|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
310-935 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1067.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 310 LNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLGEGKSTT 389
Cdd:PLN02759 10 LEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKSTT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 390 TIGLVQALGAHLYQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELT 469
Cdd:PLN02759 90 TIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 470 QTDKALFNRLVPS-VNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRFLRKITIGQ 548
Cdd:PLN02759 170 QSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVGQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 549 APTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLE 628
Cdd:PLN02759 250 GPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTLE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 629 GTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHG 708
Cdd:PLN02759 330 GTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMHG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 709 GGPTVTAGLPLPKAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAFDAVKCTHW 788
Cdd:PLN02759 410 GGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTHH 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 789 AEGGKGALALAQAVQRAAQAPSS-FQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKT 867
Cdd:PLN02759 490 AHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAKT 569
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 222136639 868 HLSLSHNPEQKGVPTGFILPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF 935
Cdd:PLN02759 570 QYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
317-935 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 1003.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 317 PSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQA 396
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 397 LGaHLYQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEltqtdkalf 476
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHG--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 477 nrlvpsvngvrrfsdiqirrlkrlgiektdpttltdeeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHT 556
Cdd:pfam01268 151 ------------------------------------------NELDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 557 RTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHA 636
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 637 GPFANIAHGNSSIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTvtag 716
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGGVGK---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 717 lplpKAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREhGAFDAVKCTHWAEGGKGAL 796
Cdd:pfam01268 342 ----DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCEA-GGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 797 A-LAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNP 875
Cdd:pfam01268 417 ElAEAVVEACEEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 876 EQKGVPTGFILPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPEtEQVNGLF 935
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
331-934 |
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: 980.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 331 IGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYqNVFACVR 410
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 411 QPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEltqtdkalfnrlvpsvngvrrfs 490
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHE----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 491 diqirrlkrlgiektdpttltdeeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHTRTAQFDISVASEIM 570
Cdd:cd00477 137 ----------------------------NTLDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 571 AVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSII 650
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 651 ADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGlplpkayiQENLEL 730
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 731 VEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAFDAVkCTHWAEGGKGALALAQAVQRAAQAP- 809
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPk 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 810 SSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIR 889
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 222136639 890 DIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPeTEQVNGL 934
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDIDD-TGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
304-934 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 967.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 304 MIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLG 383
Cdd:PTZ00386 3 PMTTRKLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 384 EGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDAR 463
Cdd:PTZ00386 83 EGKSTTTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 464 IFHELTQTDKALFNRLVpsvNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRFLRK 543
Cdd:PTZ00386 163 IFHERTQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 544 ITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNL 623
Cdd:PTZ00386 240 ITIGQGKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 624 MQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRA 703
Cdd:PTZ00386 320 MQTLEGTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 704 LKMHGGGPTVTAGlplpkayiQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSR-EHGAFDA 782
Cdd:PTZ00386 400 LKFHGGVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELALqEGGAADV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 783 VKCTHWAEGGKGALA-LAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLP 861
Cdd:PTZ00386 472 VVTDHWAKGGAGAVDlAQALIRVTENVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFP 551
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222136639 862 ICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGL 934
Cdd:PTZ00386 552 VCMAKTQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
316-935 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 889.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 316 VPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQ 395
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 396 ALGaHLYQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEltqtdkal 475
Cdd:COG2759 81 ALN-RLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 476 fnrlvpsvngvrrfsdiqirrlkrlgiektdpttltdeeiNRfarLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGH 555
