|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
305-934 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 1036.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 305 NYPTLNLLRPVPSDVAISRSCVPKPIECLAKEIGLLSDEVELYGRTKAKVQLKTIDRLQTQLDGKYVVVTGITPTPLGEG 384
Cdd:PLN02759 6 SRRKLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 385 KSTTTIGLVQALGAHLKLNAFACVRQPSQGPTFGIKGGAAGGGYSQVVPMEEFNLHLTGDIHAITAANNPVAAAVDARMF 464
Cdd:PLN02759 86 KSTTTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 465 HEATQSDKALFNRLVPLA-EGQRKFSPVQINRLERLGIKKTDPSTLTEEEITRFVRPDIDPESVTWQRVLDTNDRFLRKI 543
Cdd:PLN02759 166 HEATQSDKALFNRLCPANkEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITWRRVMDVNDRFLRKI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 544 TIGQSPTEKGFTRTAQFDITVASEIMAVLALTTGLEDMKQRLAKMVVATSRSGQPVTTEDLGVCGALTVLMRDAIKPNLM 623
Cdd:PLN02759 246 TVGQGPEEKGMTRETGFDITVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 624 QTLEGNPVFVHAGPFANIAHGNSSILADKIALKLVGPQGFVVTEAGFGADIGMEKFFNIKCRYSGLKPHAVVLVATVRAL 703
Cdd:PLN02759 326 QTLEGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRAL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 704 KMHGGGPTVTAGTPLPKEYIEENLTLLEAGCANMRKQVENAKLFGVPVVVAVNAFKTDTQAELNLICKMAKEAGAFDAVP 783
Cdd:PLN02759 406 KMHGGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 784 CSHWADGGAGAVDLARAVQRAADLPNS-FQFLYDVQLPIADKIRIIAQKIYGADDIELLPEAQQKVERYTKQGFADLPIC 862
Cdd:PLN02759 486 CTHHAHGGKGAVDLGEAVQKACEGNSQpFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPIC 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054762 863 MAKTHLSLSHDAEKKGVPTGFVLPIRDIRASVGAGFLYPLVGTMPTIPGLPTRPCFYDIDLDTESGEVIGLF 934
Cdd:PLN02759 566 MAKTQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFYDIDIDTETGKVLGLS 637
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
316-934 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 982.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 316 PSDVAISRSCVPKPIECLAKEIGLLSDEVELYGRTKAKVQLKTIDRLQTQLDGKYVVVTGITPTPLGEGKSTTTIGLVQA 395
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 396 LGaHLKLNAFACVRQPSQGPTFGIKGGAAGGGYSQVVPMEEFNLHLTGDIHAITAANNPVAAAVDARMFHEatqsdkalf 475
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHG--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 476 nrlvplaegqrkfspvqiNRLerlgikktdpstlteeeitrfvrpDIDPESVTWQRVLDTNDRFLRKITIGQSPTEKGFT 555
Cdd:pfam01268 151 ------------------NEL------------------------DIDPRRITWKRVLDMNDRALRNIVIGLGGKENGVP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 556 RTAQFDITVASEIMAVLALTTGLEDMKQRLAKMVVATSRSGQPVTTEDLGVCGALTVLMRDAIKPNLMQTLEGNPVFVHA 635
Cdd:pfam01268 189 REDGFDITVASEIMAILCLATDLADLKERLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 636 GPFANIAHGNSSILADKIALKLvgpQGFVVTEAGFGADIGMEKFFNIKCRYSGLKPHAVVLVATVRALKMHGGGPTvtag 715
Cdd:pfam01268 269 GPFANIAHGCNSVIATKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGGVGK---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 716 tplpKEYIEENLTLLEAGCANMRKQVENAKLFGVPVVVAVNAFKTDTQAELNLICKMAkEAGAFDAVPCSHWADGGAGAV 795
Cdd:pfam01268 342 ----DELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIELVRELC-EAGGVDAALSEHWAKGGEGAI 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 796 DLARAVQRAADLPNS-FQFLYDVQLPIADKIRIIAQKIYGADDIELLPEAQQKVERYTKQGFADLPICMAKTHLSLSHDA 874
Cdd:pfam01268 417 ELAEAVVEACEEEPSnFKFLYDLELSIEEKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDP 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 875 EKKGVPTGFVLPIRDIRASVGAGFLYPLVGTMPTIPGLPTRPCFYDIDLDTEsGEVIGLF 934
Cdd:pfam01268 497 KLKGAPTGFTLPVRDVRLSAGAGFIVALTGDIMTMPGLPKRPAAENIDVDED-GKITGLF 555
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
330-933 |
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: 963.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 330 IECLAKEIGLLSDEVELYGRTKAKVQLKTIDRLQTQLDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLKlNAFACVR 409
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALGK-KAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 410 QPSQGPTFGIKGGAAGGGYSQVVPMEEFNLHLTGDIHAITAANNPVAAAVDARMFHEatqsdkalfnrlvplaegqrkfs 489
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHE----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 490 pvqiNRLerlgikktdpstlteeeitrfvrpDIDPESVTWQRVLDTNDRFLRKITIGQSPTEKGFTRTAQFDITVASEIM 569
Cdd:cd00477 137 ----NTL------------------------DIDPRRITWKRVLDVNDRALRNITIGLGGKENGVPRETGFDITVASEIM 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 570 AVLALTTGLEDMKQRLAKMVVATSRSGQPVTTEDLGVCGALTVLMRDAIKPNLMQTLEGNPVFVHAGPFANIAHGNSSIL 649
Cdd:cd00477 189 AILALSTDLADLRERLGRIVVAYSKDGEPVTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSII 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 650 ADKIALKLvgpQGFVVTEAGFGADIGMEKFFNIKCRYSGLKPHAVVLVATVRALKMHGGGPTVTAGtplpkeyiEENLTL 729
Cdd:cd00477 269 ADKIALKL---ADYVVTEAGFGADLGAEKFFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 730 LEAGCANMRKQVENAKLFGVPVVVAVNAFKTDTQAELNLICKMAKEAGAFDAVpCSHWADGGAGAVDLARAVQRAADLPN 809
Cdd:cd00477 338 LKKGCANLRKHIENIKKFGVPVVVAINRFPTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 810 S-FQFLYDVQLPIADKIRIIAQKIYGADDIELLPEAQQKVERYTKQGFADLPICMAKTHLSLSHDAEKKGVPTGFVLPIR 888
Cdd:cd00477 417 SnFKFLYPLDLPIEEKIEKIAKEIYGADGVEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 41054762 889 DIRASVGAGFLYPLVGTMPTIPGLPTRPCFYDIDLDTEsGEVIGL 933
Cdd:cd00477 497 DVRLSAGAGFVVPLAGDIMTMPGLPKRPAAYDIDIDDT-GKIEGL 540
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
305-933 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 931.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 305 NYPTLNLLRPVPSDVAISRSCVPKPIECLAKEIGLLSDEVELYGRTKAKVQLKTIDRLQTQLDGKYVVVTGITPTPLGEG 384
Cdd:PTZ00386 5 TTRKLSCQWPVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 385 KSTTTIGLVQALGAHLKLNAFACVRQPSQGPTFGIKGGAAGGGYSQVVPMEEFNLHLTGDIHAITAANNPVAAAVDARMF 464
Cdd:PTZ00386 85 KSTTTIGLAQSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 465 HEATQSDKALFNRLvplAEGQRKFSPVQINRLERLGIKKTDPSTLTEEEITRFVRPDIDPESVTWQRVLDTNDRFLRKIT 544
