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Conserved domains on  [gi|2217360955|ref|XP_047274573|]
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monofunctional C1-tetrahydrofolate synthase, mitochondrial isoform X17 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 352-708 0e+00

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PLN02759:

Pssm-ID: 476819  Cd Length: 637  Bit Score: 603.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 352 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 431
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 432 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 511
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 512 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 590
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 591 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 670
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2217360955 671 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFV 708
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFV 366
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
 193-335 3.21e-68

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: 220.07  E-value: 3.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 193 GDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSP 272
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217360955 273 KPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 335
Cdd:cd05212    81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
PLN02897 super family cl31946
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 52-290 1.60e-25

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


The actual alignment was detected with superfamily member PLN02897:

Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 108.51  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  52 PQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFK------PVLAIIQAGDDNLMQEINQN---LAEEA 122
Cdd:PLN02897   35 PENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKkavgkvPGLAVVLVGQQRDSQTYVRNkikACEET 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 123 GLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFV 200
Cdd:PLN02897  115 GIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 201 SPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLT 280
Cdd:PLN02897  195 SCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGS 274

                         250
                  ....*....|
gi 2217360955 281 WIQPGTTVLN 290
Cdd:PLN02897  275 WLKPGAVVID 284
 
Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
 352-708 0e+00

Formate--tetrahydrofolate ligase


Pssm-ID: 178359  Cd Length: 637  Bit Score: 603.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 352 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 431
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 432 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 511
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 512 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 590
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 591 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 670
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2217360955 671 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFV 708
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFV 366
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
360-707 0e+00

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 535.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 360 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 439
Cdd:pfam01268   1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 440 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 519
Cdd:pfam01268  81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 520 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 599
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 600 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 679
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2217360955 680 GPFANIAHGNSSVLADKIALKL----VGEEGF 707
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKLadyvVTEAGF 300
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
 374-707 8.08e-169

formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.


Pssm-ID: 349750  Cd Length: 540  Bit Score: 495.13  E-value: 8.08e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 374 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 453
Cdd:cd00477     1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 454 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 533
Cdd:cd00477    80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 534 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 613
Cdd:cd00477   139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 614 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 693
Cdd:cd00477   189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268

                         330
                  ....*....|....*...
gi 2217360955 694 ADKIALKL----VGEEGF 707
Cdd:cd00477   269 ADKIALKLadyvVTEAGF 286
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
359-707 6.96e-158

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 467.59  E-value: 6.96e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 359 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 438
Cdd:COG2759     1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 439 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 518
Cdd:COG2759    81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 519 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 598
Cdd:COG2759   153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 599 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 678
Cdd:COG2759   189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2217360955 679 AGPFANIAHGNSSVLADKIALKL----VGEEGF 707
Cdd:COG2759   269 GGPFANIAHGCNSVIATKLALKLadyvVTEAGF 301
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
 193-335 3.21e-68

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: 220.07  E-value: 3.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 193 GDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSP 272
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217360955 273 KPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 335
Cdd:cd05212    81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
183-338 7.58e-36

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 132.59  E-value: 7.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 183 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLH 262
Cdd:pfam02882   1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 263 EADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRIQ 328
Cdd:pfam02882  79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLLQ 150

                         170
                  ....*....|
gi 2217360955 329 NMVSSGRRWL 338
Cdd:pfam02882 151 NTVEAAKRQL 160
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 97-289 1.88e-33

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 129.75  E-value: 1.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 162
Cdd:COG0190    32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 163 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAhgSLE-----AALq 237
Cdd:COG0190   107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVGR--SNIvgkplALL- 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360955 238 cLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 289
Cdd:COG0190   178 -LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 52-290 1.60e-25

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 108.51  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  52 PQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFK------PVLAIIQAGDDNLMQEINQN---LAEEA 122
Cdd:PLN02897   35 PENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKkavgkvPGLAVVLVGQQRDSQTYVRNkikACEET 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 123 GLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFV 200
Cdd:PLN02897  115 GIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 201 SPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLT 280
Cdd:PLN02897  195 SCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGS 274

                         250
                  ....*....|
gi 2217360955 281 WIQPGTTVLN 290
Cdd:PLN02897  275 WLKPGAVVID 284
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
 98-290 1.04e-24

