|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02759 |
PLN02759 |
Formate--tetrahydrofolate ligase |
314-897 |
0e+00 |
|
Formate--tetrahydrofolate ligase
Pssm-ID: 178359 Cd Length: 637 Bit Score: 621.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 314 VYTKKRPHEPQPSDAAISSSCESKPVVQLARELGLFSDEVESYGRSRAKIRLDALKRMEKQPNGKYVVVTGVTSSPLGEG 393
Cdd:PLN02759 6 SRRKLEVKSPVPADIDIAQSVEPLHISEIAKALGLLPDEYDLYGKYKAKVLLSVRDRLAGAPDGYYVVVAGITPTPLGEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 394 KRTTALGLAQALGAHLNTNAFACVQKSSLETCFGARGPAVGGGYSQIIPLEEVSLQPSGQNELVSAAGRLVMDTVKAYAH 473
Cdd:PLN02759 86 KSTTTIGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRVF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 474 YETKLSEKALFDLLVPLR-EGQRCVSLAQLNRLKKLAIEKSDPLTLTEREIRRFIRLDIDTDSAT--------DSF---- 540
Cdd:PLN02759 166 HEATQSDKALFNRLCPANkEGKRSFAAVMFRRLKKLGISKTDPDELTPEERKKFARLDIDPASITwrrvmdvnDRFlrki 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 541 -------------------SLENEMMAVLSLSSSEEEMQHRLANIIVATNKSGDPITTEDLNVSGPLAMLLKEALKPVLM 601
Cdd:PLN02759 246 tvgqgpeekgmtretgfdiTVASEIMAVLALTTSLADMRERLGKMVIGNSKAGEPVTADDLGVGGALTVLMKDAIHPTLM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 602 QTVEGTPVFLHTSPLVNVAQGGPSILADKMALKIVGSEGFVVTESGHGADVGLEKFFNIKCLYSGLQPDVLVMVATIRTL 681
Cdd:PLN02759 326 QTLEGTPVLVHAGPFANIAHGNSSIVADQIALKLVGPGGFVVTEAGFGADIGTEKFMNIKCRYSGLKPQCAVIVATVRAL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 682 KMQGGAPPIQAGLPLPKEYLQENLKQLERGCCHMRRQVEKAQAFGLPVIVAVNKFSSDTDAELELVCGQARQAGAFDAVQ 761
Cdd:PLN02759 406 KMHGGGPAVVAGKPLDHAYTTENVELVEAGCVNLARHIENTKSYGVNVVVAINMFATDTEAELEAVRQAALAAGAFDAVL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 762 CSSWSEGGAGALALAETVQRA-AKLPACFKFLYDLQTPASDKLRTVAQKMYGLKDVKLSPKAKEKLALYTKQGFENLPVC 840
Cdd:PLN02759 486 CTHHAHGGKGAVDLGEAVQKAcEGNSQPFKFLYPLDISIKEKIEAIAKESYGADGVEYSEQAEAQIEMYTRQGFSNLPIC 565
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192431 841 IAKTPLSLSNDPMMKGSSTDFMLPITDIKANAGAGFLCCLTGSTNAEMDDPMWPCFH 897
Cdd:PLN02759 566 MAKTQYSFSHDASLKGAPSGFTLPIRDVRASVGAGFIYPLVGTMSTMPGLPTRPCFY 622
|
|
| FTHFS |
pfam01268 |
Formate--tetrahydrofolate ligase; |
325-883 |
0e+00 |
|
Formate--tetrahydrofolate ligase;
Pssm-ID: 460143 Cd Length: 555 Bit Score: 606.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 325 PSDAAISSSCESKPVVQLARELGLFSDEVESYGRSRAKIRLDALKRMEKQPNGKYVVVTGVTSSPLGEGKRTTALGLAQA 404
Cdd:pfam01268 1 PSDIEIAQAAKLKPITEIAEKLGIPEDELEPYGKYKAKVSLDVLELLKDRPDGKLILVTAITPTPAGEGKTTTTIGLAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 405 LGaHLNTNAFACVQKSSLETCFGARGPAVGGGYSQIIPLEEVSLQPSGQNELVSAAGRLVMDTVKAYAHYETKLSekalF 484
Cdd:pfam01268 81 LN-RLGKKAIAALREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDIHAITAANNLLAAAIDNHIFHGNELD----I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 485 DllvPLR-EGQRCVSLaqlN-R-LKKLAIEKSDPLTLTEREiRRFirlDIDTDSatdsfslenEMMAVLSLSSSEEEMQH 561
Cdd:pfam01268 156 D---PRRiTWKRVLDM---NdRaLRNIVIGLGGKENGVPRE-DGF---DITVAS---------EIMAILCLATDLADLKE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 562 RLANIIVATNKSGDPITTEDLNVSGPLAMLLKEALKPVLMQTVEGTPVFLHTSPLVNVAQGGPSILADKMALKIvgsEGF 641
Cdd:pfam01268 217 RLGRIVVGYTRDGKPVTAEDLGVAGAMTALLKDAIKPNLVQTLEGTPAFVHGGPFANIAHGCNSVIATKIALKL---ADY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 642 VVTESGHGADVGLEKFFNIKCLYSGLQPDVLVMVATIRTLKMQGGAPPiqaglplpKEYLQENLKQLERGCCHMRRQVEK 721
Cdd:pfam01268 294 VVTEAGFGADLGAEKFFDIKCRKSGLKPDAVVLVATVRALKMHGGVGK--------DELTEENLEALEKGLANLEKHIEN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 722 AQAFGLPVIVAVNKFSSDTDAELELVCGQArQAGAFDAVQCSSWSEGGAGALALAETVQRAAKLPAC-FKFLYDLQTPAS 800
Cdd:pfam01268 366 VKKFGVPVVVAINRFPTDTDAEIELVRELC-EAGGVDAALSEHWAKGGEGAIELAEAVVEACEEEPSnFKFLYDLELSIE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 801 DKLRTVAQKMYGLKDVKLSPKAKEKLALYTKQGFENLPVCIAKTPLSLSNDPMMKGSSTDFMLPITDIKANAGAGFLCCL 880
Cdd:pfam01268 445 EKIETIAKEIYGADGVEYSPKAKKKLKRIEELGFGKLPVCMAKTQYSLSDDPKLKGAPTGFTLPVRDVRLSAGAGFIVAL 524
|
...
