|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
310-910 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 995.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 310 LNLKTPVPSDIDISRSCKPKPIGSLAREIGLLSEEVELYGDTKAKVLLSALERLKHQPDGKYVVVTGITPTPLGEGKSTT 389
Cdd:PLN02759 10 LEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKSTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 390 TIGLVQALGAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMFHELT 469
Cdd:PLN02759 90 TIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 470 QTDKALFNRLVPS-VNGVRKFSDIQIRRLQRLGIEKTDPTTLTDDEINRFARLDIDPETITWQRVLDTNDRFLRKITIGQ 548
Cdd:PLN02759 170 QSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVGQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 549 APTEKGHTRTAQFDISVASEIMAVLALTSSLEDMRERLSKMVVASSKKGEPISTEDLGVSGALTVLMKDAIKPNLMQTLE 628
Cdd:PLN02759 250 GPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 629 GTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHG 708
Cdd:PLN02759 330 GTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMHG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 709 GGPMVTAGLPLPEAYIVENLELVEKGFSNLKKQIENARMFGVPVVVAVNAFKTDTEAELDLVSRLAKEHGAFDAVKCTHW 788
Cdd:PLN02759 410 GGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTHH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 789 AEGGMGALALAQAVQRAAQAPSS-FQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKT 867
Cdd:PLN02759 490 AHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAKT 569
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1953407776 868 HLSLSHNPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTIASL 910
Cdd:PLN02759 570 QYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTM 612
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
317-907 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 954.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 317 PSDIDISRSCKPKPIGSLAREIGLLSEEVELYGDTKAKVLLSALERLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQA 396
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 397 LGaHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMFHEltqtdkalf 476
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHG--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 477 nrlvpsvngvrkfsdiqirrlqrlgiektdpttltddeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHT 556
Cdd:pfam01268 151 ------------------------------------------NELDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 557 RTAQFDISVASEIMAVLALTSSLEDMRERLSKMVVASSKKGEPISTEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHA 636
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 637 GPFANIAHGNSSIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPMvtag 716
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGGVGK---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 717 lplpEAYIVENLELVEKGFSNLKKQIENARMFGVPVVVAVNAFKTDTEAELDLVSRLAKEhGAFDAVKCTHWAEGGMGAL 796
Cdd:pfam01268 342 ----DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCEA-GGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 797 A-LAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNP 875
Cdd:pfam01268 417 ElAEAVVEACEEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590
....*....|....*....|....*....|..
gi 1953407776 876 EQKGVPTGFVLPIRDIRASVGAGFLYPLVGTI 907
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDI 528
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
331-907 |
0e+00 |
|
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: 924.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 331 IGSLAREIGLLSEEVELYGDTKAKVLLSALERLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLhQNVFACVR 410
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALG-KKAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 411 QPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMFHEltqtdkalfnrlvpsvngvrkfs 490
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHE----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 491 diqirrlqrlgiektdpttltddeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHTRTAQFDISVASEIM 570
Cdd:cd00477 137 ----------------------------NTLDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 571 AVLALTSSLEDMRERLSKMVVASSKKGEPISTEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSII 650
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 651 ADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPMVTAGlplpeayiVENLEL 730
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 731 VEKGFSNLKKQIENARMFGVPVVVAVNAFKTDTEAELDLVSRLAKEHGAFDAVkCTHWAEGGMGALALAQAVQRAAQAP- 809
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPk 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 810 SSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFVLPIR 889
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570
....*....|....*...
