|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
287-568 |
0e+00 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 553.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14180 1 MILIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14180 81 IDQLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLESCTPKGIMTMLREYGIKTEGAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGKIVG 526
Cdd:PRK14180 161 AVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDGKIVG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1735523678 527 DVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQELNR 568
Cdd:PRK14180 241 DVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQELNR 282
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
287-564 |
0e+00 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 510.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:COG0190 3 AQILDGKAVAAEIREELKERVAALKAK-GITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKkCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:COG0190 82 IDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEP-GFVPCTPAGIMELLERYGIDLAGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHV-DGKIV 525
Cdd:COG0190 161 AVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVeDGKLV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1735523678 526 GDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:COG0190 241 GDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAE 279
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
288-567 |
2.16e-149 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 430.59 E-value: 2.16e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 288 TLIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELI 367
Cdd:PRK14190 4 VIIDGKEVAKEKREQLKEEVVKLKEQ-GIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLALI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 368 DKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLrDKKCLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14190 83 DRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMML-GQDTFLPCTPHGILELLKEYNIDISGKHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVD-GKIVG 526
Cdd:PRK14190 162 VVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLEnGKLCG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1735523678 527 DVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQELN 567
Cdd:PRK14190 242 DVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAG 282
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
287-566 |
1.08e-147 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 426.25 E-value: 1.08e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MT--LIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELL 364
Cdd:PRK10792 1 MTakIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 365 ELIDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKcLESCTPKGILTMLKEYGIQTEG 444
Cdd:PRK10792 81 ALIDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPL-LRPCTPRGIMTLLERYGIDTYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 445 AHAVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHV-DGK 523
Cdd:PRK10792 160 LNAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLeDGK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1735523678 524 IVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQEL 566
Cdd:PRK10792 240 LVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEY 282
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
288-564 |
1.18e-130 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 382.88 E-value: 1.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 288 TLIDGKKLSIDLKERLADQLREYKEqTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELI 367
Cdd:PRK14189 4 QLIDGNALSKQLRAEAAQRAAALTA-RGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLARI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 368 DKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14189 83 DELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGAL-MTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVD-GKIVG 526
Cdd:PRK14189 162 VVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDaGKLCG 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 1735523678 527 DVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:PRK14189 242 DVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAE 279
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
287-564 |
3.31e-129 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 379.50 E-value: 3.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14191 1 MVLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14191 81 IKDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKL-CSQLDGFVPATPMGVMRLLKHYHIEIKGKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHV-DGKIV 525
Cdd:PRK14191 160 VVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLnDGRLV 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 1735523678 526 GDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:PRK14191 240 GDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAE 278
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
287-563 |
1.15e-124 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 367.54 E-value: 1.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHL-WSGRPVMIPCTPAGIMEMFREYNVELEGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINH-VDGKIV 525
Cdd:PRK14179 161 AVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRdENGKLI 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 1735523678 526 GDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCA 563
Cdd:PRK14179 241 GDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAA 278
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
287-567 |
1.56e-124 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 367.61 E-value: 1.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14174 1 MLIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRD-KKCLESCTPKGILTMLKEYGIQTEGA 445
Cdd:PRK14174 81 IEDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHlDKCFVSCTPYGILELLGRYNIETKGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 446 HAVVVGASNIVGKPVSQLLLN----AKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVD 521
Cdd:PRK14174 161 HCVVVGRSNIVGKPMANLMLQklkeSNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1735523678 522 G-------KIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQELN 567
Cdd:PRK14174 241 DpstksgyRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERVN 293
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
287-560 |
1.14e-123 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 365.54 E-value: 1.14e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLI-DGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLE 365
Cdd:PRK14186 1 MALIlDGKALAAEIEQRLQAQIESNLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 366 LIDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGA 445
Cdd:PRK14186 81 LIAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRL-VKGEPGLRSCTPAGVMRLLRSQQIDIAGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 446 HAVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHV----- 520
Cdd:PRK14186 160 KAVVVGRSILVGKPLALMLLAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLpssdg 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1735523678 521 DGKIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTF 560
Cdd:PRK14186 240 KTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTV 279
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
289-565 |
1.85e-122 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 362.20 E-value: 1.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKcLESCTPKGILTMLKEYGIQTEGAHAV 448
Cdd:PRK14176 90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEG-LVPCTPHGVIRALEEYGVDIEGKNAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 449 VVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGKIVGDV 528
Cdd:PRK14176 169 IVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEEDKVYGDV 248
|
250 260 270
....*....|....*....|....*....|....*..