gi 1207192431 881 TGS 883
Cdd:pfam01268 525 TGD 527
|
|
| FTHFS |
cd00477 |
formyltetrahydrofolate synthetase; Formyltetrahydrofolate synthetase (FTHFS) catalyzes the ... |
339-882 |
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: 597.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 339 VVQLARELGLFSDEVESYGRSRAKIRLDALKRMEKQPNGKYVVVTGVTSSPLGEGKRTTALGLAQALGAHLnTNAFACVQ 418
Cdd:cd00477 1 IAEIAEELGLLEDELEPYGKYKAKVSLSVLDRLKDRPDGKYILVTAITPTPLGEGKSTTTIGLAQALGALG-KKAIAALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 419 KSSLETCFGARGPAVGGGYSQIIPLEEVSLQPSGQNELVSAAGRLVMDTVKAYAHYETKLSekalfdlLVPLR-EGQRCV 497
Cdd:cd00477 80 QPSLGPTFGIKGGAAGGGYSQVIPMEEINLHFTGDIHAITAANNLLAAAIDNRIFHENTLD-------IDPRRiTWKRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 498 SLAqlNR-LKKLAIEKSDpltlTEREIRRFIRLDIDTDSatdsfslenEMMAVLSLSSSEEEMQHRLANIIVATNKSGDP 576
Cdd:cd00477 153 DVN--DRaLRNITIGLGG----KENGVPRETGFDITVAS---------EIMAILALSTDLADLRERLGRIVVAYSKDGEP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 577 ITTEDLNVSGPLAMLLKEALKPVLMQTVEGTPVFLHTSPLVNVAQGGPSILADKMALKIvgsEGFVVTESGHGADVGLEK 656
Cdd:cd00477 218 VTADDLGVAGAMAALLKDAIKPNLMQTLEGTPAFVHAGPFANIAHGNSSIIADKIALKL---ADYVVTEAGFGADLGAEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 657 FFNIKCLYSGLQPDVLVMVATIRTLKMQGGAPPIQAGlplpkeylQENLKQLERGCCHMRRQVEKAQAFGLPVIVAVNKF 736
Cdd:cd00477 295 FFDIKCRYSGLKPDAAVLVATVRALKMHGGGPKVVAG--------EENLEALKKGCANLRKHIENIKKFGVPVVVAINRF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 737 SSDTDAELELVCGQARQAGAFDAVqCSSWSEGGAGALALAETVQRAAKLPAC-FKFLYDLQTPASDKLRTVAQKMYGLKD 815
Cdd:cd00477 367 PTDTEAEIALVRELAEEAGAEVAV-SEHWAKGGKGALELAEAVIEACEKPKSnFKFLYPLDLPIEEKIEKIAKEIYGADG 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192431 816 VKLSPKAKEKLALYTKQGFENLPVCIAKTPLSLSNDPMMKGSSTDFMLPITDIKANAGAGFLCCLTG 882
Cdd:cd00477 446 VEFSPEAKKKLKRYEKQGFGNLPVCMAKTQYSLSDDPKLKGAPTGFTLPIRDVRLSAGAGFVVPLAG 512
|
|
| PTZ00386 |
PTZ00386 |
formyl tetrahydrofolate synthetase; Provisional |
323-898 |
0e+00 |
|
formyl tetrahydrofolate synthetase; Provisional
Pssm-ID: 240394 Cd Length: 625 Bit Score: 583.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 323 PQPSDAAISSSCESKPVVQLARELGLFSDEVESYGRSRAKIRLDALKRMEKQPNGKYVVVTGVTSSPLGEGKRTTALGLA 402
Cdd:PTZ00386 14 PVPSDIDIAQSVKPQPITSVAESAGILLSELDPYGSTRAKVKLSVLKRLENSPNGKYVVVAGMNPTPLGEGKSTTTIGLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 403 QALGAHLNTNAFACVQKSSLETCFGARGPAVGGGYSQIIPLEEVSLQPSGQNELVSAAGRLVMDTVKAYAHYETKLSEKA 482
Cdd:PTZ00386 94 QSLGAHLHRKTFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHERTQSDAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 483 LFDLLVplrEGQRCVSLAQLNRLKKLAIEKSDPLTLTEREIRRFIRLDIDTDSAT--------DSF-------------- 540
Cdd:PTZ00386 174 LYRRLT---DELKKFTPIMLKRLEKLGISKTDPKQLTEEERVRFARLDIDPDTISwrrvtdvnDRMlreitigqgkeekg 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 541 ---------SLENEMMAVLSLSSSEEEMQHRLANIIVATNKSGDPITTEDLNVSGPLAMLLKEALKPVLMQTVEGTPVFL 611
Cdd:PTZ00386 251 itrktgfdiSVASEVMAILALATDLADMRQRLGAIVVAKSKSGEPVTAEDLGCAGAMTVLMKDTIEPTLMQTLEGTPVLV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 612 HTSPLVNVAQGGPSILADKMALKIVGSEGFVVTESGHGADVGLEKFFNIKCLYSGLQPDVLVMVATIRTLKMQGGAPPIQ 691
Cdd:PTZ00386 331 HAGPFGNIAHGNSSIVADQIALKLAGQDGFVLTEAGFGADIGCEKFFNIKCRTSGLKPDAAVLVATVRALKFHGGVEPVV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 692 AGlplpkeylQENLKQLERGCCHMRRQVEKAQAFGLPVIVAVNKFSSDTDAELELVCGQARQ-AGAFDAVQCSSWSEGGA 770
Cdd:PTZ00386 411 AG--------KENLEAVRKGLSNLQRHIQNIRKFGVPVVVALNKFSTDTDAELELVKELALQeGGAADVVVTDHWAKGGA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 771 GALALAETVQRAAK-LPACFKFLYDLQTPASDKLRTVAQKMYGLKDVKLSPKAKEKLALYTKQGFENLPVCIAKTPLSLS 849
Cdd:PTZ00386 483 GAVDLAQALIRVTEnVPSNFKLLYPLDASLKEKIETICKEIYGAAGVEYLNDADEKLEDFERMGYGKFPVCMAKTQYSFS 562
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1207192431 850 NDPMMKGSSTDFMLPITDIKANAGAGFLCCLTGSTNAEMDDPMWPCFHG 898
Cdd:PTZ00386 563 HDPELRGAPTGFTVPIRDVRVNCGAGFVFPLLGDISTMPGLPTRPAFYN 611
