|
Name |
Accession |
Description |
Interval |
E-value |
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
1-294 |
9.06e-129 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 367.80 E-value: 9.06e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIA--KTREHHPNfhavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQG 78
Cdd:COG0190 1 MMAQILDGKAVAAEIREELKERVAalKAKGITPG----LAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 79 DLKREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQA 158
Cdd:COG0190 77 ELLALIDELNADPSVHGILVQLPLP-KH-IDEEAVLEAIDPEKDVDGFHPVNLGRLVLGE--PGFVPCTPAGIMELLERY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 159 TGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDC 238
Cdd:COG0190 153 GID---LAGKHAVVVGRSNIVGKPLALLLLRRNATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17568735 239 GINVGDDpnsRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRRR 294
Cdd:COG0190 230 GINRVED---GKLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQA 282
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-293 |
4.24e-97 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 287.68 E-value: 4.24e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIAKTREHHPNFHavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDL 80
Cdd:PRK14190 1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGIVPG--LAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 81 KREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQQATG 160
Cdd:PRK14190 79 LALIDRLNADPRINGILVQLPLP-KH-IDEKAVIERISPEKDVDGFHPINVGRMMLG--QDTFLPCTPHGILELLKEYNI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 161 DanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGI 240
Cdd:PRK14190 155 D---ISGKHVVVVGRSNIVGKPVGQLLLNENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17568735 241 NVGDDpnsRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRR 293
Cdd:PRK14190 232 NRLEN---GKLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRA 281
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-292 |
6.65e-96 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 284.93 E-value: 6.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 3 AEIVSGLEYSKKVLHDVGQKIAKTREHHpNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKR 82
Cdd:PRK14188 2 ATIIDGKAFAADVRATVAAEVARLKAAH-GVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 83 EIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQQATGDa 162
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLP-KH-LDSEAVIQAIDPEKDVDGLHVVNAGRLATG--ETALVPCTPLGCMMLLRRVHGD- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 163 nfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINV 242
Cdd:PRK14188 156 --LSGLNAVVIGRSNLVGKPMAQLLLAANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17568735 243 GDDPNSR----KIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PRK14188 234 IPAPEKGegktRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACR 287
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-292 |
1.83e-91 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 273.10 E-value: 1.83e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIA--KTREHHPNfhavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQG 78
Cdd:PRK14189 1 MTAQLIDGNALSKQLRAEAAQRAAalTARGHQPG----LAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 79 DLKREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGElqrTIF-PCTPFGCLYLVQQ 157
Cdd:PRK14189 77 ELLARIDELNRDPKIHGILVQLPLP-KH-IDSHKVIEAIAPEKDVDGFHVANAGALMTGQ---PLFrPCTPYGVMKMLES 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 158 ATGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVID 237
Cdd:PRK14189 152 IGIP---LRGAHAVVIGRSNIVGKPMAMLLLQAGATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVID 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17568735 238 CGINVGDDPnsrKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PRK14189 229 VGMNRDDAG---KLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
119-291 |
1.90e-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: 266.34 E-value: 1.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 119 PLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQATGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICH 198
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGR--PGFIPCTPAGILELLKRYGID---LAGKKVVVVGRSNIVGKPLAALLLNRNATVTVCH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 199 SKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDPNSRKIYGDVDTEAAKEVAGFLTPVPGGVGPMT 278
Cdd:cd01080 76 SKTKNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDKSGGKLVGDVDFESAKEKASAITPVPGGVGPMT 155
|
170
....*....|...