Cdd:PTZ00386 165 HERTQSDAALYRRL---TDELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISWRRVTDVNDRMLREIT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 545 IGQSPTEKGFTRTAQFDITVASEIMAVLALTTGLEDMKQRLAKMVVATSRSGQPVTTEDLGVCGALTVLMRDAIKPNLMQ 624
Cdd:PTZ00386 242 IGQGKEEKGITRKTGFDISVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 625 TLEGNPVFVHAGPFANIAHGNSSILADKIALKLVGPQGFVVTEAGFGADIGMEKFFNIKCRYSGLKPHAVVLVATVRALK 704
Cdd:PTZ00386 322 TLEGTPVLVHAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 705 MHGGGPTVTAGTplpkeyieENLTLLEAGCANMRKQVENAKLFGVPVVVAVNAFKTDTQAELNLICKMA-KEAGAFDAVP 783
Cdd:PTZ00386 402 FHGGVEPVVAGK--------ENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELAlQEGGAADVVV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 784 CSHWADGGAGAVDLARAVQRAAD-LPNSFQFLYDVQLPIADKIRIIAQKIYGADDIELLPEAQQKVERYTKQGFADLPIC 862
Cdd:PTZ00386 474 TDHWAKGGAGAVDLAQALIRVTEnVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVC 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054762 863 MAKTHLSLSHDAEKKGVPTGFVLPIRDIRASVGAGFLYPLVGTMPTIPGLPTRPCFYDIDLDTESGEVIGL 933
Cdd:PTZ00386 554 MAKTQYSFSHDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYNIDIDCETGKIVGL 624
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
315-934 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 874.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 315 VPSDVAISRSCVPKPIECLAKEIGLLSDEVELYGRTKAKVQLKTIDRLQTQLDGKYVVVTGITPTPLGEGKSTTTIGLVQ 394
Cdd:COG2759 1 MKSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 395 ALGaHLKLNAFACVRQPSQGPTFGIKGGAAGGGYSQVVPMEEFNLHLTGDIHAITAANNPVAAAVDARMFHEatqsdkal 474
Cdd:COG2759 81 ALN-RLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLAALIDNHIHQG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 475 fnrlvplaegqrkfspvqiNRLerlgikktdpstlteeeitrfvrpDIDPESVTWQRVLDTNDRFLRKITIGQSPTEKGF 554
Cdd:COG2759 152 -------------------NEL------------------------NIDPRRITWKRVLDMNDRALRNIVIGLGGKANGV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 555 TRTAQFDITVASEIMAVLALTTGLEDMKQRLAKMVVATSRSGQPVTTEDLGVCGALTVLMRDAIKPNLMQTLEGNPVFVH 634
Cdd:COG2759 189 PREDGFDITVASEVMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 635 AGPFANIAHGNSSILADKIALKLVgpqGFVVTEAGFGADIGMEKFFNIKCRYSGLKPHAVVLVATVRALKMHGGGPtvta 714
Cdd:COG2759 269 GGPFANIAHGCNSVIATKLALKLA---DYVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVA---- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 715 gtplPKEYIEENLTLLEAGCANMRKQVENAKLFGVPVVVAVNAFKTDTQAELNLICKMAKEAGAfDAVPCSHWADGGAGA 794
Cdd:COG2759 342 ----KDELTEENLEALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGA 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 795 VDLARAVQRAAD-LPNSFQFLYDVQLPIADKIRIIAQKIYGADDIELLPEAQQKVERYTKQGFADLPICMAKTHLSLSHD 873
Cdd:COG2759 417 EELAEAVVEACEeGPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054762 874 AEKKGVPTGFVLPIRDIRASVGAGFLYPLVGTMPTIPGLPTRPCFYDIDLDtESGEVIGLF 934
Cdd:COG2759 497 PKLLGAPTGFTLTVREVRLSAGAGFIVALTGDIMTMPGLPKVPAAERIDID-EDGKITGLF 556
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
314-934 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 742.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 314 PVPSDVAISRSCVPKPIECLAKEIGLLSDEVELYGRTKAKVQLKTIDRLQTQLDGKYVVVTGITPTPLGEGKSTTTIGLV 393
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 394 QALgAHLKLNAFACVRQPSQGPTFGIKGGAAGGGYSQVVPMEEFNLHLTGDIHAITAANNPVAAAVDARMFHEatqsdka 473
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQG------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 474 lfnrlvplaegqrkfspvqiNRLerlgikktdpstlteeeitrfvrpDIDPESVTWQRVLDTNDRFLRKITIGQSPTEKG 553
Cdd:PRK13505 153 --------------------NEL------------------------GIDPRRITWKRVLDMNDRALRNIVVGLGGPANG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 554 FTRTAQFDITVASEIMAVLALTTGLEDMKQRLAKMVVATSRSGQPVTTEDLGVCGALTVLMRDAIKPNLMQTLEGNPVFV 633
Cdd:PRK13505 189 VPREDGFDITVASEIMAILCLATDLKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 634 HAGPFANIAHGNSSILADKIALKLvgpQGFVVTEAGFGADIGMEKFFNIKCRYSGLKPHAVVLVATVRALKMHGGGPTvt 713
Cdd:PRK13505 269 HGGPFANIAHGCNSVLATKTALKL---ADYVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVAK-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 714 agtplpKEYIEENLTLLEAGCANMRKQVENAKLFGVPVVVAVNAFKTDTQAELNLICKMAKEAGAfDAVPCSHWADGGAG 793
Cdd:PRK13505 344 ------DDLKEENVEALKKGFANLERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 794 AVDLARAVQRAADLPNS-FQFLYDVQLPIADKIRIIAQKIYGADDIELLPEAQQKVERYTKQGFADLPICMAKTHLSLSH 872
Cdd:PRK13505 417 GVELAEKVVELIEEGESnFKPLYDDEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSD 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054762 873 DAEKKGVPTGFVLPIRDIRASVGAGFLYPLVGTMPTIPGLPTRPCFYDIDLDtESGEVIGLF 934
Cdd:PRK13505 497 DPKLLGAPTGFTITVRELRPSAGAGFIVALTGDIMTMPGLPKVPAALNIDVD-EDGNIVGLF 557
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
317-933 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 722.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 317 SDVAISRSCVPKPIECLAKEIGLLSDEVELYGRTKAKVQLKTIDRLQTQLDGKYVVVTGITPTPLGEGKSTTTIGLVQAL 396
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 397 gAHLKLNAFACVRQPSQGPTFGIKGGAAGGGYSQVVPMEEFNLHLTGDIHAITAANNPVAAAVDARMFHEatqsdkalfN 476
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHE---------Q 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 477 RLvplaeGQRKFSpvQINRLERLgikktdpstlteeeitrfvrpDIDPESVTWQRVLDTNDRFLRKITIGQSPTEKGFTR 556
Cdd:PRK13506 153 RL-----GYDAFE--AQSGLPAL---------------------DIDPEQILWKRVVDHNDRALRMITVGLGENGNGPER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 557 TAQFDITVASEIMAVLALTTGLEDMKQRLAKMVVATSRSGQPVTTEDLGVCGALTVLMRDAIKPNLMQTLEGNPVFVHAG 636
Cdd:PRK13506 205 EDGFDITAASELMAILALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 637 PFANIAHGNSSILADKIALKLVGpqgFVVTEAGFGADIGMEKFFNIKCRYSGLKPHAVVLVATVRALKMHGGGPTVTAGT 716