gi 1735523678 529 DFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQE 565
Cdd:PRK14176 249 DFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
288-567 |
2.08e-122 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 362.35 E-value: 2.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 288 TLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELI 367
Cdd:PRK14188 3 TIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLALI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 368 DKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLrDKKCLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14188 83 ARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLAT-GETALVPCTPLGCMMLLRRVHGDLSGLNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDG----- 522
Cdd:PRK14188 162 VVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPApekge 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1735523678 523 ---KIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQELN 567
Cdd:PRK14188 242 gktRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRAA 289
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
287-561 |
7.16e-120 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 355.62 E-value: 7.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14184 1 MLLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLrDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14184 81 IAELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLAL-GLPGFRPCTPAGVMTLLERYGLSPAGKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLN----AKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDG 522
Cdd:PRK14184 160 AVVVGRSNIVGKPLALMLGApgkfANATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDD 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 1735523678 523 KIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQ 561
Cdd:PRK14184 240 GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQ 278
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
287-568 |
2.84e-119 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 353.95 E-value: 2.84e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14166 1 MTLLDGKALSAKIKEELKEKNQFLKSK-GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14166 80 INTLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESGFLPCTPLGVMKLLKAYEIDLEGKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVD-GKIV 525
Cdd:PRK14166 160 AVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLEsGKIV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1735523678 526 GDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQelNR 568
Cdd:PRK14166 240 GDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAK--NR 280
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
287-565 |
3.14e-115 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 343.35 E-value: 3.14e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14183 1 MQILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14183 81 IAMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRL-VTGLDGFVPCTPLGVMELLEEYEIDVKGKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHV-DGKIV 525
Cdd:PRK14183 160 VCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTeDGRLV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1735523678 526 GDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQE 565
Cdd:PRK14183 240 GDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKN 279
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
288-564 |
3.65e-114 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 340.67 E-value: 3.65e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 288 TLIDGKKLSidlkERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELI 367
Cdd:PRK14178 1 MILDGKAVS----EKRLELLKEEIIESGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 368 DKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14178 77 RRLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRL-VSGLPGFAPCTPNGIMTLLHEYKISIAGKRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGKIVGD 527
Cdd:PRK14178 156 VVVGRSIDVGRPMAALLLNADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNGKLCGD 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1735523678 528 VDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:PRK14178 236 VDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAK 272
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
289-568 |
7.99e-109 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 327.26 E-value: 7.99e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14175 5 ILDGKQIAKDYRQGLQDQVEALKEK-GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLrDKKCLESCTPKGILTMLKEYGIQTEGAHAV 448
Cdd:PRK14175 84 RLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYI-DEQTFVPCTPLGIMEILKHADIDLEGKNAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 449 VVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVG-INHVDGKIVGD 527
Cdd:PRK14175 163 VIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGnTPDENGKLKGD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1735523678 528 VDFEAVKDKVSAITPVPGGVGPMTITELLYNTFqCAQELNR 568
Cdd:PRK14175 243 VDYDAVKEIAGAITPVPGGVGPLTITMVLNNTL-LAEKMRR 282
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
288-565 |
7.76e-107 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 322.50 E-value: 7.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 288 TLIDGKKLSIDLKERLADQLrEYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELI 367
Cdd:PRK14167 3 EIIDGNAVAAQIRDDLTDAI-ETLEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 368 DKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKcLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14167 82 DELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDAR-FKPCTPHGIQKLLAAAGVDTEGADV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLN----AKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDG- 522
Cdd:PRK14167 161 VVVGRSDIVGKPMANLLIQkadgGNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDAd 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1735523678 523 -----KIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQE 565
Cdd:PRK14167 241 tekgyELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASL 288
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
287-565 |
4.66e-105 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 317.27 E-value: 4.66e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ-DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLrDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14169 80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWA-NEPTVVASTPYGIMALLDAYDIDVAGKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINH-VDGKIV 525
Cdd:PRK14169 159 VVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRgADGKLL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1735523678 526 GDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQE 565
Cdd:PRK14169 239 GDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKR 278
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
289-558 |
2.48e-101 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 307.86 E-value: 2.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14172 4 IINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGAHAV 448
Cdd:PRK14172 84 ELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKF-YKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 449 VVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGKIVGDV 528
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNGKITGDV 242
|
250 260 270
....*....|....*....|....*....|
gi 1735523678 529 DFEAVKDKVSAITPVPGGVGPMTITELLYN 558
Cdd:PRK14172 243 NFDKVIDKASYITPVPGGVGSLTTTLLIKN 272
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
288-564 |
5.04e-101 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 306.94 E-value: 5.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 288 TLIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELI 367
Cdd:PRK14193 4 IILDGKATADEIKADLAERVAALKEK-GITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNAVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 368 DKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCLeSCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14193 83 DELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPL-PCTPRGIVHLLRRYDVELAGAHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSqLLLNAK---ATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHV-DGK 523
Cdd:PRK14193 162 VVIGRGVTVGRPIG-LLLTRRsenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAgDGK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1735523678 524 IVGDVDfEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:PRK14193 241 LVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAE 280
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
288-565 |
9.92e-101 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 306.39 E-value: 9.92e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 288 TLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELI 367
Cdd:PRK14192 4 LVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLAKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 368 DKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKkCLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14192 84 EELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEA-AYGSATPAGIMRLLKAYNIELAGKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGKIVGD 527
