NCBI Conserved Domain Search

Conserved domains on [gi|6678952|ref|NP_032664|]

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bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial precursor [Mus musculus]

Protein Classification

bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase( domain architecture ID 11415140)

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

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List of domain hits

Name

Accession

Description

Interval

E-value

FolD

COG0190

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

37-330

2.07e-155

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

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 437.52 E-value: 2.07e-155

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   37 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:COG0190   3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:COG0190  82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  197 VVAGRSKNVGMPIAMLLhtdgAHErpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:COG0190 162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678952  277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:COG0190 232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280

Name

Accession

Description

Interval

E-value

FolD

COG0190

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

37-330

2.07e-155

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

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 437.52 E-value: 2.07e-155

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   37 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:COG0190   3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:COG0190  82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  197 VVAGRSKNVGMPIAMLLhtdgAHErpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:COG0190 162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678952  277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:COG0190 232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280

PRK14190

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

37-330

5.56e-128

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

Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 367.80 E-value: 5.56e-128

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14190   3 AVIIDGKEVAKEKREQLKEEVVKLKEQG-IVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14190  82 IDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14190 162 VVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGV 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6678952   277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:PRK14190 232 NRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280

NAD_bind_m-THF_DH_Cyclohyd

cd01080

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

150-329

4.44e-87

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

Pssm-ID: 133448 Cd Length: 168 Bit Score: 259.41 E-value: 4.44e-87

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  150 PDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVT 229
Cdd:cd01080   1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  230 ISHRYTPKeqLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQDPvtAKPKLVGDVDFEGVKKKAGYITPVP 309
Cdd:cd01080  73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148

                       170       180
                ....*....|....*....|
gi 6678952  310 GGVGPMTVAMLMKNTIIAAK 329
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168

THF_DHG_CYH_C

pfam02882

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

158-330

5.71e-83

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

Pssm-ID: 427036 Cd Length: 160 Bit Score: 248.92 E-value: 5.71e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    158 HVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPk 237
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    238 eQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTV 317
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRVG-----NGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145

                         170
                  ....*....|...
gi 6678952    318 AMLMKNTIIAAKK 330
Cdd:pfam02882 146 AMLLQNTVEAAKR 158

AlaDh_PNT_C

smart01002

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

238-276

2.80e-03

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: 37.87 E-value: 2.80e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6678952     238 EQLKKHTILADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 276
Cdd:smart01002  75 ELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDVAA 121

Name

Accession

Description

Interval

E-value

FolD

COG0190

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

37-330

2.07e-155

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

Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 437.52 E-value: 2.07e-155

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   37 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:COG0190   3 AQILDGKAVAAEIREELKERVAALKAKG-ITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:COG0190  82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKHA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  197 VVAGRSKNVGMPIAMLLhtdgAHErpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:COG0190 162 VVVGRSNIVGKPLALLL----LRR----NATVTVCHSRTK--DLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGI 231

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6678952  277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:COG0190 232 NRVED-----GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280

PRK14190

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

37-330

5.56e-128

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

Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 367.80 E-value: 5.56e-128

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14190   3 AVIIDGKEVAKEKREQLKEEVVKLKEQG-IVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14190  82 IDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14190 162 VVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKTK--NLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGV 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6678952   277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:PRK14190 232 NRLEN-----GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280

PRK10792

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

37-330

3.73e-120

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 348.06 E-value: 3.73e-120

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK10792   3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK10792  83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK10792 163 VVVGASNIVGRPMSLELLLAG--------CTVTVCHRFTK--NLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGI 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6678952   277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:PRK10792 233 NRLED-----GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEE 281

PRK14189

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

37-334

2.04e-110

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 323.18 E-value: 2.04e-110

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14189   3 AQLIDGNALSKQLRAEAAQRAAALTARG-HQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14189  82 IDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14189 162 VVIGRSNIVGKPMAMLLLQAG--------ATVTICHSKTR--DLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGM 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6678952   277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRP 334
Cdd:PRK14189 232 NRDDA-----GKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERAAAA 284

