|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
309-935 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1061.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 309 KLNLKTPVPSDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKST 388
Cdd:PLN02759 9 KLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEGKST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 389 TTIGLVQALGAHLRQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEL 468
Cdd:PLN02759 89 TTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVFHEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 469 TQTDKALFNRLVPS-VNGIRKFSDIQIRRLRRLGIEKTDPTTLTDDEINRFARLDIDPETITWQRVLDTNDRFLRKITIG 547
Cdd:PLN02759 169 TQSDKALFNRLCPAnKEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKITVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 548 QSPTEKGHTRTAQFDISVASEIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTL 627
Cdd:PLN02759 249 QGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLMQTL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 628 EGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMH 707
Cdd:PLN02759 329 EGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRALKMH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 708 GGGPTVTAGLPLPKAYTEEDLDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREHGAFDAVKCTH 787
Cdd:PLN02759 409 GGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVLCTH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 788 WAEGGQGALALAQAVQRASQAPSS-FQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAK 866
Cdd:PLN02759 489 HAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPICMAK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261878543 867 THLSLSHNPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF 935
Cdd:PLN02759 569 TQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
317-935 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 994.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 317 PSDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQA 396
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 397 LGaHLRQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEltqtdkalf 476
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHG--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 477 nrlvpsvngirkfsdiqirrlrrlgiektdpttltddeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQSPTEKGHT 556
Cdd:pfam01268 151 ------------------------------------------NELDIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 557 RTAQFDISVASEIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHA 636
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 637 GPFANIAHGNSSIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPTvtag 716
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGGVGK---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 717 lplpKAYTEEDLDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREhGAFDAVKCTHWAEGGQGAL 796
Cdd:pfam01268 342 ----DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELCEA-GGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 797 ALAQAVQRA-SQAPSSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAKTHLSLSHNP 875
Cdd:pfam01268 417 ELAEAVVEAcEEEPSNFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 876 EQKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPEtEQVNGLF 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: 973.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 331 IGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLRqNVFACVR 410
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 411 QPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEltqtdkalfnrlvpsvngirkfs 490
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHE----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 491 diqirrlrrlgiektdpttltddeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQSPTEKGHTRTAQFDISVASEIM 570
Cdd:cd00477 137 ----------------------------NTLDIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 571 AVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSII 650
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 651 ADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPTVTAGlplpkaytEEDLDL 730
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 731 VEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREHGAFDAVkCTHWAEGGQGALALAQAVQRASQAP- 809
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPk 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 810 SSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFVLPIR 889
Cdd:cd00477 417 SNFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 261878543 890 DIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPeTEQVNGL 934
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDIDD-TGKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
307-934 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 954.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 307 YNKLNLKTPVPSDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGK 386
Cdd:PTZ00386 6 TRKLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 387 STTTIGLVQALGAHLRQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFH 466
Cdd:PTZ00386 86 STTTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 467 ELTQTDKALFNRLVpsvNGIRKFSDIQIRRLRRLGIEKTDPTTLTDDEINRFARLDIDPETITWQRVLDTNDRFLRKITI 546
Cdd:PTZ00386 166 ERTQSDAALYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREITI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 547 GQSPTEKGHTRTAQFDISVASEIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQT 626
Cdd:PTZ00386 243 GQGKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 627 LEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKM 706
Cdd:PTZ00386 323 LEGTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 707 HGGGPTVTAGlplpkaytEEDLDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSR-EHGAFDAVKC 785
Cdd:PTZ00386 403 HGGVEPVVAG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELALqEGGAADVVVT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 786 THWAEGGQGALALAQAVQRASQ-APSSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICM 864