gi 17568735 279 VAMLIRNTFEQAK 291
Cdd:cd01080 156 VAMLMKNTVEAAK 168
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-293 |
1.69e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 265.63 E-value: 1.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIAKTRE---HHPNfhavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQ 77
Cdd:PRK10792 1 MTAKIIDGKTIAQQVRSEVAQKVQARVAaglRAPG----LAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 78 GDLKREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLArgelQR--TIFPCTPFGCLYLV 155
Cdd:PRK10792 77 AELLALIDELNADPTIDGILVQLPLP-AH-IDNVKVLERIHPDKDVDGFHPYNVGRLA----QRipLLRPCTPRGIMTLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 156 QQATGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFV 235
Cdd:PRK10792 151 ERYGID---TYGLNAVVVGASNIVGRPMSLELLLAGCTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17568735 236 IDCGINVGDDpnsRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRR 293
Cdd:PRK10792 228 IDVGINRLED---GKLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACEEY 282
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-294 |
9.99e-87 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 261.30 E-value: 9.99e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIAKTrehhpNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDL 80
Cdd:PRK14173 1 MAARELSGPPAAEAVYAELRARLAKL-----PFVPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 81 KREIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQATG 160
Cdd:PRK14173 76 LELIARLNADPEVDGILVQLPL--PPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGG--EALEPCTPAGVVRLLKHYGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 161 DanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGI 240
Cdd:PRK14173 152 P---LAGKEVVVVGRSNIVGKPLAALLLREDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17568735 241 N-VGDDPNSRKIYGDVDTEAAkEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRRR 294
Cdd:PRK14173 229 NrVGGNGGRDILTGDVHPEVA-EVAGALTPVPGGVGPMTVAMLMANTVIAALRRR 282
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-296 |
2.23e-86 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 260.26 E-value: 2.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 3 AEIVSGLEYSKKVLHDVGQKIAKTREHhpNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKR 82
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQ--DVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 83 EIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQATGDa 162
Cdd:PRK14169 79 KVAELNHDPDVDAILVQLPL--PAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANE--PTVVASTPYGIMALLDAYDID- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 163 nfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINV 242
Cdd:PRK14169 154 --VAGKRVVIVGRSNIVGRPLAGLMVNHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISR 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17568735 243 GDDPnsrKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRRRLG 296
Cdd:PRK14169 232 GADG---KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRANG 282
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
127-294 |
1.69e-82 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 245.84 E-value: 1.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 127 TRINAGRLARGElqRTIFPCTPFGCLYLVQQATGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKE 206
Cdd:pfam02882 1 HPYNLGRLVLGK--PCFVPCTPRGIMELLKRYGID---LAGKNVVVVGRSNIVGKPLALLLLNANATVTVCHSKTKDLAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 207 KCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDpnsRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNT 286
Cdd:pfam02882 76 ITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGN---GKLVGDVDFENVKEKASAITPVPGGVGPMTVAMLLQNT 152
|
....*...
gi 17568735 287 FEQAKRRR 294
Cdd:pfam02882 153 VEAAKRQL 160
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-291 |
2.96e-80 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 244.31 E-value: 2.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 4 EIVSGLEYSKKVLHDVGQKIAKTREHHPNFHAVLAIVqVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKRE 83
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGLSIPKIASIL-VGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 84 IMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQATGDan 163
Cdd:PRK14172 82 IEELNKDNNVHGIMLQLPLP-KH-LDEKKITNKIDANKDIDCLTFISVGKFYKGE--KCFLPCTPNSVITLIKSLNID-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 164 fVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVG 243
Cdd:PRK14172 156 -IEGKEVVVIGRSNIVGKPVAQLLLNENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17568735 244 DDpnsrKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAK 291
Cdd:PRK14172 235 NG----KITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEALK 278
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
2-293 |
5.35e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 243.89 E-value: 5.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 2 VAEIVSGLEYSKKVLHDVGQKIAKTREHH---PNfhavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQG 78
Cdd:PRK14179 1 MTEIIDGKALAQKMQAELAEKVAKLKEEKgivPG----LVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 79 DLKREIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGELQrtIFPCTPFGCLYLVQQA 158
Cdd:PRK14179 77 ELLDLIERYNQDPTWHGILVQLPL--PKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPV--MIPCTPAGIMEMFREY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 159 TGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDC 238
Cdd:PRK14179 153 NVE---LEGKHAVVIGRSNIVGKPMAQLLLDKNATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17568735 239 GINVGDDPnsrKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRR 293
Cdd:PRK14179 230 GMNRDENG---KLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRS 281
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-286 |
4.36e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 242.04 E-value: 4.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 5 IVSGLEYSKKVLHDVGQKIAKTREHHpNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREI 84
Cdd:PRK14187 4 IIDGKKIANDITEILATCIDDLKRQH-NLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 85 MALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGELQRTIFPCTPFGCLYLVQQATgdaNF 164
Cdd:PRK14187 83 NELNNDDSVHGILVQLPVP-NH-IDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNCLIPCTPKGCLYLIKTIT---RN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 165 VSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGD 244
Cdd:PRK14187 158 LSGSDAVVIGRSNIVGKPMACLLLGENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17568735 245 DPNSRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNT 286
Cdd:PRK14187 238 EGGVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNT 279
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-293 |
3.32e-78 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 239.97 E-value: 3.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 37 LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDL 116
Cdd:PRK14186 35 LAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEALIAQLNQDERVDGILLQLPLP-KH-LDEVPLLHA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 117 IDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQATGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTI 196
Cdd:PRK14186 113 IDPDKDADGLHPLNLGRLVKGE--PGLRSCTPAGVMRLLRSQQID---IAGKKAVVVGRSILVGKPLALMLLAANATVTI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 197 CHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGIN-VGDDPNSRKIYGDVDTEAAKEVAGFLTPVPGGVG 275
Cdd:PRK14186 188 AHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHrLPSSDGKTRLCGDVDFEEVEPVAAAITPVPGGVG 267
|
250
....*....|....*...