Cdd:PRK13506 285 PFANIAHGNSSIIADRIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 717 PLPKEYIEENLTLLEAGCANMRKQVENAKLFGVPVVVAVNAFKTDTQAELNLICKMAKEAGAFDAVPCSHWADGGAGAVD 796
Cdd:PRK13506 362 ALPDSINAPDQARLEAGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 797 LARAVQRAADLPNSFQFLYDVQLPIADKIRIIAQKIYGADDIELLPEAQQKVERYTKQGFADLPICMAKTHLSLSHDAEK 876
Cdd:PRK13506 442 LAQAVVRACEQPSQFKLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPAL 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 41054762 877 KGVPTGFVLPIRDIRASVGAGFLYPLVGTMPTIPGLPTRPCFYDIDLDtESGEVIGL 933
Cdd:PRK13506 522 KGAPTDFEVPIRELRLCAGAGFITALVGNVMTMPGLGLKPGYLNIDID-ADGEIVGL 577
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
328-934 |
0e+00 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 683.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 328 KPIECLAKEIGLLSDEVELYGRTKAKV-QLKTIDRLQTQLDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAhLKLNAFA 406
Cdd:PRK13507 22 KPVEELAEELGLTKEELLPYGHYIAKVdFRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQGLGK-RGKKVSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 407 CVRQPSQGPTFGIKGGAAGGGYSQVVPMEEFNLHLTGDIHAITAANNPVAAAVDARMFHEATQSDKalfnrlvplaegqr 486
Cdd:PRK13507 101 AIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTDE-------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 487 kfspvqinRLERLGIKktdpstlteeeitrfvRPDIDPESVTWQRVLDTNDRFLRKITIGQSPTEKGFTRTAQFDITVAS 566
Cdd:PRK13507 167 --------QLARRGLK----------------RLDIDPTRVEMGWIIDFCAQALRNIIIGIGGKTDGYMMQSGFGIAVSS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 567 EIMAVLALTTGLEDMKQRLAKMVVATSRSGQPVTTEDLGVCGALTVLMRDAIKPNLMQTLEGNPVFVHAGPFANIAHGNS 646
Cdd:PRK13507 223 EVMAILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 647 SILADKIALKLvgpQGFVVTEAGFGADIGMEKFFNIKCRYSGLKPHAVVLVATVRALKMHGGGPTVTAGTPLPKEYIEEN 726
Cdd:PRK13507 303 SIIADRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKEN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 727 LTLLEAGCANMRKQVENAKLFGVPVVVAVNAFKTDTQAELNLICKMAKEAGAFDAVPcSHWADGGAGAVDLARAVQRAAD 806
Cdd:PRK13507 380 VGLVEKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 807 LPNSFQFLYDVQLPIADKIRIIAQKIYGADDIELLPEAQQKVERYTKQG-FADLPICMAKTHLSLSHDAEKKGVPTGFVL 885
Cdd:PRK13507 459 EPNDFKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKRLESDPeTADFGTCMVKTHLSLSHDPALKGVPKGWTL 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 41054762 886 PIRDIRASVGAGFLYPLVGTMPTIPGLPTRPCFYDIDLDTESGEVIGLF 934
Cdd:PRK13507 539 PIRDILTYGGAGFVVPVAGDISLMPGTGSDPAFRRIDVDTQTGKVKGLF 587
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
1-291 |
2.26e-133 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 401.31 E-value: 2.26e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:COG0190 1 MMAQILDGKAVAAEIREELKERVAALKAK--GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSiHtINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGV 160
Cdd:COG0190 79 LALIDELNADPSVHGILVQLPLPK-H-IDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTI 240
Cdd:COG0190 155 DLAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 41054762 241 ADSsrpsgkRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:COG0190 235 EDG------KLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAE 279
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-291 |
1.30e-107 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 334.62 E-value: 1.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 2 PAQIICGKTISAQVRERLKEEVEEMKKTHpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVL 81
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAH-GVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 82 QSVTEVNENSKIHGLIVQLPLDSiHtINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVS 161
Cdd:PRK14188 80 ALIARLNADPAIHGILVQLPLPK-H-LDSEAVIQAIDPEKDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 162 LAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIA 241
Cdd:PRK14188 156 LSGLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 41054762 242 DSSRPSGK-RVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14188 236 APEKGEGKtRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAAC 286
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-291 |
1.57e-103 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 323.50 E-value: 1.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK14190 1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQ--GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGV 160
Cdd:PRK14190 79 LALIDRLNADPRINGILVQLPLPK--HIDEKAVIERISPEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTI 240
Cdd:PRK14190 155 DISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 41054762 241 ADssrpsGKrVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14190 235 EN-----GK-LCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAK 279
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
3-291 |
5.65e-97 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 306.82 E-value: 5.65e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 3 AQIICGKTISAQVRERLKEEVEEMKKTHpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQ 82
Cdd:PLN02516 9 AQIIDGKAIAKAIRSEIAEEVAQLSEKH-GKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 83 SVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGDCFIPCTPNGCMELIKQTGVSL 162
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLPK--HINEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 163 AGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIAD 242
Cdd:PLN02516 166 KGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41054762 243 SSRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PLN02516 246 PSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAK 294
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-293 |
1.02e-96 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 305.69 E-value: 1.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKTHPNfEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK10792 1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLR-APGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSIhtINTERVINSVAPEKDVDGLTSINAGKLA------RgdlgdcfiPCTPNGCMEL 154