PRK14186

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

37-330

2.95e-109

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 320.86 E-value: 2.95e-109

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14186   2 ALILDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14186  82 IAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14186 162 VVVGRSILVGKPLALMLLA--------ANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6678952   277 NRVQDPvTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:PRK14186 232 HRLPSS-DGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284

PRK14191

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

38-333

1.06e-106

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 314.01 E-value: 1.06e-106

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    38 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 117
Cdd:PRK14191   2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   118 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVV 197
Cdd:PRK14191  82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   198 VAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 277
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGIN 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678952   278 RVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 333
Cdd:PRK14191 232 RLND-----GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQR 282

PRK14188

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

36-330

9.53e-103

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 304.19 E-value: 9.53e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    36 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 115
Cdd:PRK14188   1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   116 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 195
Cdd:PRK14188  81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   196 VVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 275
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVG 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6678952   276 INRVQDPVTA--KPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:PRK14188 231 INRIPAPEKGegKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287

PRK14185

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

39-332

2.52e-102

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 302.90 E-value: 2.52e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14185   3 LIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 198
Cdd:PRK14185  83 ELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   199 AGRSKNVGMPIAMLLHTDGAherpGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 278
Cdd:PRK14185 163 LGRSNIVGKPMAQLMMQKAY----PGDCTVTVCHSRSK--NLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6678952   279 VQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 332
Cdd:PRK14185 237 VPDATRKSGfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAI 291

PRK14174

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

38-325

5.16e-100

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

Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 297.12 E-value: 5.16e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    38 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 117
Cdd:PRK14174   2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   118 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYS--MLPATPWGVWEIIKRTGIPTLGKN 195
Cdd:PRK14174  82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDkcFVSCTPYGILELLGRYNIETKGKH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   196 VVVAGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 275
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLM----LQKLKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVG 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6678952   276 INRVQDPVT-AKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTI 325
Cdd:PRK14174 236 INRIEDPSTkSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTL 286

PRK14183

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

39-329

4.79e-99

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

Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 294.43 E-value: 4.79e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14183   3 ILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 198
Cdd:PRK14183  83 MMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVCV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   199 AGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 278
Cdd:PRK14183 163 VGASNIVGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINR 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6678952   279 VQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 329
Cdd:PRK14183 233 TED-----GRLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278

PRK14184

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

39-330

5.04e-99

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

Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 294.38 E-value: 5.04e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14184   3 LLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 198
Cdd:PRK14184  83 ELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   199 AGRSKNVGMPIAMLLHTDGaherPGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 278
Cdd:PRK14184 163 VGRSNIVGKPLALMLGAPG----KFANATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINR 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6678952   279 VQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:PRK14184 237 TDD------GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKE 282

PRK14176

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

36-332

1.54e-97

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

Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 290.55 E-value: 1.54e-97

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    36 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 115
Cdd:PRK14176   7 ESRIIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   116 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 195
Cdd:PRK14176  87 LIDSLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   196 VVVAGRSKNVGMPIA-MLLHTdgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 274
Cdd:PRK14176 167 AVIVGHSNVVGKPMAaMLLNR---------NATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDV 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6678952   275 GINRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 332
Cdd:PRK14176 236 GITKEED------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287

PRK14179

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

37-330

4.48e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;

Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 284.34 E-value: 4.48e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14179   2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14179  82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK--------NATVTLTHSRT--RNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGM 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6678952   277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:PRK14179 232 NRDEN-----GKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280

PRK14168

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

37-329

7.75e-95

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 284.08 E-value: 7.75e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14168   3 AKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCL--DQYSMLPATPWGVWEIIKRTGIPTLGK 194
Cdd:PRK14168  83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   195 NVVVAGRSKNVGMPIAMLLHTDGaherPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 274
Cdd:PRK14168 163 EVVVVGRSNIVGKPIANMMTQKG----PGANATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDV 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678952   275 GINRV-QDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 329
Cdd:PRK14168 237 GVNRVgTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292

PLN02516

methylenetetrahydrofolate dehydrogenase (NADP+)

37-332

8.03e-93

methylenetetrahydrofolate dehydrogenase (NADP+)

Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 279.08 E-value: 8.03e-93

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PLN02516   9 AQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLD--QYSMLPATPWGVWEIIKRTGIPTLGK 194
Cdd:PLN02516  89 VHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKgrEPLFLPCTPKGCLELLSRSGIPIKGK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   195 NVVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTPKEQlkkhTIL--ADIVISAAGIPNLITADMIKEGAAVI 272
Cdd:PLN02516 169 KAVVVGRSNIVGLPVSLLLLK--------ADATVTVVHSRTPDPE----SIVreADIVIAAAGQAMMIKGDWIKPGAAVI 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678952   273 DVGINRVQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVL 332
Cdd:PLN02516 237 DVGTNAVSDPSKKSGyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297

PRK14193

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

37-333

1.98e-92

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

Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 277.66 E-value: 1.98e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14193   3 AIILDGKATADEIKADLAERVAALKEKG-ITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14193  82 IDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLhtdgahERPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14193 162 VVIGRGVTVGRPIGLLL------TRRSENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6678952   277 NRVqdpvtAKPKLVGDVDfEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 333
Cdd:PRK14193 234 SRA-----GDGKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284

PRK14167

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

39-328

4.59e-92

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

Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 277.04 E-value: 4.59e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14167   4 IIDGNAVAAQIRDDLTDAIETLEDAG-VTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 198
Cdd:PRK14167  83 ELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   199 AGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 278
Cdd:PRK14167 163 VGRSDIVGKPMANLL----IQKADGGNATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINR 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 6678952   279 VQDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 328
Cdd:PRK14167 237 VDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286

PRK14166

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

39-333

7.05e-90

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

Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 271.13 E-value: 7.05e-90

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEwVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14166   3 LLDGKALSAKIKEELKEKNQF-LKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLD-QYSMLPATPWGVWEIIKRTGIPTLGKNVV 197
Cdd:PRK14166  82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   198 VAGRSKNVGMPIAMLLHTDGaherpggdATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 277
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678952   278 RVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 333
Cdd:PRK14166 232 RLE-----SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282

PLN02616

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

37-331

2.62e-89

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 272.26 E-value: 2.62e-89

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PLN02616  73 AKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSML--PATPWGVWEIIKRTGIPTLGK 194
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLfvPCTPKGCIELLHRYNVEIKGK 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   195 NVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPK-EQLKKHtilADIVISAAGIPNLITADMIKEGAAVID 273
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQRE--------DATVSIVHSRTKNpEEITRE---ADIIISAVGQPNMVRGSWIKPGAVVID 301

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6678952   274 VGINRVQDPVTAKP-KLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKV 331
Cdd:PLN02616 302 VGINPVEDASSPRGyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRI 360

PRK14187

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

36-328

1.32e-88

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 268.23 E-value: 1.32e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    36 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 115
Cdd:PRK14187   1 ETNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   116 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYS--MLPATPWGVWEIIKRTGIPTLG 193
Cdd:PRK14187  81 KINELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKncLIPCTPKGCLYLIKTITRNLSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   194 KNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVID 273
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLL--------GENCTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6678952   274 VGINRVQdpVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 328
Cdd:PRK14187 231 VGINSIE--EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283

PRK14173

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

37-328

1.67e-88

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

Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 267.47 E-value: 1.67e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVAsgnkRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14173   3 ARELSGPPAAEAVYAELRARLAKLPF----VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14173  79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHtdgaherpGGDATVTISHRYTPkeQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14173 159 VVVGRSNIVGKPLAALLL--------REDATVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGI 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6678952   277 NRVQDPvTAKPKLVGDVDfEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAA 328
Cdd:PRK14173 229 NRVGGN-GGRDILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAA 278

PRK14172

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

39-323

3.91e-88

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

Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 266.26 E-value: 3.91e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14172   4 IINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 198
Cdd:PRK14172  84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   199 AGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 278
Cdd:PRK14172 164 IGRSNIVGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSS 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 6678952   279 VQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKN 323
Cdd:PRK14172 234 VNG------KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272