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 104.97  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  98 PVLAIIQAG---DDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 172
Cdd:PLN02516   40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 252
Cdd:PLN02516  120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHS 199

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217360955 253 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PLN02516  200 RTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
90-180 1.69e-17

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 78.60  E-value: 1.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  90 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 164
Cdd:pfam00763  20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99

                          90
                  ....*....|....*.
gi 2217360955 165 FSNKVLNALKPEKDVD 180
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
 
Name Accession Description Interval E-value
PLN02759 PLN02759
Formate--tetrahydrofolate ligase
 352-708 0e+00

Formate--tetrahydrofolate ligase


Pssm-ID: 178359  Cd Length: 637  Bit Score: 603.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 352 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 431
Cdd:PLN02759    9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 432 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 511
Cdd:PLN02759   89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 512 TQTDKALYNRLVPL-VNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIG 590
Cdd:PLN02759  169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 591 QGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTL 670
Cdd:PLN02759  249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2217360955 671 EGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFV 708
Cdd:PLN02759  329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFV 366
PTZ00386 PTZ00386
formyl tetrahydrofolate synthetase; Provisional
 352-708 0e+00

formyl tetrahydrofolate synthetase; Provisional


Pssm-ID: 240394  Cd Length: 625  Bit Score: 564.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 352 KLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKST 431
Cdd:PTZ00386    8 KLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKST 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 432 VTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEN 511
Cdd:PTZ00386   88 TTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHER 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 512 TQTDKALYNRLVplvNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQ 591
Cdd:PTZ00386  168 TQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITIGQ 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 592 GNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLE 671
Cdd:PTZ00386  245 GKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLE 324

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2217360955 672 GTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFV 708
Cdd:PTZ00386  325 GTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFV 361
FTHFS pfam01268
Formate--tetrahydrofolate ligase;
360-707 0e+00

Formate--tetrahydrofolate ligase;


Pssm-ID: 460143  Cd Length: 555  Bit Score: 535.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 360 PSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQA 439
Cdd:pfam01268   1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 440 LtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkaly 519
Cdd:pfam01268  81 L-NRLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNE------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 520 nrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHY 599
Cdd:pfam01268 153 --------------------------------------------LDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 600 RQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHA 679
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2217360955 680 GPFANIAHGNSSVLADKIALKL----VGEEGF 707
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKLadyvVTEAGF 300
FTHFS cd00477
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ...
 374-707 8.08e-169

formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrofolate. FTHFS is a highly expressed key enzyme in both the Wood-Ljungdahl pathway of autotrophic CO2 fixation (acetogenesis) and the glycine synthase/reductase pathways of purinolysis. The key physiological role of this enzyme in acetogens is to catalyze the formylation of tetrahydrofolate, an initial step in the reduction of carbon dioxide and other one-carbon precursors to acetate. In purinolytic organisms, the enzymatic reaction is reversed, liberating formate from 10-formyltetrahydrofolate with concurrent production of ATP.


Pssm-ID: 349750  Cd Length: 540  Bit Score: 495.13  E-value: 8.08e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 374 VDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNvNSFACLR 453
Cdd:cd00477     1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 454 QPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdkalynrlvplvngvrefs 533
Cdd:cd00477    80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENT--------------------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 534 eiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIM 613
Cdd:cd00477   139 ------------------------------LDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 614 AVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVL 693
Cdd:cd00477   189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268

                         330
                  ....*....|....*...
gi 2217360955 694 ADKIALKL----VGEEGF 707
Cdd:cd00477   269 ADKIALKLadyvVTEAGF 286
MIS1 COG2759
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
359-707 6.96e-158

Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];


Pssm-ID: 442046  Cd Length: 556  Bit Score: 467.59  E-value: 6.96e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 359 VPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQ 438
Cdd:COG2759     1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 439 ALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENtqtdkal 518
Cdd:COG2759    81 AL-NRLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQGN------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 519 ynrlvplvngvrefseiqlarlkklginktdpstlteeevskfaRLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGH 598
Cdd:COG2759   153 --------------------------------------------ELNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 599 YRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVH 678
Cdd:COG2759   189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2217360955 679 AGPFANIAHGNSSVLADKIALKL----VGEEGF 707
Cdd:COG2759   269 GGPFANIAHGCNSVIATKLALKLadyvVTEAGF 301
PRK13506 PRK13506
formate--tetrahydrofolate ligase; Provisional
 361-707 6.00e-143