Cdd:PRK10792 80 LALIDELNADPTIDGILVQLPLPAH--IDNVKVLERIHPDKDVDGFHPYNVGRLAqripllR--------PCTPRGIMTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 155 IKQTGVSLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVID 234
Cdd:PRK10792 150 LERYGIDTYGLNAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVID 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 41054762 235 CGINTIADssrpsGKrVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKHF 293
Cdd:PRK10792 230 VGINRLED-----GK-LVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEY 282
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-292 |
4.18e-95 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 301.22 E-value: 4.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK14189 1 MTAQLIDGNALSKQLRAEAAQRAAALTAR--GHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSiHtINTERVINSVAPEKDVDGLTSINAGKLARGDLGdcFIPCTPNGCMELIKQTGV 160
Cdd:PRK14189 79 LARIDELNRDPKIHGILVQLPLPK-H-IDSHKVIEAIAPEKDVDGFHVANAGALMTGQPL--FRPCTPYGVMKMLESIGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINti 240
Cdd:PRK14189 155 PLRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMN-- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41054762 241 adssRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKH 292
Cdd:PRK14189 233 ----RDDAGKLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
3-291 |
4.13e-91 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 293.83 E-value: 4.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 3 AQIICGKTISAQVRERLKEEVEEMKKThPNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQ 82
Cdd:PLN02616 73 AKVIDGKAVAKKIRDEITIEVSRMKES-IGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 83 SVTEVNENSKIHGLIVQLPLDSiHtINTERVINSVAPEKDVDGLTSINAGKLARGDLGDCFIPCTPNGCMELIKQTGVSL 162
Cdd:PLN02616 152 FISGFNNDPSVHGILVQLPLPS-H-MDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 163 AGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIAD 242
Cdd:PLN02616 230 KGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVED 309
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41054762 243 SSRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PLN02616 310 ASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAK 358
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
119-291 |
8.45e-90 |
|
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: 282.52 E-value: 8.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 119 PEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKT 198
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 199 ADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIADssrPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMT 278
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPD---KSGGKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 41054762 279 VAMLMKNTVLSAK 291
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
3-291 |
2.08e-86 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 280.31 E-value: 2.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 3 AQIICGKTISAQVRERLKEEVEEMKKTHPNFePGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQ 82
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAVGKV-PGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 83 SVTEVNENSKIHGLIVQLPLDsiHTINTERVINSVAPEKDVDGLTSINAGKLARGDLGDCFIPCTPNGCMELIKQTGVSL 162
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQLPLP--QHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 163 AGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIAD 242
Cdd:PLN02897 213 AGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41054762 243 SSRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PLN02897 293 SSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAK 341
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-291 |
1.18e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 273.57 E-value: 1.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 4 QIICGKTISAQVRERLKEEVEEMKkTHPNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQS 83
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILT-AQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 84 VTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSLA 163
Cdd:PRK14191 81 IKDLNTDQNIDGILVQLPLPR--HIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQL--DGFVPATPMGVMRLLKHYHIEIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 164 GKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIADS 243
Cdd:PRK14191 157 GKDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLNDG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 41054762 244 srpsgkRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14191 237 ------RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-289 |
5.73e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 271.94 E-value: 5.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 2 PAQIICGKTISAQVRERLKEEVEEMKKT--HPnfePGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETE 79
Cdd:PRK14186 1 MALILDGKALAAEIEQRLQAQIESNLPKagRP---PGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 80 VLQSVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGdcFIPCTPNGCMELIKQTG 159
Cdd:PRK14186 78 VEALIAQLNQDERVDGILLQLPLPK--HLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPG--LRSCTPAGVMRLLRSQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 160 VSLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINT 239
Cdd:PRK14186 154 IDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41054762 240 IADSSRPSgkRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLS 289
Cdd:PRK14186 234 LPSSDGKT--RLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLS 281
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-290 |
7.73e-83 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 269.00 E-value: 7.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 5 IICGKTISAQVRERLKEEVEEMKKTHpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSV 84