gi 17568735 276 PMTVAMLIRNTFEQAKRR 293
Cdd:PRK14186 268 PMTVTMLLVNTVLSWQKR 285
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-298 |
1.56e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 238.21 E-value: 1.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIAKTREHhpNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDL 80
Cdd:PRK14194 2 MSAKLIDGKAAAARVLAQVREDVRTLKAA--GIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 81 KREIMALNHDNEIDGIIIQLPLDCkhEIDADSVIDLIDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQQATG 160
Cdd:PRK14194 80 LALIAELNADPSVNGILLQLPLPA--HIDEARVLQAINPLKDVDGFHSENVGGLSQG--RDVLTPCTPSGCLRLLEDTCG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 161 DanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGI 240
Cdd:PRK14194 156 D---LTGKHAVVIGRSNIVGKPMAALLLQAHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17568735 241 NVGDDPNSRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRRRLGQK 298
Cdd:PRK14194 233 NRIDDDGRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQAHAQR 290
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
2-292 |
3.62e-77 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 237.48 E-value: 3.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 2 VAEIVSGLEYSKKVLHDVGQKIAKTREHHPNFHAvLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLK 81
Cdd:PLN02516 8 VAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPG-LAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 82 REIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGELQRTIFPCTPFGCLYLVQQATGD 161
Cdd:PLN02516 87 SKVHELNANPDVHGILVQLPLP-KH-INEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLSRSGIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 162 anfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGIN 241
Cdd:PLN02516 165 ---IKGKKAVVVGRSNIVGLPVSLLLLKADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTN 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17568735 242 VGDDPNSR---KIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PLN02516 242 AVSDPSKKsgyRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKR 295
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-293 |
5.34e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 236.59 E-value: 5.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 5 IVSGLEYSKKVLHDVGQKIAKTRehhPNFHAV--LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKR 82
Cdd:PRK14191 3 LLDGKALSYKIEKDLKNKIQILT---AQTGKRpkLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 83 EIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQQATGDa 162
Cdd:PRK14191 80 LIKDLNTDQNIDGILVQLPLP-RH-IDTKMVLEAIDPNKDVDGFHPLNIGKLCSQ--LDGFVPATPMGVMRLLKHYHIE- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 163 nfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINV 242
Cdd:PRK14191 155 --IKGKDVVIIGASNIVGKPLAMLMLNAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINR 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17568735 243 GDDpnsRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRR 293
Cdd:PRK14191 233 LND---GRLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKR 280
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-291 |
5.34e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 231.38 E-value: 5.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 2 VAEIVSGLEYSKKVLHDVGQKIAKTREHhPNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLK 81
Cdd:PRK14171 1 MNNIIDGKALANEILADLKLEIQELKSQ-TNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 82 REIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGeLQRTIFPCTPFGCLYLVQQATGD 161
Cdd:PRK14171 80 SKINELNLDNEISGIIVQLPL--PSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSG-ISQGFIPCTALGCLAVIKKYEPN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 162 anfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGIN 241
Cdd:PRK14171 157 ---LTGKNVVIIGRSNIVGKPLSALLLKENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGIN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17568735 242 vgdDPNSRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAK 291
Cdd:PRK14171 234 ---RISGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKAFK 280
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-292 |
1.13e-74 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 230.86 E-value: 1.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 37 LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDL 116
Cdd:PRK14174 34 LTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIEDLNNDPDVHGILVQQPL--PKQIDEFAVTLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 117 IDPLKDVDGLTRINAGRLARGELQRTIFPCTPFGCLYLVQQATGDAnfvSGKEVVVLGRSKIVGSPAAALFLWH----HG 192
Cdd:PRK14174 112 IDPAKDVDGFHPENLGRLVMGHLDKCFVSCTPYGILELLGRYNIET---KGKHCVVVGRSNIVGKPMANLMLQKlkesNC 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 193 TVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDPNSRKIY---GDVDTEAAKEVAGFLTP 269
Cdd:PRK14174 189 TVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIEDPSTKSGYrlvGDVDYEGVSAKASAITP 268
|
250 260
....*....|....*....|...