|
|
| MIS1 |
COG2759 |
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism]; |
325-883 |
0e+00 |
|
Formyltetrahydrofolate synthetase [Nucleotide transport and metabolism];
Pssm-ID: 442046 Cd Length: 556 Bit Score: 562.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 325 PSDAAISSSCESKPVVQLARELGLFSDEVESYGRSRAKIRLDALKRMEKQPNGKYVVVTGVTSSPLGEGKRTTALGLAQA 404
Cdd:COG2759 2 KSDIEIAQEAKLKPITEIAEKLGIPEDDLEPYGKYKAKIDLDLLDRLKDRPDGKLILVTAITPTPAGEGKTTTTVGLGQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 405 LGaHLNTNAFACVQKSSLETCFGARGPAVGGGYSQIIPLEEVSLQPSGQNELVSAAGRLVMdtvkayahyetklsekALF 484
Cdd:COG2759 82 LN-RLGKKAIVALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITAAHNLLA----------------ALI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 485 DllvplregqrcvslaqlNRLKK---LAIeksDPLTLT--------EREIRRFIrldIDTDSATDSFSLEN--------E 545
Cdd:COG2759 145 D-----------------NHIHQgneLNI---DPRRITwkrvldmnDRALRNIV---IGLGGKANGVPREDgfditvasE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 546 MMAVLSLSSSEEEMQHRLANIIVATNKSGDPITTEDLNVSGPLAMLLKEALKPVLMQTVEGTPVFLHTSPLVNVAQGGPS 625
Cdd:COG2759 202 VMAILCLATDLEDLKERLGRIVVGYTYDGKPVTARDLKAAGAMAALLKDAIKPNLVQTLEGTPAFVHGGPFANIAHGCNS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 626 ILADKMALKIvgSEgFVVTESGHGADVGLEKFFNIKCLYSGLQPDVLVMVATIRTLKMQGGAPPiqaglplpKEYLQENL 705
Cdd:COG2759 282 VIATKLALKL--AD-YVVTEAGFGADLGAEKFFDIKCRKAGLKPDAVVLVATVRALKMHGGVAK--------DELTEENL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 706 KQLERGCCHMRRQVEKAQAFGLPVIVAVNKFSSDTDAELELVCGQARQAGAfDAVQCSSWSEGGAGALALAETVQRAA-K 784
Cdd:COG2759 351 EALEKGLANLEKHIENVKKFGVPVVVAINRFPTDTDAEIALVRELCEELGV-RVALSEVWAKGGEGAEELAEAVVEACeE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 785 LPACFKFLYDLQTPASDKLRTVAQKMYGLKDVKLSPKAKEKLALYTKQGFENLPVCIAKTPLSLSNDPMMKGSSTDFMLP 864
Cdd:COG2759 430 GPSNFKPLYDLEDPLEEKIETIATEIYGADGVEYSPKAEKQLKRIEELGYGKLPVCMAKTQYSLSDDPKLLGAPTGFTLT 509
|
570
....*....|....*....
gi 1207192431 865 ITDIKANAGAGFLCCLTGS 883
Cdd:COG2759 510 VREVRLSAGAGFIVALTGD 528
|
|
| PRK13506 |
PRK13506 |
formate--tetrahydrofolate ligase; Provisional |
326-883 |
1.44e-165 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237404 Cd Length: 578 Bit Score: 494.91 E-value: 1.44e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 326 SDAAISSSCESKPVVQLARELGLFSDEVESYGRSRAKIRLDALKRMEKQPNGKYVVVTGVTSSPLGEGKRTTALGLAQAL 405
Cdd:PRK13506 3 SDIEISRQAPLKPIAEIAAKLGLLPDELSPFGHTKAKVSLSVLKRLADKPKGKLVLVTAITPTPLGEGKTVTTIGLTQGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 406 gAHLNTNAFACVQKSSLETCFGARGPAVGGGYSQIIPLEEVSLQPSGQNELVSAAGRLVMDTVKAYAHYETKLSeKALFD 485
Cdd:PRK13506 83 -NALGQKVCACIRQPSMGPVFGVKGGAAGGGYAQVVPMEELNLHLTGDIHAVSAAHNLAAAAIDARLFHEQRLG-YDAFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 486 L---LVPLR-------------EGQRCvslaqlnrLKKLAIEKSDPLTLTEREiRRFirlDIDTDSatdsfslenEMMAV 549
Cdd:PRK13506 161 AqsgLPALDidpeqilwkrvvdHNDRA--------LRMITVGLGENGNGPERE-DGF---DITAAS---------ELMAI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 550 LSLSSSEEEMQHRLANIIVATNKSGDPITTEDLNVSGPLAMLLKEALKPVLMQTVEGTPVFLHTSPLVNVAQGGPSILAD 629
Cdd:PRK13506 220 LALSRDLKDMRQRIGRLVLAYNLQGQPITAEDLGVAGAMTVIMKDAIEPTLMQTLEGVPCLIHAGPFANIAHGNSSIIAD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 630 KMALKIVGsegFVVTESGHGADVGLEKFFNIKCLYSGLQPDVLVMVATIRTLKMQGGAPPIQAGLPLPKEYLQENLKQLE 709
Cdd:PRK13506 300 RIALKLAD---YVVTEGGFGSDMGFEKFCNIKARQSGKAPDCAVLVATLRALKANSGLYDLRPGQALPDSINAPDQARLE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 710 RGCCHMRRQVEKAQAFGLPVIVAVNKFSSDTDAELELVCGQARQAGAFDAVQCSSWSEGGAGALALAETVQRAAKLPACF 789
Cdd:PRK13506 377 AGFANLKWHINNVAQYGLPVVVAINRFPTDTDEELEWLKEAVLLTGAFGCEISEAFAQGGEGATALAQAVVRACEQPSQF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 790 KFLYDLQTPASDKLRTVAQKMYGLKDVKLSPKAKEKLALYTKQGFENLPVCIAKTPLSLSNDPMMKGSSTDFMLPITDIK 869
Cdd:PRK13506 457 KLLYPDEMSLEAKLMTLAEVGYGAAGVSLSDKAKQQLAQLTALGYDHLPVCMAKTPLSISHDPALKGAPTDFEVPIRELR 536
|
570
....*....|....