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQH-NLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 85 TEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGDCFIPCTPNGCMELIKQTGVSLAG 164
Cdd:PRK14187 83 NELNNDDSVHGILVQLPVPN--HIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 165 KRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIADSS 244
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 41054762 245 RpsgKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSA 290
Cdd:PRK14187 241 V---KKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-298 |
1.76e-82 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 268.25 E-value: 1.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK14194 2 MSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGV 160
Cdd:PRK14194 80 LALIAELNADPSVNGILLQLPLPA--HIDEARVLQAINPLKDVDGFHSENVGGLSQGR--DVLTPCTPSGCLRLLEDTCG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTI 240
Cdd:PRK14194 156 DLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 41054762 241 ADSSRpsgKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKHFLQAQK 298
Cdd:PRK14194 236 DDDGR---SRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQAHAQR 290
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
127-294 |
4.07e-81 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 258.93 E-value: 4.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 127 TSINAGKLARGdlGDCFIPCTPNGCMELIKQTGVSLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVG 206
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 207 KADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIadssrpSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNT 286
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRV------GNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 41054762 287 VLSAKHFL 294
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-291 |
3.77e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 261.23 E-value: 3.77e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 3 AQIICGKTISAQVRERLKEEVEEMKKTHpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQ 82
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEK-GIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 83 SVTEVNENSKIHGLIVQLPLDsiHTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSL 162
Cdd:PRK14179 81 LIERYNQDPTWHGILVQLPLP--KHINEEKILLAIDPKKDVDGFHPMNTGHLWSGR--PVMIPCTPAGIMEMFREYNVEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 163 AGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINtiad 242
Cdd:PRK14179 157 EGKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMN---- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41054762 243 ssRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14179 233 --RDENGKLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAAL 279
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-285 |
1.10e-79 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 259.71 E-value: 1.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 4 QIICGKTISAQVRERLKEEVEEMKKTHPNFePGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQS 83
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGLSI-PKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 84 VTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSLA 163
Cdd:PRK14172 82 IEELNKDNNVHGIMLQLPLPK--HLDEKKITNKIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 164 GKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGintiadS 243
Cdd:PRK14172 158 GKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVG------T 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 41054762 244 SRPSGKrVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKN 285
Cdd:PRK14172 232 SSVNGK-ITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-294 |
1.49e-79 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 259.76 E-value: 1.49e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 4 QIICGKTISAQVRERLKEEVEEMKKTHpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQS 83
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDELKLVK-NIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 84 VTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSLA 163
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLPK--HIDTTKILEAIDPKKDVDGFHPYNVGRLVTGL--DGFVPCTPLGVMELLEEYEIDVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 164 GKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIADS 243
Cdd:PRK14183 157 GKDVCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 41054762 244 srpsgkRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKHFL 294
Cdd:PRK14183 237 ------RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNRA 281
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-293 |
1.97e-79 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 259.75 E-value: 1.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 4 QIICGKTISAQVRERLKEEVEEMKKTHPNFePGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQS 83
Cdd:PRK14174 2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKV-PGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 84 VTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGDCFIPCTPNGCMELIKQTGVSLA 163
Cdd:PRK14174 81 IEDLNNDPDVHGILVQQPLPK--QIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 164 GKRAVVIGRSKIVGAPMHDLLL----WNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINT 239
Cdd:PRK14174 159 GKHCVVVGRSNIVGKPMANLMLqklkESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINR 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41054762 240 IADSSRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKHF 293
Cdd:PRK14174 239 IEDPSTKSGYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-291 |
3.14e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 253.23 E-value: 3.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 5 IICGKTISAQVRERLKEEVEEmkkthPNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSV 84