Cdd:COG2759 152 ----------------------------------------NE---LNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 556 TRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVH 635
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 636 AGPFANIAHGNSSIIADRIALKLVgpeGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPtvta 715
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKLA---DYVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 716 glplPKAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAfDAVKCTHWAEGGKGA 795
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 796 LA-LAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHN 874
Cdd:COG2759 417 EElAEAVVEACEEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222136639 875 PEQKGVPTGFILPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDpETEQVNGLF 935
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
315-935 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 758.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 315 PVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLV 394
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 395 QALgAHLYQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHeltqtdka 474
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQ-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 475 lfnrlvpsvngvrrfsdiqirrlkrlGIEktdpttltdeeinrfarLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKG 554
Cdd:PRK13505 152 --------------------------GNE-----------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 555 HTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFV 634
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 635 HAGPFANIAHGNSSIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTvt 714
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL---ADYVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVAK-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 715 aglplpKAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAfDAVKCTHWAEGGKG 794
Cdd:PRK13505 344 ------DDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 795 ALALAQA-VQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSH 873
Cdd:PRK13505 417 GVELAEKvVELIEEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222136639 874 NPEQKGVPTGFILPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDpETEQVNGLF 935
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
318-934 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 753.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 318 SDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQAL 397
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 398 gAHLYQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEltqtdkalfn 477
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 478 rlvpsvngvrrfsdiqirrlKRLGIEKTdpttltdEEINRFARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHTR 557
Cdd:PRK13506 152 --------------------QRLGYDAF-------EAQSGLPALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 558 TAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAG 637
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 638 PFANIAHGNSSIIADRIALKLVGpegFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGL 717
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 718 PLPKAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAFDAVKCTHWAEGGKGALA 797
Cdd:PRK13506 362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 798 LAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQ 877
Cdd:PRK13506 442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 222136639 878 KGVPTGFILPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVnGL 934
Cdd:PRK13506 522 KGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDIDADGEIV-GL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
329-935 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 687.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 329 KPIGKLAREIGLLSEEVELYGETKAKV-LLSALERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAhLYQNVFA 407
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVdFRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGLGK-RGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 408 CVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRlvpsvnGVR 487
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQLARR------GLK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 488 rfsdiqirrlkrlgiektdpttltdeeinrfaRLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHTRTAQFDISVAS 567
Cdd:PRK13507 175 --------------------------------RLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 568 EIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 647
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 648 SIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLPKAYIQEN 727
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 728 LELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAFDAVKcTHWAEGGKGALALAQAVQRAAQ 807
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 808 APSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQG-FGNLPICMAKTHLSLSHNPEQKGVPTGFIL 886
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 222136639 887 PIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF 935
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
3-293 |
4.93e-146 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 434.06 E-value: 4.93e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 3 PAEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVM 82
Cdd:COG0190 2 MAQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 83 KYITSLNEDSTVHGFLVQLPLDSenSINTEEVINAIAPEKDVDGLTSINAGKLARGDlnDCFIPCTPKGCLELIKETGVP 162
Cdd:COG0190 80 ALIDELNADPSVHGILVQLPLPK--HIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVP 242
Cdd:COG0190 156 LAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222136639 243 DDkkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:COG0190 236 DG------KLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
5.70e-117 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 358.55 E-value: 5.70e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPI 163
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPLPKH--IDEKAVIERISPEKDVDGFHPINVGRMMLG--QDTFLPCTPHGILELLKEYNIDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVpd 243
Cdd:PRK14190 157 SGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRL-- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 222136639 244 dkkPNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14190 235 ---ENG-KLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
1.04e-111 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 345.40 E-value: 1.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 3 PAEILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVM 82