gi 1953407776 890 DIRASVGAGFLYPLVGTI 907
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDI 514
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
304-910 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 918.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 304 MIQYNNLNLKTPVPSDIDISRSCKPKPIGSLAREIGLLSEEVELYGDTKAKVLLSALERLKHQPDGKYVVVTGITPTPLG 383
Cdd:PTZ00386 3 PMTTRKLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 384 EGKSTTTIGLVQALGAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDAR 463
Cdd:PTZ00386 83 EGKSTTTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 464 MFHELTQTDKALFNRLVpsvNGVRKFSDIQIRRLQRLGIEKTDPTTLTDDEINRFARLDIDPETITWQRVLDTNDRFLRK 543
Cdd:PTZ00386 163 IFHERTQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 544 ITIGQAPTEKGHTRTAQFDISVASEIMAVLALTSSLEDMRERLSKMVVASSKKGEPISTEDLGVSGALTVLMKDAIKPNL 623
Cdd:PTZ00386 240 ITIGQGKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 624 MQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRA 703
Cdd:PTZ00386 320 MQTLEGTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 704 LKMHGGGPMVTAGlplpeayiVENLELVEKGFSNLKKQIENARMFGVPVVVAVNAFKTDTEAELDLVSRLA-KEHGAFDA 782
Cdd:PTZ00386 400 LKFHGGVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 783 VKCTHWAEGGMGALA-LAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLP 861
Cdd:PTZ00386 472 VVTDHWAKGGAGAVDlAQALIRVTENVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFP 551
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1953407776 862 ICMAKTHLSLSHNPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTIASL 910
Cdd:PTZ00386 552 VCMAKTQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTM 600
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
316-907 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 849.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 316 VPSDIDISRSCKPKPIGSLAREIGLLSEEVELYGDTKAKVLLSALERLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQ 395
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 396 ALGaHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMFHEltqtdkal 475
Cdd:COG2759 81 ALN-RLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 476 fnrlvpsvngvrkfsdiqirrlqrlgiektdpttltddeiNRfarLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGH 555
Cdd:COG2759 152 ----------------------------------------NE---LNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 556 TRTAQFDISVASEIMAVLALTSSLEDMRERLSKMVVASSKKGEPISTEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVH 635
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 636 AGPFANIAHGNSSIIADRIALKLVgpeGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPmvta 715
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKLA---DYVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 716 glplPEAYIVENLELVEKGFSNLKKQIENARMFGVPVVVAVNAFKTDTEAELDLVSRLAKEHGAfDAVKCTHWAEGGMGA 795
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 796 LA-LAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHN 874
Cdd:COG2759 417 EElAEAVVEACEEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590
....*....|....*....|....*....|...
gi 1953407776 875 PEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTI 907
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDI 529
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
315-907 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 722.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 315 PVPSDIDISRSCKPKPIGSLAREIGLLSEEVELYGDTKAKVLLSALERLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLV 394
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 395 QALgAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMFHeltqtdka 474
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQ-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 475 lfnrlvpsvngvrkfsdiqirrlqrlGIEktdpttltddeinrfarLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKG 554
Cdd:PRK13505 152 --------------------------GNE-----------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 555 HTRTAQFDISVASEIMAVLALTSSLEDMRERLSKMVVASSKKGEPISTEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFV 634
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 635 HAGPFANIAHGNSSIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPmvT 714
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL---ADYVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVA--K 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 715 AGLPlpeayiVENLELVEKGFSNLKKQIENARMFGVPVVVAVNAFKTDTEAELDLVSRLAKEHGAfDAVKCTHWAEGGMG 794
Cdd:PRK13505 344 DDLK------EENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 795 ALALAQA-VQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSH 873
Cdd:PRK13505 417 GVELAEKvVELIEEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590
....*....|....*....|....*....|....
gi 1953407776 874 NPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTI 907
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDI 530
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
318-907 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 721.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 318 SDIDISRSCKPKPIGSLAREIGLLSEEVELYGDTKAKVLLSALERLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQAL 397
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 398 gAHLHQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMFHEltqtdkalfn 477
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 478 rlvpsvngvrkfsdiqirrlQRLGIEK-TDPTTLtddeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHT 556
Cdd:PRK13506 152 --------------------QRLGYDAfEAQSGL--------PALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 557 RTAQFDISVASEIMAVLALTSSLEDMRERLSKMVVASSKKGEPISTEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHA 636
Cdd:PRK13506 204 REDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 637 GPFANIAHGNSSIIADRIALKLVGpegFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPMVTAG 716
Cdd:PRK13506 284 GPFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 717 LPLPEAYIVENLELVEKGFSNLKKQIENARMFGVPVVVAVNAFKTDTEAELDLVSRLAKEHGAFDAVKCTHWAEGGMGAL 796
Cdd:PRK13506 361 QALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGAT 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 797 ALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPE 876
Cdd:PRK13506 441 ALAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPA 520
|
570 580 590
....*....|....*....|....*....|.