Cdd:PRK14178 2 ILDGKAVSEKRLELLKEEIIE-----SGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 85 TEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGdcFIPCTPNGCMELIKQTGVSLAG 164
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLPK--GVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPG--FAPCTPNGIMTLLHEYKISIAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 165 KRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIadss 244
Cdd:PRK14178 153 KRAVVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV---- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41054762 245 rpSGKrVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14178 229 --NGK-LCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-291 |
1.74e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 249.10 E-value: 1.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 5 IICGKTISAQVRERLKEEVEEMKkTHPNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSV 84
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELK-SQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 85 TEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGdLGDCFIPCTPNGCMELIKQTGVSLAG 164
Cdd:PRK14171 83 NELNLDNEISGIIVQLPLPS--SIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 165 KRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIadss 244
Cdd:PRK14171 160 KNVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI---- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41054762 245 rpSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14171 236 --SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK 280
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-291 |
7.82e-75 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 247.00 E-value: 7.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 4 QIICGKTISAQVRERLKEEVEEMKKTHPNfEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQS 83
Cdd:PRK14184 2 LLLDGKATAATIREELKTEVAALTARHGR-APGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 84 VTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSLA 163
Cdd:PRK14184 81 IAELNARPDIDGILLQLPLPK--GLDSQRCLELIDPAKDVDGFHPENMGRLALGL--PGFRPCTPAGVMTLLERYGLSPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 164 GKRAVVIGRSKIVGAPMHDLLL----WNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINT 239
Cdd:PRK14184 157 GKKAVVVGRSNIVGKPLALMLGapgkFANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41054762 240 IADSsrpsgkrVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14184 237 TDDG-------LVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWK 281
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-291 |
1.94e-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: 1.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 5 IICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSV 84
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAAR--GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 85 TEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGdCFIPCTPNGCMELIKQTGVSLAG 164
Cdd:PRK14182 81 ARLNADPAVHGILVQLPLPK--HVDERAVLDAISPAKDADGFHPFNVGALSIGIAG-VPRPCTPAGVMRMLDEARVDPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 165 KRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIADSs 244
Cdd:PRK14182 158 KRALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41054762 245 rpsgkRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14182 237 -----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAK 278
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-291 |
3.36e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 245.21 E-value: 3.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK14175 1 MVAKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGV 160
Cdd:PRK14175 79 LNELNRLNNDDSVSGILVQVPLPK--QVSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGiNTI 240
Cdd:PRK14175 155 DLEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG-NTP 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 41054762 241 ADSSrpsgkRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14175 234 DENG-----KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-290 |
1.27e-73 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 244.30 E-value: 1.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 3 AQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQ 82
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDA--GVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 83 SVTEVNENSKIHGLIVQLPLDSiHtINTERVINSVAPEKDVDGLTSINAGKLARGDLGdcFIPCTPNGCMELIKQTGVSL 162
Cdd:PRK14167 80 TIDELNADEDVHGILVQMPVPD-H-VDDREVLRRIDPAKDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 163 AGKRAVVIGRSKIVGAPMHDLLLWN----HATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGIN 238
Cdd:PRK14167 156 EGADVVVVGRSDIVGKPMANLLIQKadggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41054762 239 TIaDSSRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSA 290
Cdd:PRK14167 236 RV-DADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
8-293 |
9.24e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 241.42 E-value: 9.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 8 GKTISAQVRERLKEEVEEmKKTHPNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSVTEV 87
Cdd:PRK14177 8 GKKLSEKIRNEIRETIEE-RKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 88 NENSKIHGLIVQLPldSIHTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSLAGKRA 167
Cdd:PRK14177 87 NLDPNVDGILLQHP--VPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVTGKNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 168 VVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINtiadssrPS 247
Cdd:PRK14177 163 VVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN-------PG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41054762 248 GkrvVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK-HF 293
Cdd:PRK14177 236 N---VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKeHF 279
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
8-295 |