Cdd:PTZ00386 475 DHWAKGGAGAVDLAQALIRVTEnVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCM 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 865 AKTHLSLSHNPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGL 934
Cdd:PTZ00386 555 AKTQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 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: 878.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 316 VPSDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQ 395
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 396 ALGaHLRQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEltqtdkal 475
Cdd:COG2759 81 ALN-RLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 476 fnrlvpsvngirkfsdiqirrlrrlgiektdpttltddeiNRfarLDIDPETITWQRVLDTNDRFLRKITIGQSPTEKGH 555
Cdd:COG2759 152 ----------------------------------------NE---LNIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 556 TRTAQFDISVASEIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVH 635
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 636 AGPFANIAHGNSSIIADRIALKLVgpeGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPtvta 715
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKLA---DYVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 716 glplPKAYTEEDLDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREHGAfDAVKCTHWAEGGQGA 795
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 796 LALAQAVQRAS-QAPSSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAKTHLSLSHN 874
Cdd:COG2759 417 EELAEAVVEACeEGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261878543 875 PEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDpETEQVNGLF 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: 745.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 315 PVPSDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLV 394
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 395 QALgAHLRQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHeltqtdka 474
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQ-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 475 lfnrlvpsvngirkfsdiqirrlrrlGIEktdpttltddeinrfarLDIDPETITWQRVLDTNDRFLRKITIGQSPTEKG 554
Cdd:PRK13505 152 --------------------------GNE-----------------LGIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 555 HTRTAQFDISVASEIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFV 634
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 635 HAGPFANIAHGNSSIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPTvt 714
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL---ADYVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVAK-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 715 aglplpKAYTEEDLDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREHGAfDAVKCTHWAEGGQG 794
Cdd:PRK13505 344 ------DDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 795 ALALAQAVQR-ASQAPSSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAKTHLSLSH 873
Cdd:PRK13505 417 GVELAEKVVElIEEGESNFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261878543 874 NPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDpETEQVNGLF 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: 743.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 318 SDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQAL 397
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 398 gAHLRQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHEltqtdkalfn 477
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 478 rlvpsvngirkfsdiqirrlRRLGIEK-TDPTTLtddeinrfARLDIDPETITWQRVLDTNDRFLRKITIGQSPTEKGHT 556
Cdd:PRK13506 152 --------------------QRLGYDAfEAQSGL--------PALDIDPEQILWKRVVDHNDRALRMITVGLGENGNGPE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 557 RTAQFDISVASEIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHA 636
Cdd:PRK13506 204 REDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 637 GPFANIAHGNSSIIADRIALKLVGpegFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPTVTAG 716
Cdd:PRK13506 284 GPFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 717 LPLPKAYTEEDLDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREHGAFDAVKCTHWAEGGQGAL 796
Cdd:PRK13506 361 QALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGAT 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 797 ALAQAVQRASQAPSSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAKTHLSLSHNPE 876
Cdd:PRK13506 441 ALAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPA 520
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 261878543 877 QKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVnGL 934
Cdd:PRK13506 521 LKGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDIDADGEIV-GL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
329-935 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 682.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 329 KLIGNLAREIGLLTEEVELYGETKAKV-LLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAhLRQNVFA 407
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVdFRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGLGK-RGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 408 CVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRlvpsvnGIR 487
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDEQLARR------GLK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 488 kfsdiqirrlrrlgiektdpttltddeinrfaRLDIDPETITWQRVLDTNDRFLRKITIGQSPTEKGHTRTAQFDISVAS 567
Cdd:PRK13507 175 --------------------------------RLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 568 EIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNS 647
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 648 SIIADRIALKLvgpEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPTVTAGLPLPKAYTEED 727
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 728 LDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREHGAFDAVKcTHWAEGGQGALALAQAVQRASQ 807
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 808 APSSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAE-IYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFVL 886