Cdd:PRK14192 163 VVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGGGVGD 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 1735523678 528 VDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQE 565
Cdd:PRK14192 243 IELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEK 280
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
287-563 |
1.02e-100 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 306.37 E-value: 1.02e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSidlkERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14173 3 ARELSGPPAA----EAVYAELRARLAKLPFVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLrDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14173 79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWM-GGEALEPCTPAGVVRLLKHYGIPLAGKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGK--- 523
Cdd:PRK14173 158 VVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGGNggr 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1735523678 524 --IVGDVDFEaVKDKVSAITPVPGGVGPMTITELLYNTFQCA 563
Cdd:PRK14173 238 diLTGDVHPE-VAEVAGALTPVPGGVGPMTVAMLMANTVIAA 278
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
289-563 |
4.05e-100 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 305.21 E-value: 4.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKK-CLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14187 84 ELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKnCLIPCTPKGCLYLIKTITRNLSGSDA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVD----GK 523
Cdd:PRK14187 164 VVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEeggvKK 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1735523678 524 IVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCA 563
Cdd:PRK14187 244 FVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
287-559 |
5.91e-99 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 302.13 E-value: 5.91e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14185 1 MQLIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLrDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14185 81 VRELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSI-GLPCFVSATPNGILELLKRYHIETSGKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLN----AKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDG 522
Cdd:PRK14185 160 CVVLGRSNIVGKPMAQLMMQkaypGDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPD 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1735523678 523 -------KIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNT 559
Cdd:PRK14185 240 atrksgfKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNT 283
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
283-564 |
4.56e-97 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 297.57 E-value: 4.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 283 SNQKMTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQE 362
Cdd:PLN02516 5 SDHVAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 363 LLELIDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCL-ESCTPKGILTMLKEYGIQ 441
Cdd:PLN02516 85 LISKVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLfLPCTPKGCLELLSRSGIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 442 TEGAHAVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVD 521
Cdd:PLN02516 165 IKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVS 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1735523678 522 G-------KIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:PLN02516 245 DpskksgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAK 294
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
289-567 |
5.89e-97 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 299.61 E-value: 5.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PLN02616 75 VIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKFIS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCL-ESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PLN02616 155 GFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLfVPCTPKGCIELLHRYNVEIKGKRA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDG----- 522
Cdd:PLN02616 235 VVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDasspr 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1735523678 523 --KIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQELN 567
Cdd:PLN02616 315 gyRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKRIH 361
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
289-564 |
6.25e-95 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 292.13 E-value: 6.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14194 6 LIDGKAAAARVLAQVREDVRTLKAA-GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLALIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRL-QLRDkkCLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14194 85 ELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLsQGRD--VLTPCTPSGCLRLLEDTCGDLTGKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVD----GK 523
Cdd:PRK14194 163 VVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDddgrSR 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1735523678 524 IVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:PRK14194 243 LVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAAR 283
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
289-563 |
1.29e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 286.00 E-value: 1.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14168 5 IIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLALID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQL-RDKKCLESCTPKGILTMLKEYGIQTEGAHA 447
Cdd:PRK14168 85 KYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIgGDEVKFLPCTPAGIQEMLVRSGVETSGAEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 448 VVVGASNIVGKPVSQLLLN----AKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGK 523
Cdd:PRK14168 165 VVVGRSNIVGKPIANMMTQkgpgANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVGTN 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1735523678 524 I-------VGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCA 563
Cdd:PRK14168 245 EstgkailSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSA 291
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
287-568 |
2.30e-92 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 284.99 E-value: 2.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 287 MTLIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLEL 366
Cdd:PRK14182 1 MNLIDGKQIAAKVKGEVATEVRALAAR-GVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 367 IDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCLESCTPKGILTMLKEYGIQTEGAH 446
Cdd:PRK14182 80 IARLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPRPCTPAGVMRMLDEARVDPKGKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 447 AVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHV-DGKIV 525
Cdd:PRK14182 160 ALVVGRSNIVGKPMAMMLLERHATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLaDGKLV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1735523678 526 GDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQELNR 568
Cdd:PRK14182 240 GDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKRTAR 282
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
408-564 |
2.56e-91 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 277.42 E-value: 2.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 408 HPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGAHAVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTK 487
Cdd:pfam02882 1 HPYNLGRL-VLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAEITRE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1735523678 488 ADILVVAVGKPGFITADMVKDGAVVIDVGINHV-DGKIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:pfam02882 80 ADIVVVAVGKPELIKADWIKPGAVVIDVGINRVgNGKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAK 157
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
289-565 |
2.91e-90 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 279.55 E-value: 2.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCLeSCTPKGILTMLKEYGIQTEGAHAV 448
Cdd:PRK14177 85 KLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYL-PCTPYGMVLLLKEYGIDVTGKNAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 449 VVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDgkiVGDV 528
Cdd:PRK14177 164 VVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGN---VGDI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1735523678 529 DFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQE 565
Cdd:PRK14177 241 EISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKE 277
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
400-564 |
3.35e-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: 274.82 E-value: 3.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 400 PEKDVDGFHPANIGRLqLRDKKCLESCTPKGILTMLKEYGIQTEGAHAVVVGASNIVGKPVSQLLLNAKATVTTCHRFTK 479
Cdd:cd01080 1 PEKDVDGLHPVNLGRL-ALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCHSKTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 480 DLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHV----DGKIVGDVDFEAVKDKVSAITPVPGGVGPMTITEL 555
Cdd:cd01080 80 NLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVpdksGGKLVGDVDFESAKEKASAITPVPGGVGPMTVAML 159
|
....*....