2.23e-72 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 240.31 E-value: 2.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 8 GKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSVTEV 87
Cdd:PRK14166 6 GKALSAKIKEELKEKNQFLKSK--GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 88 NENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGdLGDCFIPCTPNGCMELIKQTGVSLAGKRA 167
Cdd:PRK14166 84 NHDDSVHGILVQLPLPD--HICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEGKDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 168 VVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIadssrPS 247
Cdd:PRK14166 161 VIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRL-----ES 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 41054762 248 GKrVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKHFLQ 295
Cdd:PRK14166 236 GK-IVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-290 |
3.60e-72 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 239.92 E-value: 3.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK14193 1 MTAIILDGKATADEIKADLAERVAALKEK--GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSiHtINTERVINSVAPEKDVDGLTSINAGKLARGDLGDcfIPCTPNGCMELIKQTGV 160
Cdd:PRK14193 79 NAVIDELNADPACTGYIVQLPLPK-H-LDENAVLERIDPAKDADGLHPTNLGRLVLNEPAP--LPCTPRGIVHLLRRYDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWNH--ATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGIn 238
Cdd:PRK14193 155 ELAGAHVVVIGRGVTVGRPIGLLLTRRSenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41054762 239 tiadsSRPSGKRVVGDVHYDSAkDRAAFITPVPGGVGPMTVAMLMKNTVLSA 290
Cdd:PRK14193 234 -----SRAGDGKLVGDVHPDVW-EVAGAVSPNPGGVGPMTRAFLLTNVVERA 279
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-291 |
4.82e-72 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 239.59 E-value: 4.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 3 AQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQ 82
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKE--GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 83 SVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSL 162
Cdd:PRK14170 80 VVEELNEDKTIHGILVQLPLPE--HISEEKVIDTISYDKDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELIKSTGTQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 163 AGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINtiad 242
Cdd:PRK14170 156 EGKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMD---- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41054762 243 ssRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14170 232 --RDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAK 278
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-291 |
8.85e-72 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 238.94 E-value: 8.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 5 IICGKTISAQVRERLKEEVEEMKKTHpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSV 84
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERLKSNR-GITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 85 TEVNENSKIHGLIVQLPLDSiHtINTERVINSVAPEKDVDGLTSINAGKLARGDLGdcFIPCTPNGCMELIKQTGVSLAG 164
Cdd:PRK14176 89 DSLNKRKDVHGILLQLPLPK-H-LDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEG--LVPCTPHGVIRALEEYGVDIEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 165 KRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIADss 244
Cdd:PRK14176 165 KNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEED-- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41054762 245 rpsgkRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14176 243 -----KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAE 284
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-291 |
1.26e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 238.62 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKTHpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK14168 1 MSAKIIKGTEIREEILEEIRGEVAELKEKY-GKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGDCFIPCTPNGCMELIKQTGV 160
Cdd:PRK14168 80 LALIDKYNNDDSIHGILVQLPLPK--HINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLVRSGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWN----HATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCG 236
Cdd:PRK14168 158 ETSGAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 41054762 237 INTIADSSRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14168 238 VNRVGTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-291 |
1.27e-69 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 233.18 E-value: 1.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 4 QIICGKTISAQVRERLKEEVEEMKKTHPNfEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQS 83
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAKGGK-RPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 84 VTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGVSLA 163
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLPK--HISEQKVIEAIDYRKDVDGFHPINVGRMSIGL--PCFVSATPNGILELLKRYHIETS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 164 GKRAVVIGRSKIVGAPMHDLLLWNH----ATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINT 239
Cdd:PRK14185 157 GKKCVVLGRSNIVGKPMAQLMMQKAypgdCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41054762 240 IADSSRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14185 237 VPDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGK 288
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-290 |
8.34e-69 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 230.87 E-value: 8.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKtisaQVRERLKEEVEEMKKTHPnFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK14173 1 MAARELSGP----PAAEAVYAELRARLAKLP-FVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGdlGDCFIPCTPNGCMELIKQTGV 160
Cdd:PRK14173 76 LELIARLNADPEVDGILVQLPLPP--HIDFQRVLEAIDPLKDVDGFHPLNVGRLWMG--GEALEPCTPAGVVRLLKHYGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTI 240