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237404  Cd Length: 578  Bit Score: 430.19  E-value: 6.00e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 361 SDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQAL 440
Cdd:PRK13506    3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 441 tAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHEntqtdkalyN 520
Cdd:PRK13506   83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------Q 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 521 RLvplvnGVREFseiqlarlkklginktdpstlteEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYR 600
Cdd:PRK13506  153 RL-----GYDAF-----------------------EAQSGLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 601 QAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAG 680
Cdd:PRK13506  205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2217360955 681 PFANIAHGNSSVLADKIALKL----VGEEGF 707
Cdd:PRK13506  285 PFANIAHGNSSIIADRIALKLadyvVTEGGF 315
PRK13505 PRK13505
formate--tetrahydrofolate ligase; Provisional
 358-707 6.68e-135

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 237403  Cd Length: 557  Bit Score: 408.80  E-value: 6.68e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 358 PVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLV 437
Cdd:PRK13505    1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 438 QALtAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTqtdka 517
Cdd:PRK13505   81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNE----- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 518 lynrlvplvngvrefseiqlarlkklginktdpstlteeevskfarLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKG 597
Cdd:PRK13505  155 ----------------------------------------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 598 HYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFV 677
Cdd:PRK13505  189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268

                         330       340       350
                  ....*....|....*....|....*....|....
gi 2217360955 678 HAGPFANIAHGNSSVLADKIALKL----VGEEGF 707
Cdd:PRK13505  269 HGGPFANIAHGCNSVLATKTALKLadyvVTEAGF 302
PRK13507 PRK13507
formate--tetrahydrofolate ligase; Provisional
 372-707 2.47e-106

formate--tetrahydrofolate ligase; Provisional


Pssm-ID: 184098  Cd Length: 587  Bit Score: 335.53  E-value: 2.47e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 372 KAVDVLAKEIGLLADEIEIYGKSKAKVR-LSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALtAHLNVNSFA 450
Cdd:PRK13507   22 KPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGL-GKRGKKVSG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 451 CLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKalynrlvplvngvr 530
Cdd:PRK13507  101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDE-------------- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 531 efseiQLARlkklginktdpstlteeevSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVAS 610
Cdd:PRK13507  167 -----QLAR-------------------RGLKRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 611 EIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 690
Cdd:PRK13507  223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302

                         330       340
                  ....*....|....*....|.
gi 2217360955 691 SVLADKIALKL----VGEEGF 707
Cdd:PRK13507  303 SIIADRVGLKLadyhVTESGF 323
NAD_bind_m-THF_DH_Cyclohyd_like cd05212
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ...
 193-335 3.21e-68

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: 220.07  E-value: 3.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 193 GDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSP 272
Cdd:cd05212     1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217360955 273 KPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIeedDVILLAAALRIQNMVSSGR 335
Cdd:cd05212    81 KPEKVPTEWIKPGATVINCSPTKLSGDDVKESASLYVPMTG---GVGKLTVAMRMQNMVRSVR 140
THF_DHG_CYH_C pfam02882
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
183-338 7.58e-36

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


Pssm-ID: 427036  Cd Length: 160  Bit Score: 132.59  E-value: 7.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 183 TDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLH 262
Cdd:pfam02882   1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 263 EADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHF--------------GGlieeddVILLAAALRIQ 328
Cdd:pfam02882  79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNGKLVGD--VDFenvkekasaitpvpGG------VGPMTVAMLLQ 150

                         170
                  ....*....|
gi 2217360955 329 NMVSSGRRWL 338
Cdd:pfam02882 151 NTVEAAKRQL 160
FolD COG0190
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ...
 97-289 1.88e-33

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


Pssm-ID: 439960 [Multi-domain]  Cd Length: 285  Bit Score: 129.75  E-value: 1.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDD--------NLmqeinQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ------ISE 162
Cdd:COG0190    32 TPGLAVVLVGDDpasqvyvrNK-----HKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQlplpkhIDE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 163 NlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAhgSLE-----AALq 237
Cdd:COG0190   107 E----AVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVGR--SNIvgkplALL- 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360955 238 cLFQRKGSMTM--SiqwKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 289
Cdd:COG0190   178 -LLRRNATVTVchS---RTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVI 227
PLN02897 PLN02897
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 52-290 1.60e-25