gi 1735523678 556 LYNTFQCAQ 564
Cdd:cd01080 160 MKNTVEAAK 168
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
280-564 |
1.31e-89 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 279.92 E-value: 1.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 280 IKLSN-QKMTLIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVT 358
Cdd:PLN02897 48 VSFETeQKTVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 359 TEQELLELIDKLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCL-ESCTPKGILTMLKE 437
Cdd:PLN02897 128 TEGQILSALRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLfVSCTPKGCVELLIR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 438 YGIQTEGAHAVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGI 517
Cdd:PLN02897 208 SGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGT 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1735523678 518 NHVDG-------KIVGDVDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:PLN02897 288 TPVEDsscefgyRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAK 341
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
289-566 |
2.25e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 277.34 E-value: 2.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14170 4 IIDGKKLAKEIQEKVTREVAELVKE-GKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLrDKKCLESCTPKGILTMLKEYGIQTEGAHAV 448
Cdd:PRK14170 83 ELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFI-GKDSFVPCTPAGIIELIKSTGTQIEGKRAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 449 VVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINH-VDGKIVGD 527
Cdd:PRK14170 162 VIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRdENNKLCGD 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 1735523678 528 VDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQEL 566
Cdd:PRK14170 242 VDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKRI 280
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
289-561 |
1.66e-87 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 272.60 E-value: 1.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 289 LIDGKKLSIDLKERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELID 368
Cdd:PRK14171 4 IIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 369 KLNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCLESCTPKGILTMLKEYGIQTEGAHAV 448
Cdd:PRK14171 84 ELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGISQGFIPCTALGCLAVIKKYEPNLTGKNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 449 VVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDG-KIVGD 527
Cdd:PRK14171 164 IIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGnKIIGD 243
|
250 260 270
....*....|....*....|....*....|....
gi 1735523678 528 VDFEAVKDKVSAITPVPGGVGPMTITELLYNTFQ 561
Cdd:PRK14171 244 VDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVK 277
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
301-564 |
2.91e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 250.93 E-value: 2.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 301 ERLADQLREYKEQTGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELIDKLNNDSSVHAIL 380
Cdd:PRK14181 10 EHILATIKENISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGIL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 381 VQLPLPTHINKQKVIYAIKPEKDVDGFHPANIGRLQLRDKKCLESCTPKGILTMLKEYGIQTEGAHAVVVGASNIVGKPV 460
Cdd:PRK14181 90 VQLPLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGETDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 461 SQLLL----NAKATVTTCHRFTKDLKSHTTKADILVVAVGKPGFITADMVKDGAVVIDVGINHVDGK------IVGDVDF 530
Cdd:PRK14181 170 AALLMqkhpDTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAAnpkgyiLVGDVDF 249
|
250 260 270
....*....|....*....|....*....|....
gi 1735523678 531 EAVKDKVSAITPVPGGVGPMTITELLYNTFQCAQ 564
Cdd:PRK14181 250 NNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYL 283
|
|
| PAP2_lipid_A_1_phosphatase |
cd03389 |
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ... |
47-233 |
2.29e-77 |
|
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from Francisella novicida selectively dephosphorylates lipid A at the 1-position. Lipid A is the membrane-anchor component of lipopolysaccharides (LPS), the major constituents of the outer membrane in many gram-negative bacteria.
Pssm-ID: 239483 Cd Length: 186 Bit Score: 242.23 E-value: 2.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 47 AFYNLDTPVENYIEHSMPEAVDNAFRYITDVGKAEYILIICGVIVLVRLFINIDKLSESTKIAFNKICIYSGFILATVAI 126
Cdd:cd03389 1 SYFYLDRPLALYIKALDGRILAGFFRTITDFGKSGWYLIPSLLLFLLFRFGDLRGLSAPSRARFPKAAWAGLFLFATVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 127 SGIVGQVLKIIIGRARPKFFLEYGSHYFQHFHApGYDFASMPSGHSITVGAMFIALFYIFPKFRYLWYVLIVVFAGSRII 206
Cdd:cd03389 81 SGILVNLLKFIIGRARPKLLFDDGLYGFDPFHA-DYAFTSFPSGHSATAGAAAAALALLFPRYRWAFILLALLIAFSRVI 159
|
170 180
....*....|....*....|....*..
gi 1735523678 207 VGSHYPSDVIFGVAFGCYCTAYIYYWM 233
Cdd:cd03389 160 VGAHYPSDVIAGSLLGAVTALALYQRF 186
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
290-405 |
1.89e-58 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 190.31 E-value: 1.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 290 IDGKKLSIDLKERLADQLREYKEQtGIVPKLVAIIVGDDPASKTYVGSKEKACEKVGINSEVITLPEVTTEQELLELIDK 369
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAG-GRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1735523678 370 LNNDSSVHAILVQLPLPTHINKQKVIYAIKPEKDVD 405
Cdd:pfam00763 80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| PAP2 |
pfam01569 |
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ... |
120-235 |
2.65e-26 |
|
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.