gi 17568735 270 VPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PRK14174 269 VPGGVGPMTIAMLLKNTLQSFER 291
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-294 |
4.47e-74 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 228.89 E-value: 4.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 37 LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDL 116
Cdd:PRK14184 34 LAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAELNARPDIDGILLQLPL--PKGLDSQRCLEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 117 IDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQQATGDanfVSGKEVVVLGRSKIVGSPAAALFL----WHHG 192
Cdd:PRK14184 112 IDPAKDVDGFHPENMGRLALG--LPGFRPCTPAGVMTLLERYGLS---PAGKKAVVVGRSNIVGKPLALMLGapgkFANA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 193 TVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDpnsrKIYGDVDTEAAKEVAGFLTPVPG 272
Cdd:PRK14184 187 TVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDD----GLVGDCDFEGLSDVASAITPVPG 262
|
250 260
....*....|....*....|..
gi 17568735 273 GVGPMTVAMLIRNTFEQAKRRR 294
Cdd:PRK14184 263 GVGPMTIAQLLVNTVQSWKERV 284
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-291 |
2.96e-72 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 224.75 E-value: 2.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIAKTREHHPNFHAVLAIVqVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDL 80
Cdd:PRK14168 1 MSAKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTIL-VGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 81 KREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGELQRTIFPCTPFGCLYLVQQATG 160
Cdd:PRK14168 80 LALIDKYNNDDSIHGILVQLPLP-KH-INEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVKFLPCTPAGIQEMLVRSGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 161 DAnfvSGKEVVVLGRSKIVGSPAAALFLWH----HGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVI 236
Cdd:PRK14168 158 ET---SGAEVVVVGRSNIVGKPIANMMTQKgpgaNATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17568735 237 DCGIN-VGDDPNSRK--IYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAK 291
Cdd:PRK14168 235 DVGVNrVGTNESTGKaiLSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
3-292 |
1.32e-71 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 225.27 E-value: 1.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 3 AEIVSGLEYSKKVLHDVGQKIAKTREH---HPNfhavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGD 79
Cdd:PLN02616 73 AKVIDGKAVAKKIRDEITIEVSRMKESigvVPG----LAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 80 LKREIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGELQRTIFPCTPFGCLYLVQQAT 159
Cdd:PLN02616 149 VLKFISGFNNDPSVHGILVQLPL--PSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLFVPCTPKGCIELLHRYN 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 160 GDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCG 239
Cdd:PLN02616 227 VE---IKGKRAVVIGRSNIVGMPAALLLQREDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVG 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17568735 240 INVGDDPNSRKIY---GDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PLN02616 304 INPVEDASSPRGYrlvGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-293 |
7.17e-71 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 220.66 E-value: 7.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIAKTREH--HPNfhavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQG 78
Cdd:PRK14193 1 MTAIILDGKATADEIKADLAERVAALKEKgiTPG----LGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 79 DLKREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQA 158
Cdd:PRK14193 77 ELNAVIDELNADPACTGYIVQLPLP-KH-LDENAVLERIDPAKDADGLHPTNLGRLVLNE--PAPLPCTPRGIVHLLRRY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 159 TGDanfVSGKEVVVLGRSKIVGSPAAALFLWHH--GTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVI 236
Cdd:PRK14193 153 DVE---LAGAHVVVIGRGVTVGRPIGLLLTRRSenATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17568735 237 DCGIN-VGDDpnsrKIYGDVDTEAAkEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRR 293
Cdd:PRK14193 230 DVGVSrAGDG----KLVGDVHPDVW-EVAGAVSPNPGGVGPMTRAFLLTNVVERAERR 282
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-291 |
2.15e-69 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 217.15 E-value: 2.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 5 IVSGLEYSKKVLHDVGQKIAKTREHHPNFhAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREI 84
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETIEERKTKNKRI-PKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 85 MALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQQATGDanf 164
Cdd:PRK14177 84 DKLNLDPNVDGILLQHPV--PSQIDERAAFDRIALEKDVDGVTTLSFGKLSMG--VETYLPCTPYGMVLLLKEYGID--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 165 VSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGD 244
Cdd:PRK14177 157 VTGKNAVVVGRSPILGKPMAMLLTEMNATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYNPGN 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17568735 245 dpnsrkiYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAK 291