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKrLESDPETADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 261878543 887 PIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF 935
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
3-293 |
2.13e-141 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 422.11 E-value: 2.13e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 3 PAGILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVL 82
Cdd:COG0190 2 MAQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 83 KYVISLNEDASVHGFIVQLPLDSenSINTEAVINAIAPEKDVDGLTSVSAGKLARGDlnDCFIPCTPKGCLELIKEAGVQ 162
Cdd:COG0190 80 ALIDELNADPSVHGILVQLPLPK--HIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVP 242
Cdd:COG0190 156 LAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261878543 243 DDtkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:COG0190 236 DG------KLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAER 280
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
1.82e-112 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 347.00 E-value: 1.82e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 4 AGILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLK 83
Cdd:PRK14190 3 AVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 84 YVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQI 163
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPLPKH--IDEKAVIERISPEKDVDGFHPINVGRMMLG--QDTFLPCTPHGILELLKEYNIDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVpd 243
Cdd:PRK14190 157 SGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRL-- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 261878543 244 dtkPNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14190 235 ---ENG-KLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKR 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
2.63e-108 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 336.54 E-value: 2.63e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 3 PAGILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVL 82
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAH-GVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 83 KYVISLNEDASVHGFIVQLPLdsENSINTEAVINAIAPEKDVDGLTSVSAGKLARGDlnDCFIPCTPKGCLELIKEAGVQ 162
Cdd:PRK14188 80 ALIARLNADPAIHGILVQLPL--PKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVP 242
Cdd:PRK14188 156 LSGLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 261878543 243 DDTKPNGR-KVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14188 236 APEKGEGKtRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-293 |
3.16e-104 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 328.50 E-value: 3.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 2 APAGILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEV 81
Cdd:PLN02616 71 GGAKVIDGKAVAKKIRDEITIEVSRMKESI-GVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 82 LKYVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNDCFIPCTPKGCLELIKEAGV 161
Cdd:PLN02616 150 LKFISGFNNDPSVHGILVQLPLPSH--MDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 162 QIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYV 241
Cdd:PLN02616 228 EIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPV 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 261878543 242 PDDTKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PLN02616 308 EDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-294 |
1.48e-98 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 310.31 E-value: 1.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 3 PAGILNGKLVSAQIRDRLKNQVTRMQEQvpGF-TPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEV 81
Cdd:PRK10792 2 TAKIIDGKTIAQQVRSEVAQKVQARVAA--GLrAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 82 LKYVISLNEDASVHGFIVQLPLdsENSINTEAVINAIAPEKDVDGLTSVSAGKLA------RgdlndcfiPCTPKGCLEL 155
Cdd:PRK10792 80 LALIDELNADPTIDGILVQLPL--PAHIDNVKVLERIHPDKDVDGFHPYNVGRLAqripllR--------PCTPRGIMTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 156 IKEAGVQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVID 235
Cdd:PRK10792 150 LERYGIDTYGLNAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVID 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 261878543 236 CGINYVPDDtkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRF 294
Cdd:PRK10792 230 VGINRLEDG------KLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEY 282
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
4-293 |
2.07e-96 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 305.28 E-value: 2.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 4 AGILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLK 83
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKH-GKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 84 YVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNDCFIPCTPKGCLELIKEAGVQI 163
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLPKH--INEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPD 243
Cdd:PLN02516 166 KGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 261878543 244 DTKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PLN02516 246 PSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-293 |
4.53e-95 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 301.22 E-value: 4.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 3 PAGILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVL 82
Cdd:PRK14189 2 TAQLIDGNALSKQLRAEAAQRAAALTAR--GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 83 KYVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQ 162
Cdd:PRK14189 80 ARIDELNRDPKIHGILVQLPLPKH--IDSHKVIEAIAPEKDVDGFHVANAGALMTG--QPLFRPCTPYGVMKMLESIGIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINyvp 242
Cdd:PRK14189 156 LRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMN--- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261878543 243 ddtKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 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 |
6.79e-93 |
|
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: 290.61 E-value: 6.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 120 PEKDVDGLTSVSAGKLARGDlnDCFIPCTPKGCLELIKEAGVQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKT 199