PRK14175

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

37-329

3.02e-87

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 264.47 E-value: 3.02e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGNKrPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14175   3 AKILDGKQIAKDYRQGLQDQVEALKEKGFT-PKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14175  82 LNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGi 276
Cdd:PRK14175 162 VVIGRSHIVGQPVSKLLLQ--------KNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG- 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6678952   277 nrvqDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 329
Cdd:PRK14175 231 ----NTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279

NAD_bind_m-THF_DH_Cyclohyd

cd01080

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

150-329

4.44e-87

Pssm-ID: 133448 Cd Length: 168 Bit Score: 259.41 E-value: 4.44e-87

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  150 PDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHtdgaherpGGDATVT 229
Cdd:cd01080   1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLL--------NRNATVT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  230 ISHRYTPKeqLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQDPvtAKPKLVGDVDFEGVKKKAGYITPVP 309
Cdd:cd01080  73 VCHSKTKN--LKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDK--SGGKLVGDVDFESAKEKASAITPVP 148

                       170       180
                ....*....|....*....|
gi 6678952  310 GGVGPMTVAMLMKNTIIAAK 329
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168

PRK14169

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

37-330

5.19e-83

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 253.33 E-value: 5.19e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEwVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14169   1 ATRLDGRAVSKKILADLKQTVAK-LAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14169  80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLhtdgaherPGGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGI 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6678952   277 NRVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKK 330
Cdd:PRK14169 230 SRGAD-----GKLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278

THF_DHG_CYH_C

pfam02882

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

158-330

5.71e-83

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

Pssm-ID: 427036 Cd Length: 160 Bit Score: 248.92 E-value: 5.71e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    158 HVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTPk 237
Cdd:pfam02882   1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKTK- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    238 eQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQdpvtaKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTV 317
Cdd:pfam02882  72 -DLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRVG-----NGKLVGDVDFENVKEKASAITPVPGGVGPMTV 145

                         170
                  ....*....|...
gi 6678952    318 AMLMKNTIIAAKK 330
Cdd:pfam02882 146 AMLLQNTVEAAKR 158

PRK14170

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

39-333

1.48e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 249.99 E-value: 1.48e-81

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14170   4 IIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVV 198
Cdd:PRK14170  83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   199 AGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINR 278
Cdd:PRK14170 163 IGRSNIVGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6678952   279 VQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 333
Cdd:PRK14170 233 DEN-----NKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRIWK 282

PRK14171

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

39-329

3.45e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 249.10 E-value: 3.45e-81

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14171   4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRM--CLDQySMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14171  84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLhsGISQ-GFIPCTALGCLAVIKKYEPNLTGKNV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14171 163 VIIGRSNIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGI 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6678952   277 NRVqdpvtAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 329
Cdd:PRK14171 233 NRI-----SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK 280

PRK14178

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

38-329

4.05e-81

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 248.60 E-value: 4.05e-81

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    38 VVISGRKLAQQIKQEVQQEVEEwvasGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 117
Cdd:PRK14178   1 MILDGKAVSEKRLELLKEEIIE----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   118 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVV 197
Cdd:PRK14178  77 RRLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   198 VAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 277
Cdd:PRK14178 157 VVGRSIDVGRPMAALLLN--------ADATVTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGIN 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6678952   278 RVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 329
Cdd:PRK14178 227 QVNG------KLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272

PRK14180

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

38-333

9.53e-81

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

Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 247.64 E-value: 9.53e-81

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    38 VVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 117
Cdd:PRK14180   2 ILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   118 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCL-DQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14180  82 DQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14180 162 VVVGASNVVGKPVSQLLLN--------AKATVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGI 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6678952   277 NRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 333
Cdd:PRK14180 232 NHVDG------KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELNR 282

PLN02897

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

27-331

3.50e-80

tetrahydrofolate dehydrogenase/cyclohydrolase, putative

Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 248.34 E-value: 3.50e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    27 PFHLAAVRNEAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPA 106
Cdd:PLN02897  46 PPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   107 SVSEEELLNSIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSML--PATPWGVWEII 184
Cdd:PLN02897 126 DCTEGQILSALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLfvSCTPKGCVELL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   185 KRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDgaherpggDATVTISHRYT--PKEQLKKhtilADIVISAAGIPNLITA 262
Cdd:PLN02897 206 IRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRH--------DATVSTVHAFTkdPEQITRK----ADIVIAAAGIPNLVRG 273