gi 1953407776 877 QKGVPTGFVLPIRDIRASVGAGFLYPLVGTI 907
Cdd:PRK13506 521 LKGAPTDFEVPIRELRLCAGAGFITALVGNV 551
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
329-907 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 659.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 329 KPIGSLAREIGLLSEEVELYGDTKAKV-LLSALERLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAhLHQNVFA 407
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVdFRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGLGK-RGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 408 CVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARMFHEltqtdkalfnrlvpsvngvR 487
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHE-------------------R 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 488 KFSDIQirrLQRLGIektdpttltddeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHTRTAQFDISVAS 567
Cdd:PRK13507 162 NYTDEQ---LARRGL----------------KRLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 568 EIMAVLALTSSLEDMRERLSKMVVASSKKGEPISTEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 647
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 648 SIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLRPHVVVLVATVRALKMHGGGPMVTAGLPLPEAYIVEN 727
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 728 LELVEKGFSNLKKQIENARMFGVPVVVAVNAFKTDTEAELDLVSRLAKEHGAFDAVKcTHWAEGGMGALALAQAVQRAAQ 807
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 808 APSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQG-FGNLPICMAKTHLSLSHNPEQKGVPTGFVL 886
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580
....*....|....*....|.
gi 1953407776 887 PIRDIRASVGAGFLYPLVGTI 907
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDI 559
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
3-293 |
1.97e-141 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 422.50 E-value: 1.97e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 3 PAEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVL 82
Cdd:COG0190 2 MAQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 83 KYVTSLNEDLTVHGFIVQLPLdsenP--INTEAVINAIVPEKDVDGLTSISAGKLARGDlkDCFIPCTPKGCLELIKETG 160
Cdd:COG0190 80 ALIDELNADPSVHGILVQLPL----PkhIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 161 VQIAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY 240
Cdd:COG0190 154 IDLAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1953407776 241 IPDDtkpngrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:COG0190 234 VEDG------KLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
1.22e-113 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 350.08 E-value: 1.22e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPLPKH--IDEKAVIERISPEKDVDGFHPINVGRMMLG--QDTFLPCTPHGILELLKEYNIDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIpd 243
Cdd:PRK14190 157 SGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRL-- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953407776 244 dtkPNGrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14190 235 ---ENG-KLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
6.66e-109 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 338.47 E-value: 6.66e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 3 PAEILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVL 82
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAH-GVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 83 KYVTSLNEDLTVHGFIVQLPLdsENPINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQ 162
Cdd:PRK14188 80 ALIARLNADPAIHGILVQLPL--PKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATG--ETALVPCTPLGCMMLLRRVHGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 163 IAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIP 242
Cdd:PRK14188 156 LSGLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1953407776 243 DDTKPNGR-KVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14188 236 APEKGEGKtRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-293 |
2.59e-102 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 323.49 E-value: 2.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 2 APAEILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEV 81
Cdd:PLN02616 71 GGAKVIDGKAVAKKIRDEITIEVSRMKESI-GVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 82 LKYVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDLKDCFIPCTPKGCLELIKETGV 161
Cdd:PLN02616 150 LKFISGFNNDPSVHGILVQLPLPSH--MDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 162 QIAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYI 241
Cdd:PLN02616 228 EIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPV 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1953407776 242 PDDTKPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PLN02616 308 EDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
4-293 |
3.89e-98 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 310.29 E-value: 3.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKH-GKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDLKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLPKH--INEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPD 243
Cdd:PLN02516 166 KGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953407776 244 DTKPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PLN02516 246 PSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-297 |
3.93e-98 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 309.54 E-value: 3.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 3 PAEILNGKVVSAQIRERLKNEVTQMKEQvpGF-IPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEV 81
Cdd:PRK10792 2 TAKIIDGKTIAQQVRSEVAQKVQARVAA--GLrAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 82 LKYVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDLKdcFIPCTPKGCLELIKETGV 161
Cdd:PRK10792 80 LALIDELNADPTIDGILVQLPLPAH--IDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPL--LRPCTPRGIMTLLERYGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 162 QIAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYI 241
Cdd:PRK10792 156 DTYGLNAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953407776 242 PDDtkpngrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRFLEK 297