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 178485 [Multi-domain]  Cd Length: 345  Bit Score: 108.51  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  52 PQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFK------PVLAIIQAGDDNLMQEINQN---LAEEA 122
Cdd:PLN02897   35 PENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIASEVRKMKkavgkvPGLAVVLVGQQRDSQTYVRNkikACEET 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 123 GLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFV 200
Cdd:PLN02897  115 GIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPlpQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 201 SPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLT 280
Cdd:PLN02897  195 SCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGS 274

                         250
                  ....*....|
gi 2217360955 281 WIQPGTTVLN 290
Cdd:PLN02897  275 WLKPGAVVID 284
PLN02616 PLN02616
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
 71-290 3.86e-25

tetrahydrofolate dehydrogenase/cyclohydrolase, putative


Pssm-ID: 215332 [Multi-domain]  Cd Length: 364  Bit Score: 107.78  E-value: 3.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  71 RDSIVREVIQnSKEVLSLLqeknpafkPVLAIIQAGD--DNLMQEINQNLA-EEAGLNITHICLPPDSSEAEIIDEILKI 147
Cdd:PLN02616   86 RDEITIEVSR-MKESIGVV--------PGLAVILVGDrkDSATYVRNKKKAcDSVGINSFEVRLPEDSTEQEVLKFISGF 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 148 NEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILV 225
Cdd:PLN02616  157 NNDPSVHGILVQLPlpSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEIKGKRAVV 236

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217360955 226 VGAHG--SLEAALqcLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PLN02616  237 IGRSNivGMPAAL--LLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVID 301
PRK14190 PRK14190
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 65-290 4.54e-25

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


Pssm-ID: 184560 [Multi-domain]  Cd Length: 284  Bit Score: 105.48  E-value: 4.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  65 GRTPAARdsiVREviQNSKEVLSLlqeKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEII 141
Cdd:PRK14190    8 GKEVAKE---KRE--QLKEEVVKL---KEQGIVPGLAVILVGDDPASHsyvRGKKKAAEKVGIYSELYEFPADITEEELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 142 DEILKINEDTRVHGLALQ------ISENlfsnKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSG 215
Cdd:PRK14190   80 ALIDRLNADPRINGILVQlplpkhIDEK----AVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYN 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217360955 216 VNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14190  154 IDISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVID 228
PLN02516 PLN02516
methylenetetrahydrofolate dehydrogenase (NADP+)
 98-290 1.04e-24

methylenetetrahydrofolate dehydrogenase (NADP+)


Pssm-ID: 178131 [Multi-domain]  Cd Length: 299  Bit Score: 104.97  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  98 PVLAIIQAG---DDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 172
Cdd:PLN02516   40 PGLAVVIVGsrkDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPlpKHINEEKILNE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 252
Cdd:PLN02516  120 ISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHS 199

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217360955 253 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PLN02516  200 RTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
PRK14187 PRK14187
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 98-290 9.39e-24

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172675 [Multi-domain]  Cd Length: 294  Bit Score: 102.21  E-value: 9.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14187   33 PCLIVILVGDDPASQlyvRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQlpVPNHIDKNLIINT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 252
Cdd:PRK14187  113 IDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHS 192

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217360955 253 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14187  193 ATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
PRK14172 PRK14172
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 97-300 1.46e-23

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


Pssm-ID: 172660 [Multi-domain]  Cd Length: 278  Bit Score: 101.01  E-value: 1.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDD--NLMQEINQN-LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14172   32 IPKIASILVGNDggSIYYMNNQEkVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQlpLPKHLDEKKITN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 172 ALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 251
Cdd:PRK14172  112 KIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTICH 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217360955 252 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 300
Cdd:PRK14172  190 SKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNGKI 238
PRK14175 PRK14175
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 74-274 1.11e-21