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAH-GVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 83 KYITSLNEDSTVHGFLVQLPLdsENSINTEEVINAIAPEKDVDGLTSINAGKLARGDlnDCFIPCTPKGCLELIKETGVP 162
Cdd:PRK14188 80 ALIARLNADPAIHGILVQLPL--PKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVP 242
Cdd:PRK14188 156 LSGLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 222136639 243 DDKKPNGR-KVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14188 236 APEKGEGKtRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-297 |
2.18e-104 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 325.72 E-value: 2.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 3 PAEILNGKEISAQIRARLKNQVTQLKEQ---VPGftprLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTES 79
Cdd:PRK10792 2 TAKIIDGKTIAQQVRSEVAQKVQARVAAglrAPG----LAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 80 EVMKYITSLNEDSTVHGFLVQLPLdsENSINTEEVINAIAPEKDVDGLTSINAGKLA------RgdlndcfiPCTPKGCL 153
Cdd:PRK10792 78 ELLALIDELNADPTIDGILVQLPL--PAHIDNVKVLERIHPDKDVDGFHPYNVGRLAqripllR--------PCTPRGIM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 154 ELIKETGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIV 233
Cdd:PRK10792 148 TLLERYGIDTYGLNAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222136639 234 IDCGINYVPDDkkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEK 297
Cdd:PRK10792 228 IDVGINRLEDG------KLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-293 |
2.29e-100 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 318.10 E-value: 2.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 2 APAEILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEV 81
Cdd:PLN02616 71 GGAKVIDGKAVAKKIRDEITIEVSRMKESI-GVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 82 MKYITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGV 161
Cdd:PLN02616 150 LKFISGFNNDPSVHGILVQLPLPSH--MDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 162 PIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYV 241
Cdd:PLN02616 228 EIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPV 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 222136639 242 PDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PLN02616 308 EDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
4-293 |
2.21e-98 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 310.67 E-value: 2.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKH-GKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGVPI 163
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLPKH--INEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPD 243
Cdd:PLN02516 166 KGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 222136639 244 DKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PLN02516 246 PSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-293 |
3.00e-97 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 307.00 E-value: 3.00e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 3 PAEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVM 82
Cdd:PRK14189 2 TAQLIDGNALSKQLRAEAAQRAAALTAR--GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 83 KYITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVP 162
Cdd:PRK14189 80 ARIDELNRDPKIHGILVQLPLPKH--IDSHKVIEAIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLESIGIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINyvp 242
Cdd:PRK14189 156 LRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMN--- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222136639 243 ddkKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14189 233 ---RDDAGKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
120-292 |
3.23e-94 |
|
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: 294.46 E-value: 3.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 120 PEKDVDGLTSINAGKLARGDlnDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKT 199
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 200 AHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDdkkPNGRKVVGDVAYDEAKERASFITPVPGGVGPMT 279
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPD---KSGGKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 222136639 280 VAMLMQSTVESAK 292
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
4-297 |
1.97e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 294.35 E-value: 1.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQvPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEE-KGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLdsENSINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPI 163
Cdd:PRK14179 81 LIERYNQDPTWHGILVQLPL--PKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINyvpd 243
Cdd:PRK14179 157 EGKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMN---- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 222136639 244 dKKPNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEK 297
Cdd:PRK14179 233 -RDENG-KLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSLHK 284
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-293 |
5.34e-92 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 295.33 E-value: 5.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAV-GKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGVPI 163
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQH--LDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPD 243
Cdd:PLN02897 213 AGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 222136639 244 DKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKR 342
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
2.74e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 288.89 E-value: 2.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 3 PAEILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVM 82
Cdd:PRK14186 1 MALILDGKALAAEIEQRLQAQIESNLPKA-GRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 83 KYITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDlndcfiP----CTPKGCLELIKE 158
Cdd:PRK14186 80 ALIAQLNQDERVDGILLQLPLPKH--LDEVPLLHAIDPDKDADGLHPLNLGRLVKGE------PglrsCTPAGVMRLLRS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 159 TGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGI 238
Cdd:PRK14186 152 QQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 222136639 239 NYVPDDKKPNgrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14186 232 HRLPSSDGKT--RLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-297 |
7.37e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 284.74 E-value: 7.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14191 3 LLDGKALSYKIEKDLKNKIQILTAQT-GKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSenSINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLPR--HIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDDk 245