gi 1207192431 870 ANAGAGFLCCLTGS 883
Cdd:PRK13506 537 LCAGAGFITALVGN 550
|
|
| PRK13505 |
PRK13505 |
formate--tetrahydrofolate ligase; Provisional |
323-883 |
2.59e-162 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 237403 Cd Length: 557 Bit Score: 485.84 E-value: 2.59e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 323 PQPSDAAISSSCESKPVVQLARELGLFSDEVESYGRSRAKIRLDALKRMEKQPNGKYVVVTGVTSSPLGEGKRTTALGLA 402
Cdd:PRK13505 1 TMKSDIEIAQEATLKPITEIAAKLGIPEDDLEPYGKYKAKISLDKIKALKDKKDGKLILVTAINPTPAGEGKSTVTVGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 403 QALgAHLNTNAFACVQKSSLETCFGARGPAVGGGYSQIIPLEEVSLQPSGQNELVSAAGRLVMDTVKAYAHYETKL---S 479
Cdd:PRK13505 81 DAL-NKIGKKTVIALREPSLGPVFGIKGGAAGGGYAQVVPMEDINLHFTGDFHAITSANNLLAALIDNHIHQGNELgidP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 480 EKALFdllvplregQRCVSLaqlN-R-LKKLAIEKSDPLTLTEREirrfirldidtdsatDSFSLE--NEMMAVLSLSSS 555
Cdd:PRK13505 160 RRITW---------KRVLDM---NdRaLRNIVVGLGGPANGVPRE---------------DGFDITvaSEIMAILCLATD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 556 EEEMQHRLANIIVATNKSGDPITTEDLNVSGPLAMLLKEALKPVLMQTVEGTPVFLHTSPLVNVAQGGPSILADKMALKI 635
Cdd:PRK13505 213 LKDLKERLGRIVVGYTYDGKPVTVKDLKVEGAMALLLKDAIKPNLVQTLEGTPAFVHGGPFANIAHGCNSVLATKTALKL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 636 vgSEgFVVTESGHGADVGLEKFFNIKCLYSGLQPDVLVMVATIRTLKMQGGAPPiqaglplpKEYLQENLKQLERGCCHM 715
Cdd:PRK13505 293 --AD-YVVTEAGFGADLGAEKFLDIKCRKAGLKPDAVVIVATVRALKMHGGVAK--------DDLKEENVEALKKGFANL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 716 RRQVEKAQAFGLPVIVAVNKFSSDTDAELELVCGQARQAGAfDAVQCSSWSEGGAGALALAETVQRAA-KLPACFKFLYD 794
Cdd:PRK13505 362 ERHIENIRKFGVPVVVAINKFVTDTDAEIAALKELCEELGV-EVALSEVWAKGGEGGVELAEKVVELIeEGESNFKPLYD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 795 LQTPASDKLRTVAQKMYGLKDVKLSPKAKEKLALYTKQGFENLPVCIAKTPLSLSNDPMMKGSSTDFMLPITDIKANAGA 874
Cdd:PRK13505 441 DEDSLEEKIEKIATKIYGAKGVEFSPKAKKQLKQIEKNGWDKLPVCMAKTQYSFSDDPKLLGAPTGFTITVRELRPSAGA 520
|
....*....
gi 1207192431 875 GFLCCLTGS 883
Cdd:PRK13505 521 GFIVALTGD 529
|
|
| PRK13507 |
PRK13507 |
formate--tetrahydrofolate ligase; Provisional |
327-883 |
7.70e-148 |
|
formate--tetrahydrofolate ligase; Provisional
Pssm-ID: 184098 Cd Length: 587 Bit Score: 449.55 E-value: 7.70e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 327 DAAISSSCES--KPVVQLARELGLFSDEVESYGRSRAKIR-LDALKRMEKQPNGKYVVVTGVTSSPLGEGKRTTALGLAQ 403
Cdd:PRK13507 10 DWEIAEEAEKfmKPVEELAEELGLTKEELLPYGHYIAKVDfRKVLDRLKDRPDGKYIDVTAITPTPLGEGKSTTTMGLVQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 404 ALGAhLNTNAFACVQKSSLETCFGARGPAVGGGYSQIIPLEEVSLQPSGQNELVSAAGRLVMDTVKAYAHYETKLSEkal 483
Cdd:PRK13507 90 GLGK-RGKKVSGAIRQPSGGPTMNIKGSAAGGGLSQCIPLTPFSLGLTGDINAIMNAHNLAMVALTARMQHERNYTD--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 484 fdllvplregqrcvslAQLNR--LKKLAIeksDPLTLTEREIRRFI-----RLDIDTDSATDSFSLEN--------EMMA 548
Cdd:PRK13507 166 ----------------EQLARrgLKRLDI---DPTRVEMGWIIDFCaqalrNIIIGIGGKTDGYMMQSgfgiavssEVMA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 549 VLSLSSSEEEMQHRLANIIVATNKSGDPITTEDLNVSGPLAMLLKEALKPVLMQTVEGTPVFLHTSPLVNVAQGGPSILA 628
Cdd:PRK13507 227 ILSVATDLKDLRERIGKIVVAYDKNGKPVTTADLEVDGAMTAWMVRAINPNLLQTIEGQPVFVHAGPFANIAIGQSSIIA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 629 DKMALKIvgsEGFVVTESGHGADVGLEKFFNIKCLYSGLQPDVLVMVATIRTLKMQGGAPPIQAGLPLPKEYLQENLKQL 708
Cdd:PRK13507 307 DRVGLKL---ADYHVTESGFGADIGFEKFWNLKCRLSGLKPDCAVIVATIRALKMHGGGPKVVPGKPLPEEYTKENVGLV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 709 ERGCCHMRRQVEKAQAFGLPVIVAVNKFSSDTDAELELVCGQARQAGAFDAVQcSSWSEGGAGALALAETVQRAAKLPAC 788
Cdd:PRK13507 384 EKGCANLLHHIGTVKKSGINPVVCINAFYTDTHAEIAIVRRLAEQAGARVAVS-RHWEKGGEGALELADAVIDACNEPND 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 789 FKFLYDLQTPASDKLRTVAQKMYGLKDVKLSPKAKEKLA-LYTKQGFENLPVCIAKTPLSLSNDPMMKGSSTDFMLPITD 867
Cdd:PRK13507 463 FKFLYPLEMPLRERIETIAREVYGADGVSYTPEAEAKLKrLESDPETADFGTCMVKTHLSLSHDPALKGVPKGWTLPIRD 542
|
570
....*....|....*.