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 200 ANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDdtkPNGRKVVGDVAYDEAKERASFITPVPGGVGPMT 279
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPD---KSGGKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 261878543 280 VAMLMQSTVESAQ 292
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
4-293 |
1.36e-92 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 296.87 E-value: 1.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 4 AGILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLK 83
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAV-GKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 84 YVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNDCFIPCTPKGCLELIKEAGVQI 163
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLPQH--LDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPD 243
Cdd:PLN02897 213 AGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 261878543 244 DTKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKR 342
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
4.43e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 288.50 E-value: 4.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 3 PAGILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVL 82
Cdd:PRK14186 1 MALILDGKALAAEIEQRLQAQIESNLPKA-GRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 83 KYVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDlndcfiP----CTPKGCLELIKE 158
Cdd:PRK14186 80 ALIAQLNQDERVDGILLQLPLPKH--LDEVPLLHAIDPDKDADGLHPLNLGRLVKGE------PglrsCTPAGVMRLLRS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 159 AGVQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGI 238
Cdd:PRK14186 152 QQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 261878543 239 NYVPDDTKPNgrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14186 232 HRLPSSDGKT--RLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQK 284
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
6-293 |
1.13e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 284.34 E-value: 1.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQvPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14179 4 IIDGKALAQKMQAELAEKVAKLKEE-KGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLdsENSINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14179 83 ERYNQDPTWHGILVQLPL--PKHINEEKILLAIDPKKDVDGFHPMNTGHLWSG--RPVMIPCTPAGIMEMFREYNVELEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYvpDDt 245
Cdd:PRK14179 159 KHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNR--DE- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 261878543 246 kpNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14179 236 --NG-KLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALR 280
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-297 |
2.46e-86 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 277.80 E-value: 2.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14191 3 LLDGKALSYKIEKDLKNKIQILTAQT-GKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSenSINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLPR--HIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIEIKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDDt 245
Cdd:PRK14191 158 KDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 261878543 246 kpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRFLQK 297
Cdd:PRK14191 237 -----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRK 283
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-294 |
1.13e-85 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 276.70 E-value: 1.13e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14174 3 IIDGKKVSLDLKNELKTRVEAYRAKT-GKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLPKQ--IDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLL----WNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYV 241
Cdd:PRK14174 160 KHCVVVGRSNIVGKPMANLMLqklkESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 261878543 242 PDDTKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRF 294
Cdd:PRK14174 240 EDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
128-295 |
3.62e-84 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 267.41 E-value: 3.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 128 TSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVN 207
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 208 KGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDDtkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQST 287
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGNG------KLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 261878543 288 VESAQRFL 295
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-291 |
3.32e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 269.78 E-value: 3.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQH-NLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLdsENSINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14187 83 NELNNDDSVHGILVQLPV--PNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDDT 245
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 261878543 246 KpngRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14187 241 V---KKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-295 |
2.26e-82 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 267.44 E-value: 2.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 5 GILNGKLVSAQIRDRLKNQVTRMQEQvPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKY 84
Cdd:PRK14176 9 RIIDGKALAKKIEAEVRSGVERLKSN-RGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 85 VISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDlnDCFIPCTPKGCLELIKEAGVQIA 164
Cdd:PRK14176 88 IDSLNKRKDVHGILLQLPLPKH--LDPQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVDIE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 165 GRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDd 244
Cdd:PRK14176 164 GKNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261878543 245 tkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRFL 295