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184552 [Multi-domain]  Cd Length: 286  Bit Score: 95.75  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  74 IVREVIQNSKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINED 150
Cdd:PRK14175   11 IAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYvrsKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNND 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 151 TRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVG- 227
Cdd:PRK14175   89 DSVSGILVQVPlpKQVSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADIDLEGKNAVVIGr 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217360955 228 AHGSLEAALQCLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKP 274
Cdd:PRK14175  167 SHIVGQPVSKLLLQKNASVTI-LHSRSKDMASYLKDADVIVSAVGKP 212
PRK14167 PRK14167
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 97-290 1.37e-21

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


Pssm-ID: 184549 [Multi-domain]  Cd Length: 297  Bit Score: 95.61  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14167   31 TPGLATVLMSDDPASEtyvSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQmpVPDHVDDREVLR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 172 ALKPEKDVDGVTDINLGKLVRGDAHecFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRK---GSMTM 248
Cdd:PRK14167  111 RIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQKadgGNATV 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217360955 249 SI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14167  189 TVcHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
PRK14192 PRK14192
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 98-314 8.89e-21

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184561 [Multi-domain]  Cd Length: 283  Bit Score: 92.99  E-value: 8.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14192   34 PILATILVGDDPASAtyvRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANPDVHGILLQhpVPAQIDERACFDA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 173 LKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAAL-QCLFQRKGSMTMSiQ 251
Cdd:PRK14192  114 ISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAILGKPMaMMLLNANATVTIC-H 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217360955 252 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCS-HDFLSGKVGcgspRIHFGGLIE 314
Cdd:PRK14192  191 SRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGfHPRDGGGVG----DIELQGIEE 250
PRK14170 PRK14170
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 82-319 1.38e-20

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172658 [Multi-domain]  Cd Length: 284  Bit Score: 92.45  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  82 SKEVLSLLQEKNpafKPVLAIIQAGDDNLMQEI---NQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLAL 158
Cdd:PRK14170   19 TREVAELVKEGK---KPGLAVVLVGDNQASRTYvrnKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 159 Q--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSL-EAA 235
Cdd:PRK14170   96 QlpLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIG--KDSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNIVgKPV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 236 LQCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSprIHFGGLIEE 315
Cdd:PRK14170  174 AQLLLNENATVTIA-HSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRDENNKLCGD--VDFDDVVEE 250


                  ....
gi 2217360955 316 DDVI 319
Cdd:PRK14170  251 AGFI 254
PRK10792 PRK10792
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 97-289 1.52e-20

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 236760 [Multi-domain]  Cd Length: 285  Bit Score: 92.29  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK10792   33 APGLAVVLVGSDPASQVYVASkrkACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQlpLPAHIDNVKVLE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 172 ALKPEKDVDGVTDINLGKLvrgdaheCFVSPV-----AKAVIELLEKSGVNLDGKKILVVGAHG------SLEAALqclf 240
Cdd:PRK10792  113 RIHPDKDVDGFHPYNVGRL-------AQRIPLlrpctPRGIMTLLERYGIDTYGLNAVVVGASNivgrpmSLELLL---- 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217360955 241 qrKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 289
Cdd:PRK10792  182 --AGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVI 228
PRK14186 PRK14186
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 131-290 3.11e-20

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237636 [Multi-domain]  Cd Length: 297  Bit Score: 91.66  E-value: 3.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 131 LPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVakAVI 208
Cdd:PRK14186   69 LPADTSQAEVEALIAQLNQDERVDGILLQlpLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPA--GVM 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 209 ELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTV 288
Cdd:PRK14186  147 RLLRSQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVV 226


                  ..
gi 2217360955 289 LN 290
Cdd:PRK14186  227 VD 228
PRK14180 PRK14180
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 95-300 2.48e-19

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


Pssm-ID: 172668 [Multi-domain]  Cd Length: 282  Bit Score: 88.93  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  95 AFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKV 169
Cdd:PRK14180   29 AITPKLVAIIVGNDPASKtyvASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPlpAHINKNNV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 170 LNALKPEKDVDGVTDINLGKLVRGDaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSL-EAALQCLFQRKGSMTM 248
Cdd:PRK14180  109 IYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVgKPVSQLLLNAKATVTT 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217360955 249 SIQWkTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV 300
Cdd:PRK14180  188 CHRF-TTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDGKI 238
PRK14189 PRK14189
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
97-290 2.93e-19