Cdd:PRK10792 236 EDG------KLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-293 |
3.01e-94 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 299.29 E-value: 3.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 3 PAEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVL 82
Cdd:PRK14189 2 TAQLIDGNALSKQLRAEAAQRAAALTAR--GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 83 KYVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQ 162
Cdd:PRK14189 80 ARIDELNRDPKIHGILVQLPLPKH--IDSHKVIEAIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLESIGIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 163 IAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINyip 242
Cdd:PRK14189 156 LRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMN--- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1953407776 243 ddtKPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14189 233 ---RDDAGKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-293 |
2.60e-92 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 296.49 E-value: 2.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAV-GKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDLKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQH--LDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPD 243
Cdd:PLN02897 213 AGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953407776 244 DTKPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKR 342
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
120-292 |
8.81e-91 |
|
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: 285.22 E-value: 8.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 120 PEKDVDGLTSISAGKLARGDlkDCFIPCTPKGCLELIKETGVQIAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKT 199
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 200 ANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPDdtkPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMT 279
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPD---KSGGKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 1953407776 280 VAMLMQSTVESAK 292
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
4-297 |
4.25e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 282.80 E-value: 4.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQvPGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEE-KGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLdsENPINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14179 81 LIERYNQDPTWHGILVQLPL--PKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYipD 243
Cdd:PRK14179 157 EGKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNR--D 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1953407776 244 DtkpNGrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRFLEK 297
Cdd:PRK14179 235 E---NG-KLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSLHK 284
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
6.31e-87 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 280.03 E-value: 6.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 3 PAEILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVL 82
Cdd:PRK14186 1 MALILDGKALAAEIEQRLQAQIESNLPKA-GRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 83 KYVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGD--LKDCfipcTPKGCLELIKETG 160
Cdd:PRK14186 80 ALIAQLNQDERVDGILLQLPLPKH--LDEVPLLHAIDPDKDADGLHPLNLGRLVKGEpgLRSC----TPAGVMRLLRSQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 161 VQIAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY 240
Cdd:PRK14186 154 IDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1953407776 241 IPDDTKPNgrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14186 234 LPSSDGKT--RLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-297 |
9.85e-86 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 276.65 E-value: 9.85e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14191 3 LLDGKALSYKIEKDLKNKIQILTAQT-GKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLPRH--IDTKMVLEAIDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPDDt 245
Cdd:PRK14191 158 KDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1953407776 246 kpngrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRFLEK 297
Cdd:PRK14191 237 -----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRK 283
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
128-295 |
2.24e-83 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 265.48 E-value: 2.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 128 TSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQIAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVN 207
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 208 KGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPDDtkpngrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQST 287
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNG------KLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 1953407776 288 VESAKRFL 295
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-291 |
3.17e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 270.16 E-value: 3.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQVPGFiPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQHNLF-PCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLdsENPINTEAVINAIVPEKDVDGLTSISAGKLARGDLKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14187 83 NELNNDDSVHGILVQLPV--PNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPDDT 245
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1953407776 246 KpngRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14187 241 V---KKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-294 |
6.92e-83 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 269.38 E-value: 6.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAYRAKT-GKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDLKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLPKQ--IDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLL----WNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYI 241
Cdd:PRK14174 160 KHCVVVGRSNIVGKPMANLMLqklkESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1953407776 242 PDDTKPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRF 294