gi 1207192431 868 IKANAGAGFLCCLTGS 883
Cdd:PRK13507 543 ILTYGGAGFVVPVAGD 558
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
50-301 |
7.70e-128 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 386.29 E-value: 7.70e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLdsinP--INTEKITNAVA 127
Cdd:COG0190 39 LVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLALIDELNADPSVHGILVQLPL----PkhIDEEAVLEAID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 128 PEKDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKT 207
Cdd:COG0190 115 PEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERYGIDLAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 208 PDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDeskasgKRVVGDVHYPSAKQRAGFITPVPGGVGPMT 287
Cdd:COG0190 193 KDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVED------GKLVGDVDFESVAEKASAITPVPGGVGPMT 266
|
250
....*....|....
gi 1207192431 288 VAMLMKNTVESAKR 301
Cdd:COG0190 267 IAMLLENTLKAAER 280
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-301 |
1.09e-98 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 310.74 E-value: 1.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PRK14188 39 LVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALIARLNADPAIHGILVQLPLP--KHLDSEAVIQAIDPE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14188 117 KDVDGLHVVNAGRLATGE--TALVPCTPLGCMMLLRRVHGDLSGLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKASGK-RVVGDVHYPSAKQRAGFITPVPGGVGPMTV 288
Cdd:PRK14188 195 LPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPAPEKGEGKtRLVGDVAFAEAAEVAGAITPVPGGVGPMTI 274
|
250
....*....|...
gi 1207192431 289 AMLMKNTVESAKR 301
Cdd:PRK14188 275 ACLLANTLTAACR 287
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-301 |
1.79e-98 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 309.63 E-value: 1.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLdsinP--INTEKITNAVA 127
Cdd:PRK14190 39 LVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALIDRLNADPRINGILVQLPL----PkhIDEKAVIERIS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 128 PEKDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKT 207
Cdd:PRK14190 115 PEKDVDGFHPINVGRMMLGQ--DTFLPCTPHGILELLKEYNIDISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 208 PDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIpdeskASGKrVVGDVHYPSAKQRAGFITPVPGGVGPMT 287
Cdd:PRK14190 193 KNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRL-----ENGK-LCGDVDFDNVKEKASYITPVPGGVGPMT 266
|
250
....*....|....
gi 1207192431 288 VAMLMKNTVESAKR 301
Cdd:PRK14190 267 ITMLMHNTVELAKR 280
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
128-300 |
6.09e-95 |
|
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: 295.62 E-value: 6.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 128 PEKDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKT 207
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 208 PDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKasgKRVVGDVHYPSAKQRAGFITPVPGGVGPMT 287
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDKSG---GKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 1207192431 288 VAMLMKNTVESAK 300
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
50-301 |
1.71e-92 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 294.49 E-value: 1.71e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PLN02516 46 IVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELISKVHELNANPDVHGILVQLPLP--KHINEEKILNEISLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PLN02516 124 KDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIPIKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKASGKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PLN02516 204 PESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSDPSKKSGYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVA 283
|
250
....*....|..
gi 1207192431 290 MLMKNTVESAKR 301
Cdd:PLN02516 284 MLLKNTVDGAKR 295
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
50-301 |
2.38e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 285.43 E-value: 2.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14189 39 LVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLARIDELNRDPKIHGILVQLPLPK--HIDSHKVIEAIAPE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGdcFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14189 117 KDVDGFHVANAGALMTGQPL--FRPCTPYGVMKMLESIGIPLRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHiPDESKasgkrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14189 195 LAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNR-DDAGK-----LCGDVDFAGVKEVAGYITPVPGGVGPMTIT 268
|
250
....*....|..
gi 1207192431 290 MLMKNTVESAKR 301
Cdd:PRK14189 269 MLLVNTIEAAER 280
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-302 |
2.44e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 285.27 E-value: 2.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSInpINTEKITNAVAPE 129
Cdd:PRK10792 40 LVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLALIDELNADPTIDGILVQLPLPAH--IDNVKVLERIHPD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLS------RgdlgdcfiPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTC 203
Cdd:PRK10792 118 KDVDGFHPYNVGRLAqripllR--------PCTPRGIMTLLERYGIDTYGLNAVVVGASNIVGRPMSLELLLAGCTVTVC 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 204 HSKTPDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDeskasGKrVVGDVHYPSAKQRAGFITPVPGGV 283
Cdd:PRK10792 190 HRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLED-----GK-LVGDVEFETAAERASWITPVPGGV 263
|
250
....*....|....*....
gi 1207192431 284 GPMTVAMLMKNTVESAKRF 302
Cdd:PRK10792 264 GPMTVATLLENTLQACEEY 282
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
136-303 |
5.95e-88 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 276.65 E-value: 5.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 136 TSINAGKLSRGdlGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPDLAEQVG 215
Cdd:pfam02882 1 HPYNLGRLVLG--KPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 216 KADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIpdeskaSGKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVAMLMKNT 295
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRV------GNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 1207192431 296 VESAKRFL 303
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
50-301 |
5.45e-84 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 274.19 E-value: 5.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PLN02616 110 LVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFISGFNNDPSVHGILVQLPLPS--HMDEQNILNAVSIE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PLN02616 188 KDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYNVEIKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKN 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKASGKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PLN02616 268 PEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDASSPRGYRLVGDVCYEEACKVASAVTPVPGGVGPMTIA 347
|
250
....*....|..
gi 1207192431 290 MLMKNTVESAKR 301
Cdd:PLN02616 348 MLLSNTLTSAKR 359
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
50-301 |
6.15e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 263.15 E-value: 6.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PRK14179 39 LVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDLIERYNQDPTWHGILVQLPLP--KHINEEKILLAIDPK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14179 117 KDVDGFHPMNTGHLWSGR--PVMIPCTPAGIMEMFREYNVELEGKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHipDEskaSGKrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14179 195 LAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNR--DE---NGK-LIGDVDFDEVAEVASYITPVPGGVGPMTIT 268
|
250
....*....|..
gi 1207192431 290 MLMKNTVESAKR 301
Cdd:PRK14179 269 MLMEQTYQAALR 280
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-300 |
8.85e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 262.78 E-value: 8.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14191 38 LVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLIKDLNTDQNIDGILVQLPLPR--HIDTKMVLEAIDPN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14191 116 KDVDGFHPLNIGKLCSQL--DGFVPATPMGVMRLLKHYHIEIKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDeskasgKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14191 194 LSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLND------GRLVGDVDFENVAPKASFITPVPGGVGPMTIV 267
|
250
....*....|.