Pssm-ID: 426329 [Multi-domain] Cd Length: 124 Bit Score: 103.65 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 120 ILATVAISGIVGQVLKIIIGRARPKFFLEYGSHYFQHFHAPGYdFASMPSGHSITVGAMFIALFYIFPKFRY-------- 191
Cdd:pfam01569 2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLPGL-GYSFPSGHSATAFALALLLALLLRRLRKivrvllal 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1735523678 192 LWYVLIVVFAGSRIIVGSHYPSDVIFGVAFGCYCTAYIYYWMLN 235
Cdd:pfam01569 81 LLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVYRLVPK 124
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
426-561 |
1.54e-25 |
|
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: 102.20 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 426 CTPKGILTMLKE-------YGIQTEGAHAVVVGASNIVGKPVSQLLLNAKATVTTCHRFTKDLKSHTTKADILVVAVGKP 498
Cdd:cd05212 3 CTPLFVSPVAKAvkellnkEGVRLDGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSPKP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735523678 499 GFITADMVKDGAVVIDVGINHVDGkivgdvdfEAVKDKVSAITPVPGGVGPMTITELLYNTFQ 561
Cdd:cd05212 83 EKVPTEWIKPGATVINCSPTKLSG--------DDVKESASLYVPMTGGVGKLTVAMRMQNMVR 137
|
|
| PAP2_like_2 |
cd03392 |
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
51-232 |
1.82e-24 |
|
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239486 Cd Length: 182 Bit Score: 100.38 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 51 LDTPVENYIEHSMPEAVDNAFRYITDVGKAEYILIICGVIVLVRLFINidklsesTKIAfnkiciySGFILATVAISGIV 130
Cdd:cd03392 12 FDQSVLSLLRSLRTPLLTAFMTAITFLGSPAVLLIIVLLLALLLLLKR-------RRRA-------ALFLLLALLGGGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 131 GQVLKIIIGRARPkffleygsHYFQHFHAPGYdfaSMPSGHSITVGAMFIALFYIF------PKFRYLWYVLIVVFAG-- 202
Cdd:cd03392 78 NTLLKLLVQRPRP--------PLHLLVPEGGY---SFPSGHAMGATVLYGFLAYLLarrlprRRVRILLLILAAILILlv 146
|
170 180 190
....*....|....*....|....*....|....*
gi 1735523678 203 --SRIIVGSHYPSDVIFGVAFG---CYCTAYIYYW 232
Cdd:cd03392 147 glSRLYLGVHYPSDVLAGWLLGlawLALLILLYRR 181
|
|
| PAP2_like |
cd01610 |
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ... |
115-230 |
1.39e-23 |
|
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.
Pssm-ID: 238813 [Multi-domain] Cd Length: 122 Bit Score: 95.99 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 115 IYSGFILATVAISGIVGQVLKIIIGRARPKFFLEYGSHYFQHFHAPGydFASMPSGHSITVGAMFIALFYIFPK------ 188
Cdd:cd01610 3 LLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLLLTEG--GYSFPSGHAAFAFALALFLALLLPRrllrll 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1735523678 189 FRYLWYVLIVVFAGSRIIVGSHYPSDVIFGVAFGCYCTAYIY 230
Cdd:cd01610 81 LGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
|
|
| PgpB |
COG0671 |
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ... |
36-236 |
3.64e-20 |
|
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 440435 [Multi-domain] Cd Length: 189 Bit Score: 88.56 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 36 TFVPILILVVFAFYNLDTPVENYIEHSMPEAVDNAFRYITDVGKAEYILIICGVIVLVRLFINIDKLSestkiafnkicI 115
Cdd:COG0671 5 LLLALLLLLLLLADLLALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLL-----------L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 116 YSGFILATVAISGIVGQVLKIIIGRARPkffleYGSHYFQHFHAPGYDFaSMPSGHSITVGAMFIALFYIFPK--FRYLW 193
Cdd:COG0671 74 LLLLAALLLLLLLLLLLLLKYLFGRPRP-----FVVPDLELLLGTAGGY-SFPSGHAAAAFALALVLALLLPRrwLAALL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1735523678 194 YVLIVVFAGSRIIVGSHYPSDVIFGVAFGcYCTAYIYYWMLNR 236
Cdd:COG0671 148 LALALLVGLSRVYLGVHYPSDVLAGALLG-LAIALLLLALLRR 189
|
|
| acidPPc |
smart00014 |
Acid phosphatase homologues; |
125-222 |
7.03e-14 |
|
Acid phosphatase homologues;
Pssm-ID: 214471 [Multi-domain] Cd Length: 116 Bit Score: 68.14 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 125 AISGIVGQVLKIIIGRARPKFFLEYGSHYFQHFHAPGYDFASMPSGHS-ITVGAMFIALFYIFPKFR-----YLWYVLIV 198
Cdd:smart00014 5 VVSQLFNGVIKNYFGRPRPFFLSIGDACCTPNFLLTLEAGYSFPSGHTaFAFAFALFLLLYLPARAGrklliFLLLLLAL 84
|
90 100
....*....|....*....|....