Cdd:PRK14177 237 -------VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFK 276
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-294 |
1.52e-67 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 212.47 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIAKTREHhpNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDL 80
Cdd:PRK14175 1 MVAKILDGKQIAKDYRQGLQDQVEALKEK--GFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 81 KREIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQATG 160
Cdd:PRK14175 79 LNELNRLNNDDSVSGILVQVPL--PKQVSEQKILEAINPEKDVDGFHPINIGKLYIDE--QTFVPCTPLGIMEILKHADI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 161 DanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDcgi 240
Cdd:PRK14175 155 D---LEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIID--- 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17568735 241 nVGDDPNSR-KIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRRR 294
Cdd:PRK14175 229 -VGNTPDENgKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMRR 282
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
37-292 |
8.17e-66 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 209.82 E-value: 8.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 37 LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDL 116
Cdd:PLN02897 89 LAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSALRKFNEDTSIHGILVQLPLP-QH-LDESKILNM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 117 IDPLKDVDGLTRINAGRLARGELQRTIFPCTPFGCLYLVQQATGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTI 196
Cdd:PLN02897 167 VRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRSGVE---IAGKNAVVIGRSNIVGLPMSLLLQRHDATVST 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 197 CHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDPNSR---KIYGDVDTEAAKEVAGFLTPVPGG 273
Cdd:PLN02897 244 VHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSSCEfgyRLVGDVCYEEALGVASAITPVPGG 323
|
250
....*....|....*....
gi 17568735 274 VGPMTVAMLIRNTFEQAKR 292
Cdd:PLN02897 324 VGPMTITMLLCNTLDAAKR 342
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-292 |
8.78e-66 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 207.62 E-value: 8.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 2 VAEIVSGLEYSKKVLHDVGQKIAKTREHHPNfhAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLK 81
Cdd:PRK14170 1 MGEIIDGKKLAKEIQEKVTREVAELVKEGKK--PGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 82 REIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQqATGD 161
Cdd:PRK14170 79 SVVEELNEDKTIHGILVQLPLP-EH-ISEEKVIDTISYDKDVDGFHPVNVGNLFIG--KDSFVPCTPAGIIELIK-STGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 162 AnfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGIn 241
Cdd:PRK14170 154 Q--IEGKRAVVIGRSNIVGKPVAQLLLNENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGM- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17568735 242 vgDDPNSRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PRK14170 231 --DRDENNKLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
13-293 |
6.60e-65 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 205.45 E-value: 6.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 13 KKVLHDVGQKIAKTREHHPNFHAV---LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREIMALNH 89
Cdd:PRK14183 7 KALSDKIKENVKKEVDELKLVKNIvpgLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETIAMMNN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 90 DNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQQATGDanfVSGKE 169
Cdd:PRK14183 87 NPNIDGILVQLPLP-KH-IDTTKILEAIDPKKDVDGFHPYNVGRLVTG--LDGFVPCTPLGVMELLEEYEID---VKGKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 170 VVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDPnsr 249
Cdd:PRK14183 160 VCVVGASNIVGKPMAALLLNANATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTEDG--- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17568735 250 KIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRR 293
Cdd:PRK14183 237 RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKNR 280
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
37-292 |
7.55e-65 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 205.26 E-value: 7.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 37 LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDL 116
Cdd:PRK14182 33 LTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARLNADPAVHGILVQLPLP-KH-VDERAVLDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 117 IDPLKDVDGLTRINAGRLARGeLQRTIFPCTPFGCLYLVQQATGDANfvsGKEVVVLGRSKIVGSPAAALFLWHHGTVTI 196
Cdd:PRK14182 111 ISPAKDADGFHPFNVGALSIG-IAGVPRPCTPAGVMRMLDEARVDPK---GKRALVVGRSNIVGKPMAMMLLERHATVTI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 197 CHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDPnsrKIYGDVDTEAAKEVAGFLTPVPGGVGP 276
Cdd:PRK14182 187 AHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLADG---KLVGDVEFAAAAARASAITPVPGGVGP 263
|
250
....*....|....*.