Cdd:PRK14191 158 KDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 222136639 246 kpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEK 297
Cdd:PRK14191 237 -----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRK 283
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-291 |
2.39e-86 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 278.25 E-value: 2.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQH-NLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLdsENSINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14187 83 NELNNDDSVHGILVQLPV--PNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDDK 245
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 222136639 246 KpngRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14187 241 V---KKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
128-295 |
5.59e-86 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 272.03 E-value: 5.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 128 TSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVN 207
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 208 KGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDDkkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQST 287
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNG------KLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 222136639 288 VESAKRFL 295
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-294 |
2.88e-84 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 272.85 E-value: 2.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAYRAKT-GKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLPKQ--IDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLL----WNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYV 241
Cdd:PRK14174 160 KHCVVVGRSNIVGKPMANLMLqklkESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 222136639 242 PDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRF 294
Cdd:PRK14174 240 EDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-292 |
2.94e-84 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 272.04 E-value: 2.94e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 5 EILNGKEISAQIRARLKNQVTQLKEQVPGfTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKY 84
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGLS-IPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 85 ITSLNEDSTVHGFLVQLPLdsENSINTEEVINAIAPEKDVDGLTSINAGKLARGDlnDCFIPCTPKGCLELIKETGVPIA 164
Cdd:PRK14172 82 IEELNKDNNVHGIMLQLPL--PKHLDEKKITNKIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 165 GRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVpdd 244
Cdd:PRK14172 158 GKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV--- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 222136639 245 kkpNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14172 235 ---NG-KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK 278
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
1.53e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 270.63 E-value: 1.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 3 PAEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVM 82
Cdd:PRK14175 2 VAKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 83 KYITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDlnDCFIPCTPKGCLELIKETGVP 162
Cdd:PRK14175 80 NELNRLNNDDSVSGILVQVPLPKQ--VSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGinYVP 242
Cdd:PRK14175 156 LEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG--NTP 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222136639 243 DDkkpNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14175 234 DE---NG-KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKM 280
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-292 |
5.73e-82 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 267.10 E-value: 5.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 1 MAPAEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESE 80
Cdd:PRK14194 1 LMSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 81 VMKYITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETG 160
Cdd:PRK14194 79 LLALIAELNADPSVNGILLQLPLPAH--IDEARVLQAINPLKDVDGFHSENVGGLSQG--RDVLTPCTPSGCLRLLEDTC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 161 VPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY 240
Cdd:PRK14194 155 GDLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINR 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 222136639 241 VPDDkkpnGR-KVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14194 235 IDDD----GRsRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-295 |
6.42e-82 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 266.29 E-value: 6.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQvPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERLKSN-RGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDlnDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14176 89 DSLNKRKDVHGILLQLPLPKH--LDPQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDdk 245
Cdd:PRK14176 165 KNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED-- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 222136639 246 kpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFL 295
Cdd:PRK14176 243 -----KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-292 |
2.72e-81 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 264.33 E-value: 2.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQvPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTAR-HGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSenSINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14184 82 AELNARPDIDGILLQLPLPK--GLDSQRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLL----WNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYV 241
Cdd:PRK14184 158 KKAVVVGRSNIVGKPLALMLGapgkFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222136639 242 PDDkkpngrkVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14184 238 DDG-------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWK 281
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-291 |
4.32e-80 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 261.63 E-value: 4.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDA--GVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLdsENSINTEEVINAIAPEKDVDGLTSINAGKLARGDLNdcFIPCTPKGCLELIKETGVPI 163
Cdd:PRK14167 80 TIDELNADEDVHGILVQMPV--PDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWN----NATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGIN 239
Cdd:PRK14167 156 EGADVVVVGRSDIVGKPMANLLIQKadggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 222136639 240 YVPDDKKpNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14167 236 RVDADTE-KGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