Cdd:PRK14176 243 ------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-292 |
3.32e-82 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 266.65 E-value: 3.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQvpGFT-PGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKY 84
Cdd:PRK14172 4 IINGKEVALKIKEEIKNFVEERKEN--GLSiPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 85 VISLNEDASVHGFIVQLPLdsENSINTEAVINAIAPEKDVDGLTSVSAGKLARGDlnDCFIPCTPKGCLELIKEAGVQIA 164
Cdd:PRK14172 82 IEELNKDNNVHGIMLQLPL--PKHLDEKKITNKIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 165 GRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVpdd 244
Cdd:PRK14172 158 GKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV--- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 261878543 245 tkpNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQ 292
Cdd:PRK14172 235 ---NG-KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK 278
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-291 |
3.57e-81 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 264.72 E-value: 3.57e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14167 4 IIDGNAVAAQIRDDLTDAIETLEDA--GVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLdsENSINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNdcFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14167 82 DELNADEDVHGILVQMPV--PDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDTEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWN----NATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYV 241
Cdd:PRK14167 158 ADVVVVGRSDIVGKPMANLLIQKadggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 261878543 242 PDDTKpNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14167 238 DADTE-KGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
1.06e-79 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 259.95 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 4 AGILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLK 83
Cdd:PRK14193 3 AIILDGKATADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 84 YVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLArgdLN-DCFIPCTPKGCLELIKEAGVQ 162
Cdd:PRK14193 81 VIDELNADPACTGYIVQLPLPKH--LDENAVLERIDPAKDADGLHPTNLGRLV---LNePAPLPCTPRGIVHLLRRYDVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 163 IAGRHAVVVGRSKIVGAPMHDLLLWN--NATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINY 240
Cdd:PRK14193 156 LAGAHVVVIGRGVTVGRPIGLLLTRRseNATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 261878543 241 VPDDtkpngrKVVGDVAYDEAkERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14193 236 AGDG------KLVGDVHPDVW-EVAGAVSPNPGGVGPMTRAFLLTNVVERAER 281
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-292 |
2.98e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 259.78 E-value: 2.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 1 MAPAGILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESE 80
Cdd:PRK14194 1 LMSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 81 VLKYVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAG 160
Cdd:PRK14194 79 LLALIAELNADPSVNGILLQLPLPAH--IDEARVLQAINPLKDVDGFHSENVGGLSQG--RDVLTPCTPSGCLRLLEDTC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 161 VQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINY 240
Cdd:PRK14194 155 GDLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINR 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 261878543 241 VPDDtkpnGR-KVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQ 292
Cdd:PRK14194 235 IDDD----GRsRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-293 |
2.52e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 256.38 E-value: 2.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 3 PAGILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVL 82
Cdd:PRK14175 2 VAKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 83 KYVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDlnDCFIPCTPKGCLELIKEAGVQ 162
Cdd:PRK14175 80 NELNRLNNDDSVSGILVQVPLPKQ--VSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGinYVP 242
Cdd:PRK14175 156 LEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG--NTP 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261878543 243 DDtkpNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14175 234 DE---NG-KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKM 280
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-290 |
1.58e-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: 1.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQvPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14184 3 LLDGKATAATIREELKTEVAALTAR-HGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSenSINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14184 82 AELNARPDIDGILLQLPLPK--GLDSQRCLELIDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLSPAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLL----WNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYV 241
Cdd:PRK14184 158 KKAVVVGRSNIVGKPLALMLGapgkFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 261878543 242 PDDtkpngrkVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVES 290
Cdd:PRK14184 238 DDG-------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-300 |
4.41e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 252.97 E-value: 4.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQVPGFtPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETIEERKTKNKRI-PKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14177 84 DKLNLDPNVDGILLQHPVPSQ--IDERAAFDRIALEKDVDGVTTLSFGKLSMG--VETYLPCTPYGMVLLLKEYGIDVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINyvPDDt 245
Cdd:PRK14177 160 KNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGN- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 261878543 246 kpngrkvVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESaqrFLQKFKP 300
Cdd:PRK14177 237 -------VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYS---FKEHFTP 281
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-293 |