gi 1735523678 199 VFAGSRIIVGSHYPSDVIFGVAFG 222
Cdd:smart00014 85 VVGFSRVYLGAHWPSDVLAGSLLG 108
|
|
| PAP2_like_4 |
cd03395 |
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
65-231 |
1.77e-13 |
|
PAP2_like_4 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239489 Cd Length: 177 Bit Score: 68.83 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 65 EAVDNAFRYITDVGKAEYILIICGVIVLVRlfinidklsestkiAFNKICIYSGFILATVAIS-GIVGQVLKIIIGRARP 143
Cdd:cd03395 20 PLLDDLMPFLTGKKLSVPIFLLLALFILFR--------------KGPIGLLILLLVLLAVGFAdQLASGFLKPLVARLRP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 144 KFFLEyGSHYFQHFHAPG-YDFASMPSGHSITVgAMFIALFYIFPKFRYLWYVLIVVFAGSRIIVGSHYPSDVIFGVAFG 222
Cdd:cd03395 86 CNALD-GVRLVVLGDQGGsYSFASSHAANSFAL-ALFIWLFFRRGLFSPVLLLWALLVGYSRVYVGVHYPGDVIAGALIG 163
|
....*....
gi 1735523678 223 CYCTAYIYY 231
Cdd:cd03395 164 IISGLLFYL 172
|
|
| PAP2_like_6 |
cd03396 |
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
118-234 |
2.22e-11 |
|
PAP2_like_6 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which mainly contains bacterial proteins, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239490 Cd Length: 197 Bit Score: 63.09 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 118 GFILATVAISGIVGQVLKIIIGRARPKFFLEYG------SHYFQHFHA--PGYDFasmPSGHSITvGAMFIALFYIF--- 186
Cdd:cd03396 70 LLLILVIGLGLLVVAILKSHWGRPRPWDLTEFGgdapytPLFSGPSNGcgKGCSF---PSGHASA-GFALLALYFLFrrr 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1735523678 187 -PKFRYLWYV----LIVVFAGSRIIVGSHYPSDVIFGVAFgCYCTAYIYYWML 234
Cdd:cd03396 146 rPRLARLVLAaglaLGALMGLARMARGAHFLSDVLWSLLL-VWLIALLLYRLI 197
|
|
| PAP2_like_5 |
cd03394 |
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
121-230 |
4.04e-11 |
|
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239488 [Multi-domain] Cd Length: 106 Bit Score: 60.04 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 121 LATVAISGIVGQVLKIIIGRARPkffleYGSHYfqhfhapgyDFASMPSGHSITV--GAMFIALFYIFPKFRYLWYVLIV 198
Cdd:cd03394 9 AEAAALTAAVTEGLKFAVGRARP-----DGSNN---------GYRSFPSGHTASAfaAATFLQYRYGWRWYGIPAYALAS 74
|
90 100 110
....*....|....*....|....*....|..
gi 1735523678 199 VFAGSRIIVGSHYPSDVIFGVAFGCYCTAYIY 230
Cdd:cd03394 75 LVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
400-561 |
7.54e-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: 61.67 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 400 PEKDVDGFHPANIGRL--------QLRDKKCLESCTPKGILTMLK---------EYGIQTEGAHAVVVGASNIVGKPVSQ 462
Cdd:cd01079 1 PHKDVEGLSHKYIFNLyhnirfldPENRKKSILPCTPLAIVKILEflgiynkilPYGNRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 463 LLLNAKATV-----TTCHRFTK----DLKSH------------TTKADILVVAVGKPGF-ITADMVKDGAVVIDV-GINH 519
Cdd:cd01079 81 LLANDGARVysvdiNGIQVFTRgesiRHEKHhvtdeeamtldcLSQSDVVITGVPSPNYkVPTELLKDGAICINFaSIKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1735523678 520 VDgkivgdvdfEAVKDKVSAITPVpggVGPMTITELLYNTFQ 561
Cdd:cd01079 161 FE---------PSVKEKASIYVPS---IGKVTIAMLLRNLLR 190
|
|
| PAP2_containing_1_like |
cd03390 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. ... |
118-232 |
1.13e-10 |
|
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_1. Most likely membrane-associated phosphatidic acid phosphatases. Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity, they may have a more generic housekeeping role in lipid metabolism.
Pssm-ID: 239484 [Multi-domain] Cd Length: 193 Bit Score: 61.08 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 118 GFILAtVAISGIVGQVLKIIIGRARPKFF--------LEYGSHYFQHFHAPG-----YD-FASMPSGHS--ITVGAMFIA 181
Cdd:cd03390 50 GLLLS-VSLNGVITNVLKNYAGRPRPDFLarcfpdggTPSDTLVGIDICCTGdpgvlKEgRKSFPSGHSsfAFAGLGFLS 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735523678 182 LFY-----IFPKFRYLWYVLIVVF--------AGSRIIVGSHYPSDVIFGVAFGCYCTAYIYYW 232
Cdd:cd03390 129 LYLagklhIFDPRGSSWRLLLALLplllailvAVSRTRDYRHHFSDVIAGSLIGLIIAYLSYRQ 192
|
|
| PAP2_containing_2_like |
cd03391 |
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. ... |
121-222 |
1.63e-06 |
|
PAP2, subfamily similar to human phosphatidic_acid_phosphatase_type_2_domain_containing_2. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to eukaryota, lacks functional characterization and may act as a membrane-associated phosphatidic acid phosphatase.