6.83e-79 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 258.22 E-value: 6.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKeqvpgFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14173 3 ARELSGPPAAEAVYAELRARLAKLP-----FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDlnDCFIPCTPKGCLELIKETGVPI 163
Cdd:PRK14173 78 LIARLNADPEVDGILVQLPLPPH--IDFQRVLEAIDPLKDVDGFHPLNVGRLWMGG--EALEPCTPAGVVRLLKHYGIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPD 243
Cdd:PRK14173 154 AGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222136639 244 DKkpnGR-KVVGDVAyDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14173 234 NG---GRdILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALR 280
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-300 |
1.63e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 256.82 E-value: 1.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQVPGFtPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETIEERKTKNKRI-PKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14177 84 DKLNLDPNVDGILLQHPVPSQ--IDERAAFDRIALEKDVDGVTTLSFGKLSMG--VETYLPCTPYGMVLLLKEYGIDVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINyvPDDk 245
Cdd:PRK14177 160 KNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGN- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 222136639 246 kpngrkvVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKrflEKFKP 300
Cdd:PRK14177 237 -------VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK---EHFTP 281
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
7.05e-78 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 255.32 E-value: 7.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14193 3 AIILDGKATADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLArgdLN-DCFIPCTPKGCLELIKETGVP 162
Cdd:PRK14193 81 VIDELNADPACTGYIVQLPLPKH--LDENAVLERIDPAKDADGLHPTNLGRLV---LNePAPLPCTPRGIVHLLRRYDVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 163 IAGRHAVVVGRSKIVGAPMHDLLLWN--NATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY 240
Cdd:PRK14193 156 LAGAHVVVIGRGVTVGRPIGLLLTRRseNATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 222136639 241 VPDDkkpngrKVVGDVAYDEAkERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14193 236 AGDG------KLVGDVHPDVW-EVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-292 |
8.14e-78 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 254.95 E-value: 8.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSK--GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdLNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14166 81 NTLNHDDSVHGILVQLPLPDH--ICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVpddk 245
Cdd:PRK14166 158 KDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRL---- 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 222136639 246 kpNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14166 234 --ESGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK 278
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-297 |
8.79e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 255.52 E-value: 8.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 5 EILNGKEISAQIRARLKNQVTQLKEQvPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKY 84
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAK-GGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 85 ITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPIA 164
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLPKH--ISEQKVIEAIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 165 GRHAVVVGRSKIVGAPMHDLLL----WNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY 240
Cdd:PRK14185 157 GKKCVVLGRSNIVGKPMAQLMMqkayPGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 222136639 241 VPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEK 297
Cdd:PRK14185 237 VPDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIYK 293
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-292 |
1.73e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 254.50 E-value: 1.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQT-NASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLdsENSINTEEVINAIAPEKDVDGLTSINAGKLARGdLNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14171 83 NELNLDNEISGIIVQLPL--PSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVpddk 245
Cdd:PRK14171 160 KNVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI---- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 222136639 246 kpNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14171 236 --SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK 280
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-292 |
2.54e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 253.61 E-value: 2.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQlkeqvPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEIIE-----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSenSINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLPK--GVDTERVIAAILPEKDVDGFHPLNLGRLVSG--LPGFAPCTPNGIMTLLHEYKISIAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVpddk 245
Cdd:PRK14178 153 KRAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV---- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 222136639 246 kpNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14178 229 --NG-KLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-293 |
4.51e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 253.07 E-value: 4.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKE--GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPI 163
Cdd:PRK14170 80 VVEELNEDKTIHGILVQLPLPEH--ISEEKVIDTISYDKDVDGFHPVNVGNLFIG--KDSFVPCTPAGIIELIKSTGTQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGInyvpd 243
Cdd:PRK14170 156 EGKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGM----- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 222136639 244 DKKPNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14170 231 DRDENN-KLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-295 |
2.20e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 251.30 E-value: 2.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEALKAKT-GRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDlnDCFIPCTPKGCLELIKETGVPI 163
Cdd:PRK14192 82 KIEELNANPDVHGILLQHPVPAQ--IDERACFDAISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINyvpd 243
Cdd:PRK14192 158 AGKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFH---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 222136639 244 dkkPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFL 295
Cdd:PRK14192 234 ---PRDGGGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-292 |