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   263 DMIKEGAAVIDVGINRVQDPVTA-KPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKV 331
Cdd:PLN02897 274 SWLKPGAVVIDVGTTPVEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343

PRK14177

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

36-334

2.31e-78

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 241.80 E-value: 2.31e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    36 EAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLN 115
Cdd:PRK14177   2 SPILLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   116 SIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN 195
Cdd:PRK14177  82 VIDKLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   196 VVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG 275
Cdd:PRK14177 162 AVVVGRSPILGKPMAMLLTE--------MNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAG 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6678952   276 INrvqdpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRP 334
Cdd:PRK14177 232 YN---------PGNVGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHFTP 281

PRK14194

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

35-329

3.82e-77

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 238.98 E-value: 3.82e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    35 NEAVVISGRKLAQQIKQEVQQEVEEWVASGNKrPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELL 114
Cdd:PRK14194   2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIE-PALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   115 NSIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGK 194
Cdd:PRK14194  81 ALIAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   195 NVVVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDV 274
Cdd:PRK14194 161 HAVVIGRSNIVGKPMAALLLQ--------AHCSVTVVH--SRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDV 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6678952   275 GINRVQDpvTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAK 329
Cdd:PRK14194 231 GINRIDD--DGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283

PRK14181

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

38-324

4.26e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 235.91 E-value: 4.26e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    38 VVISGRKLAQQIKQEVQQEVeewvASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSI 117
Cdd:PRK14181   1 MLLKGAPAAEHILATIKENI----SASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   118 RKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQY-SMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14181  77 HRLNNDPNIHGILVQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETdGFIPCTPAGIIELLKYYEIPLHGRHV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLhtdgAHERPGGDATVTISHryTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14181 157 AIVGRSNIVGKPLAALL----MQKHPDTNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGT 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6678952   277 NRVQdpvTAKPK---LVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNT 324
Cdd:PRK14181 231 SRVP---AANPKgyiLVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNT 278

PRK14192

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...

37-333

5.04e-76

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;

Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 235.51 E-value: 5.04e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    37 AVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNS 116
Cdd:PRK14192   3 ALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   117 IRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNV 196
Cdd:PRK14192  83 IEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKHA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   197 VVAGRSKNVGMPIAMLLHTdgaherpgGDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGI 276
Cdd:PRK14192 163 VVVGRSAILGKPMAMMLLN--------ANATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGF 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6678952   277 NRVQDpvtakpKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 333
Cdd:PRK14192 233 HPRDG------GGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283

PRK14182

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

39-333

5.07e-71

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

Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 222.97 E-value: 5.07e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952    39 VISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIR 118
Cdd:PRK14182   3 LIDGKQIAAKVKGEVATEVRALAARG-VQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   119 KLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSM-LPATPWGVWEIIKRTGIPTLGKNVV 197
Cdd:PRK14182  82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVpRPCTPAGVMRMLDEARVDPKGKRAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952   198 VAGRSKNVGMPIAMLLhtdgaHERpggDATVTISHRYTpkEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGIN 277
Cdd:PRK14182 162 VVGRSNIVGKPMAMML-----LER---HATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMN 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678952   278 RVQDpvtakPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLR 333
Cdd:PRK14182 232 RLAD-----GKLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTAR 282

THF_DHG_CYH

pfam00763

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;

40-155

5.92e-60

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;

Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 188.38 E-value: 5.92e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952     40 ISGRKLAQQIKQEVQQEVEEWVASGnKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIRK 119
Cdd:pfam00763   1 IDGKAIAKKIREELKEEVAALKAGG-RKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 6678952    120 LNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVD 155
Cdd:pfam00763  80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115