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 184559 [Multi-domain]  Cd Length: 285  Bit Score: 88.59  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLN 171
Cdd:PRK14189   32 QPGLAVILVGDNPASQVYVRNKVkacEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQlpLPKHIDSHKVIE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 172 ALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQ 251
Cdd:PRK14189  112 AIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLESIGIPLRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICH 189

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217360955 252 WKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14189  190 SKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
PRK14174 PRK14174
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 98-290 3.43e-19

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


Pssm-ID: 172662 [Multi-domain]  Cd Length: 295  Bit Score: 88.72  E-value: 3.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  98 PVLAIIQAGDDNLMQEINQNLAE---EAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNA 172
Cdd:PRK14174   32 PGLTVIIVGEDPASQVYVRNKAKsckEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQqpLPKQIDEFAVTLA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 173 LKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAH---GSLEAALQCLFQRKGSMTMS 249
Cdd:PRK14174  112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSnivGKPMANLMLQKLKESNCTVT 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217360955 250 I-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14174  192 IcHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVID 233
PRK14194 PRK14194
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 65-290 2.47e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172682 [Multi-domain]  Cd Length: 301  Bit Score: 86.44  E-value: 2.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  65 GRTPAARdsivreVIQNSKEVLSLLqeKNPAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEII 141
Cdd:PRK14194    9 GKAAAAR------VLAQVREDVRTL--KAAGIEPALAVILVGNDPASQVYVRNkilRAEEAGIRSLEHRLPADTSQARLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 142 DEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAhecFVSPVAKA-VIELLEKSGVNL 218
Cdd:PRK14194   81 ALIAELNADPSVNGILLQlpLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRD---VLTPCTPSgCLRLLEDTCGDL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217360955 219 DGKKILVVGAH---GSLEAALqcLFQRKGSMTMsIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14194  158 TGKHAVVIGRSnivGKPMAAL--LLQAHCSVTV-VHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVID 229
PRK14191 PRK14191
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 98-290 2.72e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172679 [Multi-domain]  Cd Length: 285  Bit Score: 85.97  E-value: 2.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  98 PVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLNA 172
Cdd:PRK14191   32 PKLAVILVGKDPASQtyvNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLPlpRHIDTKMVLEA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 173 LKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW 252
Cdd:PRK14191  112 IDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCHI 189

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217360955 253 KTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14191  190 LTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVD 227
PRK14177 PRK14177
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 75-301 3.24e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172665 [Multi-domain]  Cd Length: 284  Bit Score: 85.41  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  75 VREVIQNskEVLSLLQEKNPAFK--PVLAIIQAGDdNLMQEINQNL----AEEAGLNITHICLPPDSSEAEIIDEILKIN 148
Cdd:PRK14177   11 LSEKIRN--EIRETIEERKTKNKriPKLATILVGN-NPASETYVSMkvkaCHKVGMGSEMIRLKEQTTTEELLGVIDKLN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 149 EDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVV 226
Cdd:PRK14177   88 LDPNVDGILLQhpVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVTGKNAVVV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217360955 227 GAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDflSGKVG 301
Cdd:PRK14177  166 GRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGNVG 238
PRK14168 PRK14168
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 119-290 4.22e-18

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 237633 [Multi-domain]  Cd Length: 297  Bit Score: 85.31  E-value: 4.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 119 AEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAH 196
Cdd:PRK14168   58 AHRLGFHEIQDNQSVDITEEELLALIDKYNNDDSIHGILVQlpLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDE 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 197 ECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKG----SMTMSIQWKTRQLQSKLHEADIVVLGSP 272
Cdd:PRK14168  138 VKFLPCTPAGIQEMLVRSGVETSGAEVVVVGRSNIVGKPIANMMTQKGpganATVTIVHTRSKNLARHCQRADILIVAAG 217

                         170
                  ....*....|....*...
gi 2217360955 273 KPEEIPLTWIQPGTTVLN 290
Cdd:PRK14168  218 VPNLVKPEWIKPGATVID 235
PRK14188 PRK14188
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 97-289 1.07e-17