2.60e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 251.15 E-value: 2.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14170 4 IIDGKKLAKEIQEKVTREVAELVKE--GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14170 82 EELNEDKTIHGILVQLPLPEH--ISEEKVIDTISYDKDVDGFHPVNVGNLFIG--KDSFVPCTPAGIIELIKSTGTQIEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINyvpddt 245
Cdd:PRK14170 158 KRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD------ 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 261878543 246 KPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14170 232 RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-296 |
5.09e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 250.15 E-value: 5.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 4 AGILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLK 83
Cdd:PRK14192 3 ALVLDGKALAKQIEEELSVRVEALKAKT-GRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 84 YVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDlnDCFIPCTPKGCLELIKEAGVQI 163
Cdd:PRK14192 82 KIEELNANPDVHGILLQHPVPAQ--IDERACFDAISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINyvpd 243
Cdd:PRK14192 158 AGKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFH---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 261878543 244 dtkPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRFLQ 296
Cdd:PRK14192 234 ---PRDGGGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-292 |
1.12e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 248.99 E-value: 1.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRmqeqvPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEIIE-----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSenSINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLPK--GVDTERVIAAILPEKDVDGFHPLNLGRLVSG--LPGFAPCTPNGIMTLLHEYKISIAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVpddt 245
Cdd:PRK14178 153 KRAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV---- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 261878543 246 kpNGrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQ 292
Cdd:PRK14178 229 --NG-KLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-297 |
1.80e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 248.98 E-value: 1.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQvPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14185 3 LIDGKAISAQIKQEIAAEVAEIVAK-GGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14185 82 RELNQDDDVDGFIVQLPLPKH--ISEQKVIEAIDYRKDVDGFHPINVGRMSIG--LPCFVSATPNGILELLKRYHIETSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLL----WNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYV 241
Cdd:PRK14185 158 KKCVVLGRSNIVGKPMAQLMMqkayPGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 261878543 242 PDDTKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRFLQK 297
Cdd:PRK14185 238 PDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIYK 293
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-296 |
2.15e-75 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 248.40 E-value: 2.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSK--GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdLNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14166 81 NTLNHDDSVHGILVQLPLPDH--ICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVpddt 245
Cdd:PRK14166 158 KDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRL---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261878543 246 kpNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRFLQ 296
Cdd:PRK14166 234 --ESGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-290 |
4.94e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 247.56 E-value: 4.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQT-NASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLdsENSINTEAVINAIAPEKDVDGLTSVSAGKLARGdLNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14171 83 NELNLDNEISGIIVQLPL--PSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVpddt 245
Cdd:PRK14171 160 KNVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI---- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 261878543 246 kpNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVES 290
Cdd:PRK14171 236 --SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-293 |
6.25e-75 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 247.24 E-value: 6.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR--GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdLNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14182 81 ARLNADPAVHGILVQLPLPKH--VDERAVLDAISPAKDADGFHPFNVGALSIG-IAGVPRPCTPAGVMRMLDEARVDPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDDt 245
Cdd:PRK14182 158 KRALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 261878543 246 kpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14182 237 -----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
6.08e-74 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 244.74 E-value: 6.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 4 AGILNGKLVSAQIRDRLKNQVTRMQeqvpgFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLK 83
Cdd:PRK14173 3 ARELSGPPAAEAVYAELRARLAKLP-----FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 84 YVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQI 163
Cdd:PRK14173 78 LIARLNADPEVDGILVQLPLPPH--IDFQRVLEAIDPLKDVDGFHPLNVGRLWMG--GEALEPCTPAGVVRLLKHYGIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 164 AGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPD 243
Cdd:PRK14173 154 AGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261878543 244 DtkpNGR-KVVGDVAyDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14173 234 N---GGRdILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALR 280
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-291 |
5.55e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 242.47 E-value: 5.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 4 AGILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLK 83
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKY-GKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 84 YVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNDCFIPCTPKGCLELIKEAGVQI 163