NAD_bind_m-THF_DH_Cyclohyd_like

cd05212

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

173-329

1.45e-20

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: 86.41 E-value: 1.45e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  173 LPATPWGVWEIIKRTGI-------PTLGKNVVVAGRSKNVGMPIAMLLHTDGAherpggdaTVTISHRYTPKEQLKKHTi 245
Cdd:cd05212   1 GPCTPLFVSPVAKAVKEllnkegvRLDGKKVLVVGRSGIVGAPLQCLLQRDGA--------TVYSCDWKTIQLQSKVHD- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  246 lADIVISAAGIPNLITADMIKEGAAVIDVGINrvqdpvtakpKLVGDVdfegVKKKAGYITPVPGGVGPMTVAMLMKNTI 325
Cdd:cd05212  72 -ADVVVVGSPKPEKVPTEWIKPGATVINCSPT----------KLSGDD----VKESASLYVPMTGGVGKLTVAMRMQNMV 136


                ....
gi 6678952  326 IAAK 329
Cdd:cd05212 137 RSVR 140

NAD_bind_m-THF_DH

cd01079

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

150-325

4.49e-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: 4.49e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  150 PDKDVDGFHVINVGRMC-----LD----QYSMLPATPWGVWEIIKRTGI---------PTLGKNVVVAGRSKNVGMPIAM 211
Cdd:cd01079   1 PHKDVEGLSHKYIFNLYhnirfLDpenrKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952  212 LLHTDGAH----ERPGGDA-TVTISHRYTPK------EQLKKHTILADIVISAAGIPNL-ITADMIKEGAAVIDVGinrv 279
Cdd:cd01079  81 LLANDGARvysvDINGIQVfTRGESIRHEKHhvtdeeAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINFA---- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 6678952  280 qdpvtakpklvGDVDFE-GVKKKAGYITPVpggVGPMTVAMLMKNTI 325
Cdd:cd01079 157 -----------SIKNFEpSVKEKASIYVPS---IGKVTIAMLLRNLL 189

AlaDh_PNT_C

smart01002

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

238-276

2.80e-03

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: 37.87 E-value: 2.80e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6678952     238 EQLKKHTILADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 276
Cdd:smart01002  75 ELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDVAA 121

L-AlaDH

cd05305

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...

223-276

3.59e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.

Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 38.93 E-value: 3.59e-03

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678952  223 GGDATVTISHRYTPKEQLKKhtilADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 276
Cdd:cd05305 212 GGRVTTLYSNPANLEEALKE----ADLVIGAVLIPGakapkLVTEEMVktmKPGSVIVDVAI 269

Ald

COG0686

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...

219-276

5.49e-03

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle

Pssm-ID: 440450 [Multi-domain] Cd Length: 372 Bit Score: 38.45 E-value: 5.49e-03

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678952  219 HERPGGDATVTISHRYTPKEQLKKhtilADIVISAAGIPN-----LITADMI---KEGAAVIDVGI 276
Cdd:COG0686 208 DDIFGGRVTTLYSNPANIEEALKE----ADLVIGAVLIPGarapkLVTREMVkrmKPGSVIVDVAI 269

AlaDh_PNT_C

pfam01262

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...

233-276

5.73e-03

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.

Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 37.47 E-value: 5.73e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6678952    233 RYTPKEQLKKHTILADIVISAAGI-----PNLITADMI---KEGAAVIDVGI 276
Cdd:pfam01262  79 LYSQAELIAEAVKEADLVIGTALIpgakaPKLVTREMVksmKPGSVIVDVAI 130

AdoHcyase_NAD

smart00997

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;

180-277

9.03e-03

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;

Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 36.27 E-value: 9.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678952     180 VWEIIKR-TGIPTLGKNVVVAGRSKnVGMPIAMLLHtdgaherpGGDATVTIS--------------HRYTPKEQLKKht 244
Cdd:smart00997   9 LLDGILRaTNVLLAGKNVVVAGYGD-VGKGVAARLR--------GLGARVIVTeidpiraleaamdgFEVMKMEEAAK-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 6678952     245 iLADIVISAAGIPNLITADMI---KEGAAV-----IDVGIN 277
Cdd:smart00997  78 -RADIFVTATGNKDVITREHFramKDGAILanaghFDVEID 117

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