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184558 [Multi-domain]  Cd Length: 296  Bit Score: 84.24  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDDNLMQEINQN---LAEEAGLN-ITHIcLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENLFSNKVL 170
Cdd:PRK14188   32 TPGLAVVLVGEDPASQVYVRSkgkQTKEAGMAsFEHK-LPADTSQAELLALIARLNADPAIHGILVQlpLPKHLDSEAVI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 171 NALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAH---GSLEAALqcLFQRKGSMT 247
Cdd:PRK14188  111 QAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSnlvGKPMAQL--LLAANATVT 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217360955 248 MSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVL 289
Cdd:PRK14188  187 IA-HSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVI 227
PRK14176 PRK14176
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 91-290 1.16e-17

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


Pssm-ID: 184553 [Multi-domain]  Cd Length: 287  Bit Score: 84.09  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  91 EKNPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLF 165
Cdd:PRK14176   32 KSNRGITPGLATILVGDDPASKmyvRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPlpKHLD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 166 SNKVLNALKPEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGS 245
Cdd:PRK14176  112 PQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNVVGKPMAAMLLNRNA 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217360955 246 MTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14176  190 TVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFD 234
THF_DHG_CYH pfam00763
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
90-180 1.69e-17

Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;


Pssm-ID: 459930 [Multi-domain]  Cd Length: 115  Bit Score: 78.60  E-value: 1.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  90 QEKNPAFKPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ--ISENL 164
Cdd:pfam00763  20 ALKAGGRKPGLAVILVGDDpasQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQlpLPKHI 99

                          90
                  ....*....|....*.
gi 2217360955 165 FSNKVLNALKPEKDVD 180
Cdd:pfam00763 100 DEEKVLEAIDPEKDVD 115
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 69-290 1.86e-17

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


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 83.14  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  69 AARDSIVREViqnsKEVLSLLQEKnpAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEIL 145
Cdd:PRK14193   10 ATADEIKADL----AERVAALKEK--GITPGLGTVLVGDDPGSQayvRGKHRDCAEVGITSIRRDLPADATQEELNAVID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 146 KINEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLEKSGVNLDGKKI 223
Cdd:PRK14193   84 ELNADPACTGYIVQLPlpKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTP--RGIVHLLRRYDVELAGAHV 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217360955 224 LVVGAHGSLEAALQCLFQRKG-SMTMSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14193  162 VVIGRGVTVGRPIGLLLTRRSeNATVTLcHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLD 230
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 175-291 4.07e-17

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: 79.52  E-value: 4.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 175 PEKDVDGVTDINLGKLVRGDahECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKT 254
Cdd:cd01080     1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2217360955 255 RQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNC 291
Cdd:cd01080    79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDV 115
PRK14178 PRK14178
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 82-303 4.73e-17

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172666 [Multi-domain]  Cd Length: 279  Bit Score: 82.20  E-value: 4.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  82 SKEVLSLLQEK--NPAFKPVLAIIQAGDDNLMQ---EINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGL 156
Cdd:PRK14178    9 SEKRLELLKEEiiESGLYPRLATVIVGDDPASQmyvRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 157 ALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPvaKAVIELLEKSGVNLDGKKILVVGAH---GS 231
Cdd:PRK14178   89 LVQLPlpKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTP--NGIMTLLHEYKISIAGKRAVVVGRSidvGR 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217360955 232 LEAALqcLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVgCG 303
Cdd:PRK14178  167 PMAAL--LLNADATVTIC-HSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNGKL-CG 234
PRK14179 PRK14179
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
83-290 8.70e-17

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;


Pssm-ID: 237634 [Multi-domain]  Cd Length: 284  Bit Score: 81.34  E-value: 8.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  83 KEVLSLLQEKnpAFKPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ 159
Cdd:PRK14179   20 EKVAKLKEEK--GIVPGLVVILVGDNPASQVYVRNkerSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQ 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 160 --ISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAAL- 236
Cdd:PRK14179   98 lpLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNIVGKPMa 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360955 237 QCLFQRKGSMTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14179  176 QLLLDKNATVTLT-HSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVID 228
PRK14184 PRK14184
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 83-290 4.27e-16

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


Pssm-ID: 237635 [Multi-domain]  Cd Length: 286  Bit Score: 79.43  E-value: 4.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  83 KEVLSLLQEKNPAfkPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQ 159
Cdd:PRK14184   19 TEVAALTARHGRA--PGLAVILVGEDPASQVYVRNkerACEDAGIVSEAFRLPADTTQEELEDLIAELNARPDIDGILLQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 160 IS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQ 237
Cdd:PRK14184   97 LPlpKGLDSQRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNIVGKPLA 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217360955 238 CLFQRKGSM---TMSI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14184  175 LMLGAPGKFanaTVTVcHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVD 231
PRK14182 PRK14182
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 97-290 5.42e-15