Cdd:PRK14168 82 LIDKYNNDDSIHGILVQLPLPKH--INEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLVRSGVET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 164 AGRHAVVVGRSKIVGAPMHDLLLWN----NATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGIN 239
Cdd:PRK14168 160 SGAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 261878543 240 YVpdDTKPNGRKVV--GDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:PRK14168 240 RV--GTNESTGKAIlsGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSA 291
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-295 |
1.34e-72 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 240.89 E-value: 1.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQeQVPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14183 3 ILDGKALSDKIKENVKKEVDELK-LVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGdlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14183 82 AMMNNNPNIDGILVQLPLPKH--IDTTKILEAIDPKKDVDGFHPYNVGRLVTG--LDGFVPCTPLGVMELLEEYEIDVKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDDt 245
Cdd:PRK14183 158 KDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDG- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 261878543 246 kpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRFL 295
Cdd:PRK14183 237 -----RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-294 |
2.17e-71 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 237.62 E-value: 2.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTRMQEQVpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHT-AITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDlNDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPAH--INKNNVIYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDdt 245
Cdd:PRK14180 159 AYAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDG-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 261878543 246 kpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRF 294
Cdd:PRK14180 237 -----KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQEL 280
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-293 |
5.15e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 236.77 E-value: 5.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 4 AGILNGKLVSAQIRDRLKNQVTRMQEQvpGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLK 83
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 84 YVISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLArgdLND-CFIPCTPKGCLELIKEAGVQ 162
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPLPAG--LDEQAVIDAIDPDKDVDGFSPVSVGRLW---ANEpTVVASTPYGIMALLDAYDID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 163 IAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVP 242
Cdd:PRK14169 154 VAGKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 261878543 243 DDtkpngrKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQR 293
Cdd:PRK14169 234 DG------KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-294 |
6.79e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 236.30 E-value: 6.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 6 ILNGKLVSAQIRDRLKNQVTrmqeQVPGfTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYV 85
Cdd:PRK14181 2 LLKGAPAAEHILATIKENIS----ASST-APGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 86 ISLNEDASVHGFIVQLPLDSEnsINTEAVINAIAPEKDVDGLTSVSAGKLARGDLnDCFIPCTPKGCLELIKEAGVQIAG 165
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLPKH--LDAQAILQAISPDKDVDGLHPVNMGKLLLGET-DGFIPCTPAGIIELLKYYEIPLHG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 166 RHAVVVGRSKIVGAPMHDLLLW----NNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYV 241
Cdd:PRK14181 154 RHVAIVGRSNIVGKPLAALLMQkhpdTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 261878543 242 PDDTkPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRF 294
Cdd:PRK14181 234 PAAN-PKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
138-291 |
3.06e-56 |
|
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: 190.41 E-value: 3.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 138 GDLNDCFIPCTPKGCLELIKEAGVQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATG 217
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261878543 218 QPEMVKGEWIKPGAVVIDCGINYvpddtkpngrkvvgdVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESA 291
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTK---------------LSGDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSV 139
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
7-125 |
2.87e-46 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 161.03 E-value: 2.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 7 LNGKLVSAQIRDRLKNQVTRMQEqvPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYVI 86
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKA--GGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALID 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 261878543 87 SLNEDASVHGFIVQLPLDSenSINTEAVINAIAPEKDVD 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 |
6.14e-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: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 120 PEKDVDGLTSVSAGKLARG-------DLNDCFIPCTPKG---CLELIK------EAGVQIAGRHAVVVGRSKIVGAPMHD 183
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYHNirfldpeNRKKSILPCTPLAivkILEFLGiynkilPYGNRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 184 LLLWNNATVTTC---------------HSKTANLDKEVNKGDIL----VVATGQPE---MVKGEWIKPGAVVID-CGINY 240
Cdd:cd01079 81 LLANDGARVYSVdingiqvftrgesirHEKHHVTDEEAMTLDCLsqsdVVITGVPSpnyKVPTELLKDGAICINfASIKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 261878543 241 VPDDtkpngrkvvgdvaydeAKERASFITPVpggVGPMTVAMLMQSTV 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 |
3.52e-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: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878543 147 CTPKGCLELIKEAGV----QIAGRHAVVVGRsKIVGAPMHDLLLWN-NATVTTCHSktanldkevnkgDILVVATGQPEM 221
Cdd:cd05191 1 ATAAGAVALLKAAGKvtnkSLKGKTVVVLGA-GEVGKGIAKLLADEgGKKVVLCDR------------DILVTATPAGVP 67
|
90
....*....|....*....
gi 261878543 222 VKGE---WIKPGAVVIDCG 237
Cdd:cd05191 68 VLEEataKINEGAVVIDLA 86
|
|
| |