7.24e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 247.48 E-value: 7.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKY-GKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGVPI 163
Cdd:PRK14168 82 LIDKYNNDDSIHGILVQLPLPKH--INEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLVRSGVET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 164 AGRHAVVVGRSKIVGAPMHDLLLWN----NATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGIN 239
Cdd:PRK14168 160 SGAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 222136639 240 YV---PDDKKPNGRkvvGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:PRK14168 240 RVgtnESTGKAILS---GDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-295 |
1.17e-74 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 246.28 E-value: 1.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 5 EILNGKEISAQIRARLKNQVTQLKeQVPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKY 84
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDELK-LVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 85 ITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdlNDCFIPCTPKGCLELIKETGVPIA 164
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLPKH--IDTTKILEAIDPKKDVDGFHPYNVGRLVTG--LDGFVPCTPLGVMELLEEYEIDVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 165 GRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDD 244
Cdd:PRK14183 157 GKDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222136639 245 kkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFL 295
Cdd:PRK14183 237 ------RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-293 |
1.85e-74 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 246.09 E-value: 1.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR--GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGdLNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14182 81 ARLNADPAVHGILVQLPLPKH--VDERAVLDAISPAKDADGFHPFNVGALSIG-IAGVPRPCTPAGVMRMLDEARVDPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDDk 245
Cdd:PRK14182 158 KRALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 222136639 246 kpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14182 237 -----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-294 |
6.95e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 241.69 E-value: 6.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEqvpgfTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14181 2 LLKGAPAAEHILATIKENISASST-----APGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDLnDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLPKH--LDAQAILQAISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLW----NNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYV 241
Cdd:PRK14181 154 RHVAIVGRSNIVGKPLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 222136639 242 PDDkKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRF 294
Cdd:PRK14181 234 PAA-NPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-293 |
1.00e-72 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 241.39 E-value: 1.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 4 AEILNGKEISAQIRARLKNQVTQLKEQvpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMK 83
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 84 YITSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLArgdLND-CFIPCTPKGCLELIKETGVP 162
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPLPAG--LDEQAVIDAIDPDKDVDGFSPVSVGRLW---ANEpTVVASTPYGIMALLDAYDID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVP 242
Cdd:PRK14169 154 VAGKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 222136639 243 DDkkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKR 293
Cdd:PRK14169 234 DG------KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-294 |
1.19e-72 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 241.09 E-value: 1.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 6 ILNGKEISAQIRARLKNQVTQLKEQVpGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYI 85
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHT-AITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 86 TSLNEDSTVHGFLVQLPLDSEnsINTEEVINAIAPEKDVDGLTSINAGKLARGDlNDCFIPCTPKGCLELIKETGVPIAG 165
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPAH--INKNNVIYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDdk 245
Cdd:PRK14180 159 AYAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDG-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 222136639 246 kpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRF 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 |
2.73e-58 |
|
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: 196.19 E-value: 2.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 145 IPCTPKGCLELIKET-------GVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATG 217
Cdd:cd05212 1 GPCTPLFVSPVAKAVkellnkeGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222136639 218 QPEMVKGEWIKPGAIVIDCGINYvpddkkpngrkvvgdVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAK 292
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTK---------------LSGDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
7-125 |
2.31e-47 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 164.12 E-value: 2.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 7 LNGKEISAQIRARLKNQVTQLKEqvPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYIT 86
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKA--GGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALID 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 222136639 87 SLNEDSTVHGFLVQLPLDSenSINTEEVINAIAPEKDVD 125
Cdd:pfam00763 79 KLNADPSVHGILVQLPLPK--HIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
120-288 |
2.88e-12 |
|
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 66.68 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 120 PEKDVDGLTSINAGKLARG-------DLNDCFIPCTPKGCLELIKETGV---------PIAGRHAVVVGRSKIVGAPMHD 183
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYHNirfldpeNRKKSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 184 LLLWNNATVTTC---------------HSKTAHLDEEVNKGDIL----VVATGQPE---MVKGEWIKPGAIVID-CGINY 240
Cdd:cd01079 81 LLANDGARVYSVdingiqvftrgesirHEKHHVTDEEAMTLDCLsqsdVVITGVPSpnyKVPTELLKDGAICINfASIKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 222136639 241 VPDDkkpngrkvvgdvaydeAKERASFITPVpggVGPMTVAMLMQSTV 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 |
3.07e-10 |
|
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: 57.39 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222136639 147 CTPKGCLELIKETGV----PIAGRHAVVVGRsKIVGAPMHDLLLWN-NATVTTCHSktahldeevnkgDILVVATGQPEM 221
Cdd:cd05191 1 ATAAGAVALLKAAGKvtnkSLKGKTVVVLGA-GEVGKGIAKLLADEgGKKVVLCDR------------DILVTATPAGVP 67
|
90
....*....|....*....
gi 222136639 222 VKGE---WIKPGAIVIDCG 237
Cdd:cd05191 68 VLEEataKINEGAVVIDLA 86
|
|
| |