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


Pssm-ID: 172670 [Multi-domain]  Cd Length: 282  Bit Score: 75.83  E-value: 5.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDD---NLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 171
Cdd:PRK14182   30 QTGLTVVRVGDDpasAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPlpKHVDERAVLD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 172 ALKPEKDVDGVTDINLGKL---VRGDAHECfvspVAKAVIELLEKSGVNLDGKKILVVGAH---GSLEAALqcLFQRKGS 245
Cdd:PRK14182  110 AISPAKDADGFHPFNVGALsigIAGVPRPC----TPAGVMRMLDEARVDPKGKRALVVGRSnivGKPMAMM--LLERHAT 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217360955 246 MTMSiQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14182  184 VTIA-HSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVID 227
PRK14171 PRK14171
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 73-298 3.56e-14

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172659 [Multi-domain]  Cd Length: 288  Bit Score: 73.45  E-value: 3.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  73 SIVREVIQNSKEVLSLLQEKNPAfKPVLAIIQAGDDN-----LMQEINQnlAEEAGLNITHICLPPDSSEAEIIDEILKI 147
Cdd:PRK14171    9 ALANEILADLKLEIQELKSQTNA-SPKLAIVLVGDNPasiiyVKNKIKN--AHKIGIDTLLVNLSTTIHTNDLISKINEL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 148 NEDTRVHGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEKSGVNLDGKKILV 225
Cdd:PRK14171   86 NLDNEISGIIVQLPlpSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTGKNVVI 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217360955 226 VGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSG 298
Cdd:PRK14171  165 IGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISG 237
PRK14185 PRK14185
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 97-290 8.53e-14

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 184556 [Multi-domain]  Cd Length: 293  Bit Score: 72.55  E-value: 8.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  97 KPVLAIIQAGDDNLMQEINQN---LAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 171
Cdd:PRK14185   31 RPHLAAILVGHDGGSETYVANkvkACEECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGFIVQLPlpKHISEQKVIE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 172 ALKPEKDVDGVTDINLGKLVRGdaHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRK---GSMTM 248
Cdd:PRK14185  111 AIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETSGKKCVVLGRSNIVGKPMAQLMMQKaypGDCTV 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217360955 249 SI-QWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14185  189 TVcHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVID 231
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 82-300 9.03e-14

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


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 72.37  E-value: 9.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  82 SKEVLSLLQEKNPAFK-----PVLAIIQAGDDNLMQEINQNLA---EEAGLNITHICLPPDSSEAEIIDEILKINEDTRV 153
Cdd:PRK14166   10 SAKIKEELKEKNQFLKskgieSCLAVILVGDNPASQTYVKSKAkacEECGIKSLVYHLNENTTQNELLALINTLNHDDSV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 154 HGLALQIS--ENLFSNKVLNALKPEKDVDGVTDINLGKLVRGdAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGS 231
Cdd:PRK14166   90 HGILVQLPlpDHICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNI 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 232 LEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFL-SGKV 300
Cdd:PRK14166  169 VGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLeSGKI 238
PRK14181 PRK14181
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ...
 98-290 4.74e-13

bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;


Pssm-ID: 172669 [Multi-domain]  Cd Length: 287  Bit Score: 70.28  E-value: 4.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955  98 PVLAIIQAGDDNlMQEINQNLAEEAGLNITHIC----LPPDSSEAEIIDEILKINEDTRVHGLALQIS--ENLFSNKVLN 171
Cdd:PRK14181   27 PGLAVVLIGNDP-ASEVYVGMKVKKATDLGMVSkahrLPSDATLSDILKLIHRLNNDPNIHGILVQLPlpKHLDAQAILQ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360955 172 ALKPEKDVDGVTDINLGKLVRGDAhECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMS-- 249
Cdd:PRK14181  106 AISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLMQKHPDTNAtv 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217360955 250 --IQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLN 290
Cdd:PRK14181  185 tlLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVD 227
 
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

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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