Pssm-ID: 239485 [Multi-domain] Cd Length: 159 Bit Score: 48.08 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 121 LATVAIsgivgqvLKIIIGRARP-----KFFLEYG-SHYfqhfhapgydfaSMPSGHSiTVGAMFIALFYIFPKFRYLWY 194
Cdd:cd03391 60 IITVAI-------LKALVRRRRPaynspDMLDYVAvDKY------------SFPSGHA-SRAAFVARFLLNHLVLAVPLR 119
|
90 100 110
....*....|....*....|....*....|..
gi 1735523678 195 VLIVVFAG----SRIIVGSHYPSDVIFGVAFG 222
Cdd:cd03391 120 VLLVLWATvvgiSRVLLGRHHVLDVLAGAFLG 151
|
|
| PAP2_BcrC_like |
cd03385 |
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as ... |
124-232 |
1.86e-06 |
|
PAP2_like proteins, BcrC_like subfamily. Several members of this family have been annotated as bacitracin transport permeases, as it was suspected that they form the permease component of an ABC transporter system. It was shown, however, that BcrC from Bacillus subtilis posesses undecaprenyl pyrophosphate (UPP) phospatase activity, and it is hypothesized that it competes with bacitracin for UPP, increasing the cell's resistance to bacitracin.
Pssm-ID: 239480 Cd Length: 144 Bit Score: 47.64 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 124 VAISGIVGQVLKIIIGRA----RPkfFLEYGSHYFQHfHAPGydfASMPSGHSITVGAMFIA-LFYIFPKFRYLWYVLIV 198
Cdd:cd03385 38 ATIAVAVALLINYIIGLLyfhpRP--FVVGLGHNLLP-HAAD---SSFPSDHTTLFFSIAFSlLLRRRKWAGWILLILAL 111
|
90 100 110
....*....|....*....|....*....|....
gi 1735523678 199 VFAGSRIIVGSHYPSDVIFGVAFGCYcTAYIYYW 232
Cdd:cd03385 112 LVAWSRIYLGVHYPLDMLGAALVAVL-SALLVFQ 144
|
|
| PAP2_like_3 |
cd03393 |
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ... |
112-222 |
3.27e-06 |
|
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria and archaea, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
Pssm-ID: 239487 [Multi-domain] Cd Length: 125 Bit Score: 46.60 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 112 KICIYSGFILAtvaISGIVGQVLKIIIGRARPkfFLEYGSHYFQHFHAPGYDFasmPSGHsITVGAMFIALFYIFPKFRY 191
Cdd:cd03393 13 RLGRYLGLALC---ASGYLNAALKEVFKIPRP--FTYDGIQAIYEESAGGYGF---PSGH-AQTSATFWGSLMLHVRKKW 83
|
90 100 110
....*....|....*....|....*....|....
gi 1735523678 192 LWY---VLIVVFAGSRIIVGSHYPSDVIFGVAFG 222
Cdd:cd03393 84 FTLigvVLVVLISFSRLYLGVHWPSDVIGGVLIG 117
|
|
| PAP2_like_1 |
cd03380 |
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ... |
164-222 |
3.83e-06 |
|
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium chloroperoxidases and vanadium bromoperoxidases.
Pssm-ID: 239475 Cd Length: 209 Bit Score: 47.81 E-value: 3.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 164 FASMPSGHSITVGAMFIALFYIFP-KFRYLWyVLIVVFAGSRIIVGSHYPSDVIFGVAFG 222
Cdd:cd03380 142 HPSYPSGHATFGGAAALVLAELFPeRAAELL-ARAAEAGNSRVVAGVHWPSDVEAGRILG 200
|
|
| PAP2_SPPase1 |
cd03388 |
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ... |
108-222 |
8.42e-05 |
|
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family.
Pssm-ID: 239482 Cd Length: 151 Bit Score: 42.99 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 108 IAFNKICIYSGFILATVAISGI------VGQVLKIIIGRARP-----------KFFLEYGshyfqhfhapgydfasMPSG 170
Cdd:cd03388 20 ILFLPFLFWNGDPYVGRDLVVVlalgmyIGQFIKDLFCLPRPssppvvrltmsSAALEYG----------------FPST 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 171 HSI-TVGAMFIALFYIFPKFRY--LWYVLIVVF-----AGSRIIVGSHYPSDVIFGVAFG 222
Cdd:cd03388 84 HAMnATAISFYLLIYLYDRYQYpfVLGLILALFystlvCLSRIYMGMHSVLDVIAGSLIG 143
|
|
| PAP2_dolichyldiphosphatase |
cd03382 |
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ... |
113-231 |
1.98e-04 |
|
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a membrane-associated protein located in the endoplasmic reticulum and hydrolyzes dolichyl pyrophosphate, as well as dolichylmonophosphate at a low rate. The enzyme is necessary for maintaining proper levels of dolichol-linked oligosaccharides and protein N-glycosylation, and might play a role in re-utilization of the glycosyl carrier lipid for additional rounds of lipid intermediate biosynthesis after its release during protein N-glycosylation reactions.