Cdd:PRK14173 152 PLAGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 41054762 241 ADSsrpSGK-RVVGDVHYDSAkDRAAFITPVPGGVGPMTVAMLMKNTVLSA 290
Cdd:PRK14173 232 GGN---GGRdILTGDVHPEVA-EVAGALTPVPGGVGPMTVAMLMANTVIAA 278
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-293 |
7.64e-68 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 227.99 E-value: 7.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 5 IICGKTISAQVRERLKEEVEEMKKtHPNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSV 84
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKH-HTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 85 TEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDlGDCFIPCTPNGCMELIKQTGVSLAG 164
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPA--HINKNNVIYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 165 KRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIadss 244
Cdd:PRK14180 159 AYAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHV---- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41054762 245 rpSGKrVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKHF 293
Cdd:PRK14180 235 --DGK-IVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQEL 280
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-295 |
2.49e-67 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 226.65 E-value: 2.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 1 MPAQIICGKTISAQVRERLKEEVEEMKKTHPNfEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEV 80
Cdd:PRK14192 1 MMALVLDGKALAKQIEEELSVRVEALKAKTGR-TPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 81 LQSVTEVNENSKIHGLIVQLPLDsiHTINTERVINSVAPEKDVDGLTSINAGKLARGDlgDCFIPCTPNGCMELIKQTGV 160
Cdd:PRK14192 80 LAKIEELNANPDVHGILLQHPVP--AQIDERACFDAISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 161 SLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINti 240
Cdd:PRK14192 156 ELAGKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFH-- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 41054762 241 adssrPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKHFLQ 295
Cdd:PRK14192 234 -----PRDGGGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKALG 283
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-291 |
2.58e-64 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 218.28 E-value: 2.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 3 AQIICGKTISAQVRERLKEEVEEMKKThpNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQ 82
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 83 SVTEVNENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGdcFIPCTPNGCMELIKQTGVSL 162
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPLPA--GLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPT--VVASTPYGIMALLDAYDIDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 163 AGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIAD 242
Cdd:PRK14169 155 AGKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGAD 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41054762 243 SSrpsgkrVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:PRK14169 235 GK------LLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAK 277
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
8-293 |
5.03e-63 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 214.72 E-value: 5.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 8 GKTISAQVRERLKEEVEEMKKThpnfePGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSVTEV 87
Cdd:PRK14181 5 GAPAAEHILATIKENISASSTA-----PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 88 NENSKIHGLIVQLPLDSihTINTERVINSVAPEKDVDGLTSINAGKLARGDLGDcFIPCTPNGCMELIKQTGVSLAGKRA 167
Cdd:PRK14181 80 NNDPNIHGILVQLPLPK--HLDAQAILQAISPDKDVDGLHPVNMGKLLLGETDG-FIPCTPAGIIELLKYYEIPLHGRHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 168 VVIGRSKIVGAPMHDLLLWNH----ATVTTCHSKTADLVSEVGKADILVTGIGKPEMVHGDWLKTGAEVIDCGINTIAdS 243
Cdd:PRK14181 157 AIVGRSNIVGKPLAALLMQKHpdtnATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVP-A 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41054762 244 SRPSGKRVVGDVHYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAKHF 293
Cdd:PRK14181 236 ANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLRH 285
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
137-291 |
2.01e-45 |
|
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: 159.98 E-value: 2.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 137 GDLGDCFIPCTPNGCMELIKQTGVSLAGKRAVVIGRSKIVGAPMHDLLLWNHATVTTCHSKTADLVSEVGKADILVTGIG 216
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054762 217 KPEMVHGDWLKTGAEVIDCGINTIAdssrpsgkrvvgdvhYDSAKDRAAFITPVPGGVGPMTVAMLMKNTVLSAK 291
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLS---------------GDDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
8-124 |
6.54e-44 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 154.49 E-value: 6.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 8 GKTISAQVRERLKEEVEEMKKthPNFEPGLVVLQVGDRDDSNLYISMKLKAAAQIGITAVHIKLPQTATETEVLQSVTEV 87
Cdd:pfam00763 3 GKAIAKKIREELKEEVAALKA--GGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKL 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 41054762 88 NENSKIHGLIVQLPLDSiHtINTERVINSVAPEKDVD 124
Cdd:pfam00763 81 NADPSVHGILVQLPLPK-H-IDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
119-287 |
4.12e-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: 63.21 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 119 PEKDVDGLTSINAGKL---ARGDLGD----CFIPCTPNGCMELIKQTGV---------SLAGKRAVVIGRSKIVGAPMHD 182
Cdd:cd01079 1 PHKDVEGLSHKYIFNLyhnIRFLDPEnrkkSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054762 183 LLLWNHATV---------------------TTCHSKTADLVSEVGKADILVTGIGKPEM-VHGDWLKTGAEVID-CGINT 239
Cdd:cd01079 81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICINfASIKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 41054762 240 IAdssrpsgkrvvgdvhyDSAKDRAAFITPVpggVGPMTVAMLMKNTV 287
Cdd:cd01079 161 FE----------------PSVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| |