Cdd:PRK14174 240 EDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-292 |
8.94e-82 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 265.88 E-value: 8.94e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 5 EILNGKVVSAQIRERLKNEVTQMKEQVPGfIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKY 84
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGLS-IPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 85 VTSLNEDLTVHGFIVQLPLdsENPINTEAVINAIVPEKDVDGLTSISAGKLARGDlkDCFIPCTPKGCLELIKETGVQIA 164
Cdd:PRK14172 82 IEELNKDNNVHGIMLQLPL--PKHLDEKKITNKIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 165 GRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIpdd 244
Cdd:PRK14172 158 GKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV--- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1953407776 245 tkpNGrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14172 235 ---NG-KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK 278
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-292 |
3.75e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 262.09 E-value: 3.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 1 MAPAEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESE 80
Cdd:PRK14194 1 LMSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 81 VLKYVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETG 160
Cdd:PRK14194 79 LLALIAELNADPSVNGILLQLPLPAH--IDEARVLQAINPLKDVDGFHSENVGGLSQG--RDVLTPCTPSGCLRLLEDTC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 161 VQIAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY 240
Cdd:PRK14194 155 GDLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINR 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1953407776 241 IPDDtkpnGR-KVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14194 235 IDDD----GRsRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-293 |
5.34e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 258.47 E-value: 5.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKE--GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14170 80 VVEELNEDKTIHGILVQLPLPEH--ISEEKVIDTISYDKDVDGFHPVNVGNLFIG--KDSFVPCTPAGIIELIKSTGTQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINyipd 243
Cdd:PRK14170 156 EGKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD---- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953407776 244 dtKPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14170 232 --RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
2.07e-78 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 256.86 E-value: 2.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14193 3 AIILDGKATADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14193 81 VIDELNADPACTGYIVQLPLPKH--LDENAVLERIDPAKDADGLHPTNLGRLVLN--EPAPLPCTPRGIVHLLRRYDVEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNH--ATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYI 241
Cdd:PRK14193 157 AGAHVVVIGRGVTVGRPIGLLLTRRSenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1953407776 242 PDDtkpngrKVVGDVAyNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14193 237 GDG------KLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-295 |
1.59e-77 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 254.73 E-value: 1.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQvPGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERLKSN-RGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDlkDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14176 89 DSLNKRKDVHGILLQLPLPKH--LDPQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGInyipddT 245
Cdd:PRK14176 165 KNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGI------T 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953407776 246 KPNGrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRFL 295
Cdd:PRK14176 239 KEED-KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-291 |
1.59e-77 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 255.09 E-value: 1.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDA--GVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLdsENPINTEAVINAIVPEKDVDGLTSISAGKLARGDLKdcFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14167 80 TIDELNADEDVHGILVQMPV--PDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWN----HATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGIN 239
Cdd:PRK14167 156 EGADVVVVGRSDIVGKPMANLLIQKadggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1953407776 240 YIPDDTKpNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14167 236 RVDADTE-KGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-292 |
1.63e-77 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 254.32 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQvPGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTAR-HGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14184 82 AELNARPDIDGILLQLPLPKG--LDSQRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLL----WNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYI 241
Cdd:PRK14184 158 KKAVVVGRSNIVGKPLALMLGapgkFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1953407776 242 PDDtkpngrkVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14184 238 DDG-------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWK 281
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-300 |
2.23e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 254.13 E-value: 2.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQVPGfIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETIEERKTKNKR-IPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14177 84 DKLNLDPNVDGILLQHPVPSQ--IDERAAFDRIALEKDVDGVTTLSFGKLSMG--VETYLPCTPYGMVLLLKEYGIDVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINyiPDDt 245
Cdd:PRK14177 160 KNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGN- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1953407776 246 kpngrkvVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKrflEKFKP 300
Cdd:PRK14177 237 -------VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK---EHFTP 281
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-292 |