gi 17568735 277 MTVAMLIRNTFEQAKR 292
Cdd:PRK14182 264 MTRAMLLVNTVELAKR 279
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-293 |
1.19e-64 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 204.87 E-value: 1.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 5 IVSGLEYSKKVLHDVGQKIAKTREHhpNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREI 84
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSK--GIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 85 MALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGeLQRTIFPCTPFGCLYLVQQATGDanf 164
Cdd:PRK14166 81 NTLNHDDSVHGILVQLPL--PDHICKDLILESIISSKDVDGFHPINVGYLNLG-LESGFLPCTPLGVMKLLKAYEID--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 165 VSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGD 244
Cdd:PRK14166 155 LEGKDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17568735 245 dpnSRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKRR 293
Cdd:PRK14166 235 ---SGKIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNR 280
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-292 |
1.90e-64 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 204.27 E-value: 1.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 5 IVSGLEYSKKVLHDVGQKIAKTrEHHPNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREI 84
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERL-KSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 85 MALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQATGDanf 164
Cdd:PRK14176 89 DSLNKRKDVHGILLQLPLP-KH-LDPQEAMEAIDPAKDADGFHPYNMGKLMIGD--EGLVPCTPHGVIRALEEYGVD--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 165 VSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGD 244
Cdd:PRK14176 162 IEGKNAVIVGHSNVVGKPMAAMLLNRNATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17568735 245 DpnsrKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PRK14176 242 D----KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-293 |
2.65e-64 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 203.92 E-value: 2.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 37 LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLP-DTITQGDLKReIMALNHDNEIDGIIIQLPLdcKHEIDADSVID 115
Cdd:PRK14178 29 LATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPgDATTRTVLER-IRRLNEDPDINGILVQLPL--PKGVDTERVIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 116 LIDPLKDVDGLTRINAGRLARGelQRTIFPCTPFGCLYLVQQATGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVT 195
Cdd:PRK14178 106 AILPEKDVDGFHPLNLGRLVSG--LPGFAPCTPNGIMTLLHEYKIS---IAGKRAVVVGRSIDVGRPMAALLLNADATVT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 196 ICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDpnsrKIYGDVDTEAAKEVAGFLTPVPGGVG 275
Cdd:PRK14178 181 ICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNG----KLCGDVDFDAVKEIAGAITPVPGGVG 256
|
250
....*....|....*...
gi 17568735 276 PMTVAMLIRNTFEQAKRR 293
Cdd:PRK14178 257 PMTIATLMENTFDAAKMR 274
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
37-292 |
1.23e-62 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 200.06 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 37 LAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREIMALNHDNEIDGIIIQLPLDcKHeIDADSVIDL 116
Cdd:PRK14185 34 LAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKVRELNQDDDVDGFIVQLPLP-KH-ISEQKVIEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 117 IDPLKDVDGLTRINAGRLARGelqrtiFPC----TPFGCLYLVQQATGDAnfvSGKEVVVLGRSKIVGSPAAALFLWHH- 191
Cdd:PRK14185 112 IDYRKDVDGFHPINVGRMSIG------LPCfvsaTPNGILELLKRYHIET---SGKKCVVLGRSNIVGKPMAQLMMQKAy 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 192 ---GTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGDDPNSR---KIYGDVDTEAAKEVAG 265
Cdd:PRK14185 183 pgdCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDATRKsgfKLTGDVKFDEVAPKCS 262
|
250 260
....*....|....*....|....*..
