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322   6 LDGKATRDEIFVDLKERVAALTEQGRTPGLGTVLVGDDPGSQAYVRGKHSDCAKVGINSIRRDLPADISQAELDATIDEL 85
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1828258322  86 NANPECTGYIVQLPLPKHLDENAALERIDPGKDAD 120
Cdd:pfam00763  81 NADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115

NAD_bind_m-THF_DH_Cyclohyd_like

cd05212

NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...

138-280

8.44e-23

NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.

Pssm-ID: 133451 Cd Length: 140 Bit Score: 91.41 E-value: 8.44e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 138 LPCTPRGIV-------HLLRRYEVEIAGAHVVVIGRGVTVGRPLGLLLTRRseNATVTLCHTATRHLPQFTREADIIVAA 210
Cdd:cd05212     1 GPCTPLFVSpvakavkELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRD--GATVYSCDWKTIQLQSKVHDADVVVVG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 211 AGVPHMVTAEMVRPGAAVIDVGVSrddngKLVGDvapDVWEVAGHVSPNPGGVGPLTRAFLLTNVVERAE 280
Cdd:cd05212    79 SPKPEKVPTEWIKPGATVINCSPT-----KLSGD---DVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140

NAD_bind_m-THF_DH

cd01079

NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ...

115-276

3.16e-09

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: 55.51 E-value: 3.16e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 115 PGKDADGLHPTNLGRLVLNE---------PAPLPCTPRGIVHLLRRYEV---------EIAGAHVVVIGRGVTVGRPLGL 176
Cdd:cd01079     1 PHKDVEGLSHKYIFNLYHNIrfldpenrkKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 177 LLTrrSENATV-------TLCHT---ATRHLP-QFTRE----------ADIIVAAAGVPHM-VTAEMVRPGAAVIDvgVS 234
Cdd:cd01079    81 LLA--NDGARVysvdingIQVFTrgeSIRHEKhHVTDEeamtldclsqSDVVITGVPSPNYkVPTELLKDGAICIN--FA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1828258322 235 RDDNgklvgdVAPDVWEVAGHVSPNpggVGPLTRAFLLTNVV 276
Cdd:cd01079   157 SIKN------FEPSVKEKASIYVPS---IGKVTIAMLLRNLL 189

AlaDh_PNT_C

smart01002

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...

158-231

1.60e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.

Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 40.95 E-value: 1.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322  158 GAHVVVIGRGVTVGRPLGLLLtrrseNATVTLCHTATRHLPQFTREADIIVAAAGV-----PHMVTAEMV---RPGAAVI 229
Cdd:smart01002  43 GAEVTVLDVRPARLRQLESLL-----GARFTTLYSQAELLEEAVKEADLVIGAVLIpgakaPKLVTREMVksmKPGSVIV 117


                   ..
gi 1828258322  230 DV 231
Cdd:smart01002 118 DV 119

COG5322

Predicted amino acid dehydrogenase [General function prediction only];

149-236

2.04e-04

Predicted amino acid dehydrogenase [General function prediction only];

Pssm-ID: 444114 [Multi-domain] Cd Length: 362 Bit Score: 42.13 E-value: 2.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 149 LRRYEVEIAGAHVVV------IGRGVT------------VGRPLGLLLT-----RRSENATVTLCHTATRHLpqftREAD 205
Cdd:COG5322   142 AERMGIDLKKATVAVvgatgsIGSVCArllarevkrltlVARNLERLEElaeeiLRNPGGKVTITTDIDEAL----READ 217

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1828258322 206 IIVAAAGVPHMV-TAEMVRPGAAVIDVGVSRD 236
Cdd:COG5322   218 IVVTVTSAVGAIiDPEDLKPGAVVCDVARPRD 249

NAD_bind_amino_acid_DH

cd05191

NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ...

140-232

7.47e-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: 7.47e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828258322 140 CTPRGIVHLLRR----YEVEIAGAHVVVIGRGvTVGRPLGLLLTRRSeNATVTLCHTatrhlpqftreaDIIVAAAGVPH 215
Cdd:cd05191     1 ATAAGAVALLKAagkvTNKSLKGKTVVVLGAG-EVGKGIAKLLADEG-GKKVVLCDR------------DILVTATPAGV 66

                          90       100
                  ....*....|....*....|
gi 1828258322 216 MVTAEMV---RPGAAVIDVG 232
Cdd:cd05191    67 PVLEEATakiNEGAVVIDLA 86

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01