4.98e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 250.15 E-value: 4.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQmkeqvPGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEIIE-----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLPKG--VDTERVIAAILPEKDVDGFHPLNLGRLVSG--LPGFAPCTPNGIMTLLHEYKISIAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIpddt 245
Cdd:PRK14178 153 KRAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV---- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1953407776 246 kpNGrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14178 229 --NG-KLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-292 |
5.99e-76 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 250.33 E-value: 5.99e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSK--GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdLKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14166 81 NTLNHDDSVHGILVQLPLPDH--ICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIpddt 245
Cdd:PRK14166 158 KDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRL---- 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1953407776 246 kpNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14166 234 --ESGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
6.10e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 250.22 E-value: 6.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 3 PAEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVL 82
Cdd:PRK14175 2 VAKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 83 KYVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDlkDCFIPCTPKGCLELIKETGVQ 162
Cdd:PRK14175 80 NELNRLNNDDSVSGILVQVPLPKQ--VSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 163 IAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGinYIP 242
Cdd:PRK14175 156 LEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG--NTP 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1953407776 243 DDtkpNGrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14175 234 DE---NG-KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKM 280
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-297 |
6.81e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 250.52 E-value: 6.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 5 EILNGKVVSAQIRERLKNEVTQMKEQvPGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKY 84
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAK-GGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 85 VTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQIA 164
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLPKH--ISEQKVIEAIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 165 GRHAVVVGRSKIVGAPMHDLLLWNH----ATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY 240
Cdd:PRK14185 157 GKKCVVLGRSNIVGKPMAQLMMQKAypgdCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953407776 241 IPDDTKPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRFLEK 297
Cdd:PRK14185 237 VPDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIYK 293
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-293 |
8.16e-76 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 249.94 E-value: 8.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR--GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdLKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14182 81 ARLNADPAVHGILVQLPLPKH--VDERAVLDAISPAKDADGFHPFNVGALSIG-IAGVPRPCTPAGVMRMLDEARVDPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPDDt 245
Cdd:PRK14182 158 KRALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1953407776 246 kpngrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14182 237 -----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
3.76e-75 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 248.21 E-value: 3.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSaqirERLKNEVTQMKEQVPgFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14173 3 ARELSGPPAA----EAVYAELRARLAKLP-FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSENPINteAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14173 78 LIARLNADPEVDGILVQLPLPPHIDFQ--RVLEAIDPLKDVDGFHPLNVGRLWMG--GEALEPCTPAGVVRLLKHYGIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPD 243
Cdd:PRK14173 154 AGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1953407776 244 DtkpNGR-KVVGDVAyNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14173 234 N---GGRdILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALR 280
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-292 |
3.78e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 248.33 E-value: 3.78e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQT-NASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLdsENPINTEAVINAIVPEKDVDGLTSISAGKLARGdLKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14171 83 NELNLDNEISGIIVQLPL--PSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIpddt 245
Cdd:PRK14171 160 KNVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI---- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1953407776 246 kpNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14171 236 --SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK 280
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-295 |
2.02e-73 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 243.20 E-value: 2.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 5 EILNGKVVSAQIRERLKNEVTQMKeQVPGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKY 84
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDELK-LVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 85 VTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQIA 164
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLPKH--IDTTKILEAIDPKKDVDGFHPYNVGRLVTG--LDGFVPCTPLGVMELLEEYEIDVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 165 GRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPDD 244
Cdd:PRK14183 157 GKDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1953407776 245 tkpngrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRFL 295
Cdd:PRK14183 237 ------RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-292 |