gi 1207192431 290 MLMKNTVESAK 300
Cdd:PRK14191 268 SLLENTLIAAE 278
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
50-301 |
9.20e-81 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 264.90 E-value: 9.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PLN02897 93 LVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPLP--QHLDESKILNMVRLE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PLN02897 171 KDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKASGKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PLN02897 251 PEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTIT 330
|
250
....*....|..
gi 1207192431 290 MLMKNTVESAKR 301
Cdd:PLN02897 331 MLLCNTLDAAKR 342
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
34-302 |
3.71e-80 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 261.29 E-value: 3.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 34 SVSRFQAwSCGAAGGH---LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLP 110
Cdd:PRK14174 20 RVEAYRA-KTGKVPGLtviIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQQP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 111 LDSinPINTEKITNAVAPEKDVDGLTSINAGKLSRGDLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMH 190
Cdd:PRK14174 99 LPK--QIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIETKGKHCVVVGRSNIVGKPMA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 191 DLLL----WSHATVTTCHSKTPDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKASGKRVVGDVHY 266
Cdd:PRK14174 177 NLMLqklkESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIEDPSTKSGYRLVGDVDY 256
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207192431 267 PSAKQRAGFITPVPGGVGPMTVAMLMKNTVESAKRF 302
Cdd:PRK14174 257 EGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-300 |
5.78e-77 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 252.01 E-value: 5.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PRK14172 39 LVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIEELNKDNNVHGIMLQLPLP--KHLDEKKITNKIDAN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14172 117 KDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNIDIEGKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGInhipdeSKASGKrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14172 195 LKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGT------SSVNGK-ITGDVNFDKVIDKASYITPVPGGVGSLTTT 267
|
250
....*....|.
gi 1207192431 290 MLMKNTVESAK 300
Cdd:PRK14172 268 LLIKNVCEALK 278
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
51-301 |
8.36e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 252.29 E-value: 8.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 51 VGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPEK 130
Cdd:PRK14186 40 VGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEALIAQLNQDERVDGILLQLPLPK--HLDEVPLLHAIDPDK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 131 DVDGLTSINAGKLSRGDLGdcFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPDL 210
Cdd:PRK14186 118 DADGLHPLNLGRLVKGEPG--LRSCTPAGVMRLLRSQQIDIAGKKAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 211 AEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKASgkRVVGDVHYPSAKQRAGFITPVPGGVGPMTVAM 290
Cdd:PRK14186 196 ASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLPSSDGKT--RLCGDVDFEEVEPVAAAITPVPGGVGPMTVTM 273
|
250
....*....|.
gi 1207192431 291 LMKNTVESAKR 301
Cdd:PRK14186 274 LLVNTVLSWQK 284
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-299 |
7.66e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 247.05 E-value: 7.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PRK14187 39 LVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINELNNDDSVHGILVQLPVP--NHIDKNLIINTIDPE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14187 117 KDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTITRNLSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKasgKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14187 197 LADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEEGGV---KKFVGDVDFAEVKKKASAITPVPGGVGPMTIA 273
|
250
....*....|
gi 1207192431 290 MLMKNTVESA 299
Cdd:PRK14187 274 FLMVNTVIAA 283
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-303 |
4.28e-74 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 244.35 E-value: 4.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14183 38 LVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIAMMNNNPNIDGILVQLPLPK--HIDTTKILEAIDPK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14183 116 KDVDGFHPYNVGRLVTGL--DGFVPCTPLGVMELLEEYEIDVKGKDVCVVGASNIVGKPMAALLLNANATVDICHIFTKD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDeskasgKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14183 194 LKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTED------GRLVGDVDFENVAKKCSYITPVPGGVGPMTIA 267
|
250
....*....|....
gi 1207192431 290 MLMKNTVESAKRFL 303
Cdd:PRK14183 268 MLLSNTLKAAKNRA 281
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-299 |
3.75e-73 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 242.37 E-value: 3.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PRK14167 38 LMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTIDELNADEDVHGILVQMPVP--DHVDDREVLRRIDPA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGdcFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLW----SHATVTTCHS 205
Cdd:PRK14167 116 KDVDGFHPENVGRLVAGDAR--FKPCTPHGIQKLLAAAGVDTEGADVVVVGRSDIVGKPMANLLIQkadgGNATVTVCHS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 206 KTPDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIpDESKASGKRVVGDVHYPSAKQRAGFITPVPGGVGP 285
Cdd:PRK14167 194 RTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRV-DADTEKGYELVGDVEFESAKEKASAITPVPGGVGP 272
|
250
....*....|....
gi 1207192431 286 MTVAMLMKNTVESA 299
Cdd:PRK14167 273 MTRAMLLYNTVKAA 286
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
51-301 |
1.32e-71 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 238.00 E-value: 1.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 51 VGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPEK 130
Cdd:PRK14182 38 VGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPLP--KHVDERAVLDAISPAK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 131 DVDGLTSINAGKLSRGDLGdCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPDL 210
Cdd:PRK14182 116 DADGFHPFNVGALSIGIAG-VPRPCTPAGVMRMLDEARVDPKGKRALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 211 AEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDeskasgKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVAM 290
Cdd:PRK14182 195 AGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLAD------GKLVGDVEFAAAAARASAITPVPGGVGPMTRAM 268
|
250
....*....|.
gi 1207192431 291 LMKNTVESAKR 301
Cdd:PRK14182 269 LLVNTVELAKR 279
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
51-301 |
1.73e-71 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 237.81 E-value: 1.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 51 VGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPEK 130
Cdd:PRK14173 37 LGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLELIARLNADPEVDGILVQLPLPP--HIDFQRVLEAIDPLK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 131 DVDGLTSINAGKLSRGdlGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPDL 210
Cdd:PRK14173 115 DVDGFHPLNVGRLWMG--GEALEPCTPAGVVRLLKHYGIPLAGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 211 AEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDEskASGKRVVGDVHyPSAKQRAGFITPVPGGVGPMTVAM 290
Cdd:PRK14173 193 PAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGGN--GGRDILTGDVH-PEVAEVAGALTPVPGGVGPMTVAM 269
|
250
....*....|.