Pssm-ID: 239477 Cd Length: 159 Bit Score: 42.26 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 113 ICIYSGFILAT---VAISGIVGQ--------VLKIIIGRARPkffleygsHYFQHFHAPGYdfaSMPSGHSITVG--AMF 179
Cdd:cd03382 29 LVGYATLILFRrelEAIYLFIGLlanealnyVLKRIIKEPRP--------CSGAYFVRSGY---GMPSSHSQFMGffAVY 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1735523678 180 IALFYIF---PKFRYLWYVLIVVF--------AGSRIIVGSHYPSDVIFGVAFGCyCTAYIYY 231
Cdd:cd03382 98 LLLFIYLrlgRLNSLVSRFLLSLGllllallvSYSRVYLGYHTVSQVVVGAIVGI-LLGILWF 159
|
|
| COG5322 |
COG5322 |
Predicted amino acid dehydrogenase [General function prediction only]; |
430-532 |
2.74e-04 |
|
Predicted amino acid dehydrogenase [General function prediction only];
Pssm-ID: 444114 [Multi-domain] Cd Length: 362 Bit Score: 43.29 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 430 GILTMLKEYGIQTEGAHAVVVGASNIVGKPVSQLLL---------------------------NAKATVTTchrftkDLK 482
Cdd:COG5322 137 ATKQAAERMGIDLKKATVAVVGATGSIGSVCARLLArevkrltlvarnlerleelaeeilrnpGGKVTITT------DID 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1735523678 483 SHTTKADILVVAVGKPGF-ITADMVKDGAVVIDVG---------------INHVDGKIV---GDVDFEA 532
Cdd:COG5322 211 EALREADIVVTVTSAVGAiIDPEDLKPGAVVCDVArprdvsrrvaekrpdVLVIEGGVVevpGDVDFGF 279
|
|
| PAP2_3 |
pfam14378 |
PAP2 superfamily; |
164-223 |
3.18e-04 |
|
PAP2 superfamily;
Pssm-ID: 433919 Cd Length: 190 Bit Score: 41.94 E-value: 3.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1735523678 164 FASMPSGHsiTVGAMFIALFYIF----PKFRYLWYVLIVVFAGSRIIVGSHYPSDVIFGVAFGC 223
Cdd:pfam14378 124 LAAMPSLH--VAWALLCALALWRlrrtRILRWLAVAYNVLMIVSTVATGNHYLLDVVAGVALAL 185
|
|
| PRK10699 |
PRK10699 |
phosphatidylglycerophosphatase B; Provisional |
155-219 |
8.52e-04 |
|
phosphatidylglycerophosphatase B; Provisional
Pssm-ID: 182658 Cd Length: 244 Bit Score: 41.17 E-value: 8.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1735523678 155 QHFHA-PGYDFasmPSGHSitvgaMFIALFYIF------PKFRYLWYVLIVVFA----GSRIIVGSHYPSDVIFGV 219
Cdd:PRK10699 149 SHWQKeTGFAF---PSGHT-----MFAASWALLavgllwPRRRYKTVALLMLWAtgvmGSRLLLGMHWPRDLVVAT 216
|
|
| PAP2_Aur1_like |
cd03386 |
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ... |
141-232 |
8.70e-04 |
|
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin.
Pssm-ID: 239481 Cd Length: 186 Bit Score: 40.76 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 141 ARPKFFLEYGSHYFQH--FHAPGYD---------FASMPSGHSITVGAMFIALFYIFPK-FRYLWYVLIVVFAGSRIIVG 208
Cdd:cd03386 82 APPRYEPPYGLILLVLlmYGSAGYTsgfggfdnpFNAFPSLHVAWAVLAALFLWRHRRRlLRWLAVLWPLLIWLSTLYLG 161
|
90 100
....*....|....*....|....
gi 1735523678 209 SHYPSDVIFGVAFGCYCTAYIYYW 232
Cdd:cd03386 162 NHYFIDLVGGIALALLSFYLARRV 185
|
|
| PAP2_glucose_6_phosphatase |
cd03381 |
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ... |
132-256 |
1.43e-03 |
|
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.
Pssm-ID: 239476 Cd Length: 235 Bit Score: 40.44 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 132 QVLKIIIGRARPKFFLEYGSHYFQHFHAPGYDFAS-------MPSGHSITVGA----MFIALFYIF---PKFRYLWYVLI 197
Cdd:cd03381 32 LVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLtcetgpgSPSGHAMGTTAvllvMVTALLSHLagrKRSRFLRVMLW 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1735523678 198 VVFAG-------SRIIVGSHYPSDVIFGV----AFGCYCTAYIYYWmlNRELPPKNKTLKIFNYFLIYFY 256
Cdd:cd03381 112 LVFWGvqlavclSRIYLAAHFPHQVIAGVisgiAVAETFSHIRYIY--SASLKRYVLITFFLFGFALGFY 179
|
|
| PAP2_acid_phosphatase |
cd03397 |
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ... |
166-218 |
2.22e-03 |
|
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined.
Pssm-ID: 239491 Cd Length: 232 Bit Score: 40.01 E-value: 2.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735523678 166 SMPSGHSITVGAMFIALFYIFPKfRYlwyVLIVV----FAGSRIIVGSHYPSDVIFG 218
Cdd:cd03397 151 SYPSGHTAAGYAWALILAELVPE-RA---DEILArgseYGQSRIVCGVHWPSDVMGG 203
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
469-517 |
7.44e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 37.10 E-value: 7.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1735523678 469 ATVTTCHRFTKDLKSHTTKADILVVAVGKPG-----FITADMV---KDGAVVIDVGI 517
Cdd:smart01002 65 ARFTTLYSQAELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDVAA 121
|
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| |