6.88e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 242.47 E-value: 6.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKY-GKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDLKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14168 82 LIDKYNNDDSIHGILVQLPLPKH--INEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLVRSGVET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWN----HATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGIN 239
Cdd:PRK14168 160 SGAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1953407776 240 YIpdDTKPNGRKVV--GDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14168 240 RV--GTNESTGKAIlsGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-294 |
1.65e-72 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 240.92 E-value: 1.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQvpgfiPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14181 2 LLKGAPAAEHILATIKENISASSTA-----PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDLkDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLPKH--LDAQAILQAISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNH----ATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYI 241
Cdd:PRK14181 154 RHVAIVGRSNIVGKPLAALLMQKHpdtnATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1953407776 242 PDDTkPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRF 294
Cdd:PRK14181 234 PAAN-PKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-295 |
2.26e-72 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 240.52 E-value: 2.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEALKAKT-GRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDlkDCFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14192 82 KIEELNANPDVHGILLQHPVPAQ--IDERACFDAISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINyipd 243
Cdd:PRK14192 158 AGKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFH---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1953407776 244 dtkPNGRKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRFL 295
Cdd:PRK14192 234 ---PRDGGGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-293 |
3.52e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 237.15 E-value: 3.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 4 AEILNGKVVSAQIRERLKNEVTQMKEQvpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLK 83
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 84 YVTSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGdlKDCFIPCTPKGCLELIKETGVQI 163
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPLPAG--LDEQAVIDAIDPDKDVDGFSPVSVGRLWAN--EPTVVASTPYGIMALLDAYDIDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 164 AGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPD 243
Cdd:PRK14169 155 AGKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGAD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953407776 244 DtkpngrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14169 235 G------KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-294 |
7.62e-70 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 233.38 E-value: 7.62e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 6 ILNGKVVSAQIRERLKNEVTQMKEQVpGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYV 85
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHT-AITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 86 TSLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVDGLTSISAGKLARGDlKDCFIPCTPKGCLELIKETGVQIAG 165
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPAH--INKNNVIYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 166 RHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYIPDdt 245
Cdd:PRK14180 159 AYAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDG-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1953407776 246 kpngrKVVGDVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAKRF 294
Cdd:PRK14180 237 -----KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQEL 280
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
145-292 |
1.02e-53 |
|
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: 183.48 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 145 IPCTPKGCLELIKET-------GVQIAGRHAVVVGRSKIVGAPMHDLLLWNHATVTTCHSKTANLSEEVNKGDILVVATG 217
Cdd:cd05212 1 GPCTPLFVSPVAKAVkellnkeGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953407776 218 QPEMVKGEWIKPGAIVIDCGINYipddtkpngrkvvgdVAYNEAKERAGFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTK---------------LSGDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
7-125 |
4.04e-45 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 157.95 E-value: 4.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 7 LNGKVVSAQIRERLKNEVTQMKEqvPGFIPGLAILQVGDRDDSNLYINVKLKAAEEIGIRATHIKLPKTATESEVLKYVT 86
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKA--GGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALID 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1953407776 87 SLNEDLTVHGFIVQLPLDSEnpINTEAVINAIVPEKDVD 125
Cdd:pfam00763 79 KLNADPSVHGILVQLPLPKH--IDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
120-288 |
5.88e-11 |
|
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 62.83 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 120 PEKDVDGLTSISAGKLARG-------DLKDCFIPCTPKGCLELIKETGV---------QIAGRHAVVVGRSKIVGAPMHD 183
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYHNirfldpeNRKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 184 LLLWNHATV---------------------TTCHSKTANLSEEVNKGDILVVATGQPEM-VKGEWIKPGAIVID-CGINY 240
Cdd:cd01079 81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINfASIKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953407776 241 IPDDtkpngrkvvgdvayneAKERAGFITPVpggVGPMTVAMLMQSTV 288
Cdd:cd01079 161 FEPS----------------VKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| NAD_bind_amino_acid_DH |
cd05191 |
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ... |
147-237 |
3.23e-09 |
|
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133449 [Multi-domain] Cd Length: 86 Bit Score: 54.69 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953407776 147 CTPKGCLELIKETGV----QIAGRHAVVVGRsKIVGAPMHDLLLWNH-ATVTTCHSktanlseevnkgDILVVATGQPEM 221
Cdd:cd05191 1 ATAAGAVALLKAAGKvtnkSLKGKTVVVLGA-GEVGKGIAKLLADEGgKKVVLCDR------------DILVTATPAGVP 67
|
90
....*....|....*....
gi 1953407776 222 VKGE---WIKPGAIVIDCG 237
Cdd:cd05191 68 VLEEataKINEGAVVIDLA 86
|
|
| |