gi 1207192431 291 LMKNTVESAKR 301
Cdd:PRK14173 270 LMANTVIAALR 280
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-300 |
2.13e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 237.05 E-value: 2.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14178 33 IVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDINGILVQLPLPK--GVDTERVIAAILPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGdcFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14178 111 KDVDGFHPLNLGRLVSGLPG--FAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVGRPMAALLLNADATVTICHSKTEN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIpdeskaSGKrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14178 189 LKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQV------NGK-LCGDVDFDAVKEIAGAITPVPGGVGPMTIA 261
|
250
....*....|.
gi 1207192431 290 MLMKNTVESAK 300
Cdd:PRK14178 262 TLMENTFDAAK 272
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-309 |
4.03e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 234.35 E-value: 4.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14194 40 LVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIAELNADPSVNGILLQLPLPA--HIDEARVLQAINPL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14194 118 KDVDGFHSENVGGLSQGR--DVLTPCTPSGCLRLLEDTCGDLTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKAsgkRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14194 196 AKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDDDGRS---RLVGDVDFDSALPVVSAITPVPGGVGPMTIA 272
|
250 260
....*....|....*....|
gi 1207192431 290 MLMKNTVESAKrfLQTHTPG 309
Cdd:PRK14194 273 FLMKNTVTAAR--LQAHAQR 290
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-301 |
4.33e-70 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 233.75 E-value: 4.33e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLdsinP--INTEKITNAVA 127
Cdd:PRK14193 39 LVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAVIDELNADPACTGYIVQLPL----PkhLDENAVLERID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 128 PEKDVDGLTSINAGKLSRGDLGDcfIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSH--ATVTTCHS 205
Cdd:PRK14193 115 PAKDADGLHPTNLGRLVLNEPAP--LPCTPRGIVHLLRRYDVELAGAHVVVIGRGVTVGRPIGLLLTRRSenATVTLCHT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 206 KTPDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGInhipdeSKASGKRVVGDVHyPSAKQRAGFITPVPGGVGP 285
Cdd:PRK14193 193 GTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGV------SRAGDGKLVGDVH-PDVWEVAGAVSPNPGGVGP 265
|
250
....*....|....*.
gi 1207192431 286 MTVAMLMKNTVESAKR 301
Cdd:PRK14193 266 MTRAFLLTNVVERAER 281
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-300 |
4.90e-70 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 233.51 E-value: 4.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14184 38 LVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAELNARPDIDGILLQLPLPK--GLDSQRCLELIDPA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLL----WSHATVTTCHS 205
Cdd:PRK14184 116 KDVDGFHPENMGRLALGL--PGFRPCTPAGVMTLLERYGLSPAGKKAVVVGRSNIVGKPLALMLGapgkFANATVTVCHS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 206 KTPDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDEskasgkrVVGDVHYPSAKQRAGFITPVPGGVGP 285
Cdd:PRK14184 194 RTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDG-------LVGDCDFEGLSDVASAITPVPGGVGP 266
|
250
....*....|....*
gi 1207192431 286 MTVAMLMKNTVESAK 300
Cdd:PRK14184 267 MTIAQLLVNTVQSWK 281
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-303 |
2.90e-68 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 228.92 E-value: 2.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14176 45 LVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDSLNKRKDVHGILLQLPLPK--HLDPQEAMEAIDPA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGdcFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14176 123 KDADGFHPYNMGKLMIGDEG--LVPCTPHGVIRALEEYGVDIEGKNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINhipdesKASGKrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14176 201 LKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGIT------KEEDK-VYGDVDFENVIKKASLITPVPGGVGPLTIA 273
|
250
....*....|....
gi 1207192431 290 MLMKNTVESAKRFL 303
Cdd:PRK14176 274 MLMKHVLMCAEKSL 287
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-300 |
1.16e-67 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 227.45 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14168 40 LVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLALIDKYNNDDSIHGILVQLPLPK--HINEKKVLNAIDPD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLW----SHATVTTCHS 205
Cdd:PRK14168 118 KDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLVRSGVETSGAEVVVVGRSNIVGKPIANMMTQkgpgANATVTIVHT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 206 KTPDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKASGKRVVGDVHYPSAKQRAGFITPVPGGVGP 285
Cdd:PRK14168 198 RSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVGTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGP 277
|
250
....*....|....*
gi 1207192431 286 MTVAMLMKNTVESAK 300
Cdd:PRK14168 278 MTIAMLMRNTLKSAK 292
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-300 |
3.00e-67 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 226.01 E-value: 3.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14177 40 LVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDKLNLDPNVDGILLQHPVPS--QIDERAAFDRIALE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14177 118 KDVDGVTTLSFGKLSMGV--ETYLPCTPYGMVLLLKEYGIDVTGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINhiPDEskasgkrvVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14177 196 LPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGN--------VGDIEISKAKDKSSFYTPVPGGVGPMTIA 265
|
250
....*....|.
gi 1207192431 290 MLMKNTVESAK 300
Cdd:PRK14177 266 VLLLQTLYSFK 276
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-304 |
6.93e-67 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 224.90 E-value: 6.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14166 37 LVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINTLNHDDSVHGILVQLPLPD--HICKDLILESIISS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGdLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14166 115 KDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEIDLEGKDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIpdeskASGKrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14166 194 LSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRL-----ESGK-IVGDVDFEEVSKKSSYITPVPGGVGPMTIA 267
|
250
....*....|....*
gi 1207192431 290 MLMKNTVESAKRFLQ 304
Cdd:PRK14166 268 MLLENTVKSAKNRLN 282
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-301 |
1.04e-66 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 224.57 E-value: 1.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14170 38 LVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVEELNEDKTIHGILVQLPLPE--HISEEKVIDTISYD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14170 116 KDVDGFHPVNVGNLFIGK--DSFVPCTPAGIIELIKSTGTQIEGKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHipDESkasgKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14170 194 LPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDR--DEN----NKLCGDVDFDDVVEEAGFITPVPGGVGPMTIT 267
|
250
....*....|..
gi 1207192431 290 MLMKNTVESAKR 301
Cdd:PRK14170 268 MLLANTLKAAKR 279
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-305 |
2.03e-66 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 224.07 E-value: 2.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PRK14171 39 LVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINELNLDNEISGIIVQLPLP--SSIDKNKILSAVSPS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGdLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14171 117 KDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPNLTGKNVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIpdeskaSGKRVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14171 196 LSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRI------SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIA 269
|
250
....*....|....*.
gi 1207192431 290 MLMKNTVESAKRFLQT 305
Cdd:PRK14171 270 FLLKNTVKAFKDSLYT 285
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-301 |
2.51e-65 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 221.24 E-value: 2.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PRK14185 38 LVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGFIVQLPLP--KHISEQKVIEAIDYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSH----ATVTTCHS 205
Cdd:PRK14185 116 KDVDGFHPINVGRMSIGL--PCFVSATPNGILELLKRYHIETSGKKCVVLGRSNIVGKPMAQLMMQKAypgdCTVTVCHS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 206 KTPDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESKASGKRVVGDVHYPSAKQRAGFITPVPGGVGP 285
Cdd:PRK14185 194 RSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDATRKSGFKLTGDVKFDEVAPKCSYITPVPGGVGP 273
|
250
....*....|....*.
gi 1207192431 286 MTVAMLMKNTVESAKR 301
Cdd:PRK14185 274 MTIVSLMKNTLLAGKK 289
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-301 |
2.86e-65 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 220.56 E-value: 2.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14175 39 LVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNNDDSVSGILVQVPLPK--QVSEQKILEAINPE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14175 117 KDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADIDLEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGinHIPDEskaSGKrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14175 195 MASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG--NTPDE---NGK-LKGDVDYDAVKEIAGAITPVPGGVGPLTIT 268
|
250
....*....|..
gi 1207192431 290 MLMKNTVESAKR 301
Cdd:PRK14175 269 MVLNNTLLAEKM 280
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-304 |
2.26e-62 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 212.40 E-value: 2.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14192 40 LVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKIEELNANPDVHGILLQHPVPA--QIDERACFDAISLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlgDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14192 118 KDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKAYNIELAGKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINhiPDESKAsgkrvVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14192 196 LPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFH--PRDGGG-----VGDIELQGIEEIASAYTPVPGGVGPMTIN 268
|
250
....*....|....*
gi 1207192431 290 MLMKNTVESAKRFLQ 304
Cdd:PRK14192 269 TLIRQTVEAAEKALG 283
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-302 |
3.96e-62 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 212.03 E-value: 3.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDsiNPINTEKITNAVAPE 129
Cdd:PRK14181 33 LIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGILVQLPLP--KHLDAQAILQAISPD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGDcFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSH----ATVTTCHS 205
Cdd:PRK14181 111 KDVDGLHPVNMGKLLLGETDG-FIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLMQKHpdtnATVTLLHS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 206 KTPDLAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESkASGKRVVGDVHYPSAKQRAGFITPVPGGVGP 285
Cdd:PRK14181 190 QSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAAN-PKGYILVGDVDFNNVVPKCRAITPVPGGVGP 268
|
250
....*....|....*..
gi 1207192431 286 MTVAMLMKNTVESAKRF 302
Cdd:PRK14181 269 MTVAMLMRNTWESYLRH 285
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
50-301 |
1.81e-61 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 210.19 E-value: 1.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14169 37 LVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKVAELNHDPDVDAILVQLPLPA--GLDEQAVIDAIDPD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDLGdcFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14169 115 KDVDGFSPVSVGRLWANEPT--VVASTPYGIMALLDAYDIDVAGKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIPDESkasgkrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14169 193 LKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRGADGK------LLGDVDEAAVAPIASAITPVPGGVGPMTIA 266
|
250
....*....|..
gi 1207192431 290 MLMKNTVESAKR 301
Cdd:PRK14169 267 SLMAQTVTLAKR 278
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
50-302 |
2.52e-61 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 209.50 E-value: 2.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLDSinPINTEKITNAVAPE 129
Cdd:PRK14180 38 IVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELIDQLNNDSSVHAILVQLPLPA--HINKNNVIYSIKPE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 130 KDVDGLTSINAGKLSRGDlGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPD 209
Cdd:PRK14180 116 KDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKTEGAYAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 210 LAEQVGKADILVVGAGRAEMVKGEWVKEGAVVIDCGINHIpdeskaSGKrVVGDVHYPSAKQRAGFITPVPGGVGPMTVA 289
Cdd:PRK14180 195 LKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHV------DGK-IVGDVDFAAVKDKVAAITPVPGGVGPMTIT 267
|
250
....*....|...
gi 1207192431 290 MLMKNTVESAKRF 302
Cdd:PRK14180 268 ELLYNTFQCAQEL 280
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
146-300 |
1.52e-44 |
|
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: 157.28 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 146 GDLGDCFIPCTPNGCMELISQTGVSVMGKNAVVIGRSKIVGAPMHDLLLWSHATVTTCHSKTPDLAEQVGKADILVVGAG 225
Cdd:cd05212 1 GPCTPLFVSPVAKAVKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192431 226 RAEMVKGEWVKEGAVVIDCGINHIPDEskasgkrvvgdvhypSAKQRAGFITPVPGGVGPMTVAMLMKNTVESAK 300
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPTKLSGD---------------DVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
50-133 |
5.73e-32 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 120.20 E-value: 5.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 50 LVGDREDSNLYISMKLKAAAEIGINANHIRLPETATENEVLRNIVAVNENPAFHGLIVQLPLdsinP--INTEKITNAVA 127
Cdd:pfam00763 34 LVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKLNADPSVHGILVQLPL----PkhIDEEKVLEAID 109
|
....*.
gi 1207192431 128 PEKDVD 133
Cdd:pfam00763 110 PEKDVD 115
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
128-296 |
2.99e-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: 63.60 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 128 PEKDVDGLTSINAGKL---SRGDLGD----CFIPCTPNGCMELISQTGV---------SVMGKNAVVIGRSKIVGAPMHD 191
Cdd:cd01079 1 PHKDVEGLSHKYIFNLyhnIRFLDPEnrkkSILPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192431 192 LLLWSHATV---------------------TTCHSKTPDLAEQVGKADILVVGAGRAEM-VKGEWVKEGAVVIDcginhi 249
Cdd:cd01079 81 LLANDGARVysvdingiqvftrgesirhekHHVTDEEAMTLDCLSQSDVVITGVPSPNYkVPTELLKDGAICIN------ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207192431 250 pdeskASGKRVVGdvhyPSAKQRAGFITPVpggVGPMTVAMLMKNTV 296
Cdd:cd01079 155 -----FASIKNFE----PSVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| |