gi 17568735 266 FLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PRK14185 263 YITPVPGGVGPMTIVSLMKNTLLAGKK 289
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-292 |
7.04e-62 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 197.76 E-value: 7.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 1 MVAEIVSGLEYSKKVLHDVGQKIAKTRE---HHPnfhaVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQ 77
Cdd:PRK14192 1 MMALVLDGKALAKQIEEELSVRVEALKAktgRTP----ILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 78 GDLKREIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGElqRTIFPCTPFGCLYLVQQ 157
Cdd:PRK14192 77 EQLLAKIEELNANPDVHGILLQHPV--PAQIDERACFDAISLAKDVDGVTCLGFGRMAMGE--AAYGSATPAGIMRLLKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 158 ATGDanfVSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVID 237
Cdd:PRK14192 153 YNIE---LAGKHAVVVGRSAILGKPMAMMLLNANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVD 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17568735 238 CGINvgddPNSRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PRK14192 230 AGFH----PRDGGGVGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEK 280
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
5-292 |
9.22e-62 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 197.39 E-value: 9.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 5 IVSGLEYSKKVLHDVGQKIAKTREHhPNfhavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREI 84
Cdd:PRK14181 2 LLKGAPAAEHILATIKENISASSTA-PG----LAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 85 MALNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVDGLTRINAGRLARGELQRTIfPCTPFGCLYLVQQATGDanf 164
Cdd:PRK14181 77 HRLNNDPNIHGILVQLPLP-KH-LDAQAILQAISPDKDVDGLHPVNMGKLLLGETDGFI-PCTPAGIIELLKYYEIP--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 165 VSGKEVVVLGRSKIVGSPAAALFLWHH----GTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGI 240
Cdd:PRK14181 151 LHGRHVAIVGRSNIVGKPLAALLMQKHpdtnATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGT 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17568735 241 N--VGDDPNSRKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAKR 292
Cdd:PRK14181 231 SrvPAANPKGYILVGDVDFNNVVPKCRAITPVPGGVGPMTVAMLMRNTWESYLR 284
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-290 |
5.35e-58 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 188.06 E-value: 5.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 3 AEIVSGLEYSKKVLHDVGQKIAKTRE--HHPNfhavLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDL 80
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDagVTPG----LATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 81 KREIMALNHDNEIDGIIIQLPLdcKHEIDADSVIDLIDPLKDVDGLTRINAGRLARGELQRTifPCTPFGCLYLVQQATG 160
Cdd:PRK14167 78 YDTIDELNADEDVHGILVQMPV--PDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFK--PCTPHGIQKLLAAAGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 161 DanfVSGKEVVVLGRSKIVGSPAAALFLWH----HGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVI 236
Cdd:PRK14167 154 D---TEGADVVVVGRSDIVGKPMANLLIQKadggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17568735 237 DCGINVGDDPNSR--KIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQA 290
Cdd:PRK14167 231 DVGINRVDADTEKgyELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAA 286
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
5-291 |
3.76e-54 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 177.91 E-value: 3.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 5 IVSGLEYSKKVLHDVGQKIAKTREHHPNFHAVLAIVqVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREI 84
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAII-VGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 85 MALNHDNEIDGIIIQLPLDCkhEIDADSVIDLIDPLKDVDGLTRINAGRLARGElQRTIFPCTPFGCLYLVQQATGDAnf 164
Cdd:PRK14180 82 DQLNNDSSVHAILVQLPLPA--HINKNNVIYSIKPEKDVDGFHPTNVGRLQLRD-KKCLESCTPKGIMTMLREYGIKT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 165 vSGKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIGRKHFVKADWIKPGAFVIDCGINVGD 244
Cdd:PRK14180 157 -EGAYAVVVGASNVVGKPVSQLLLNAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17568735 245 DpnsrKIYGDVDTEAAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAK 291
Cdd:PRK14180 236 G----KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQ 278
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
145-291 |
2.60e-37 |
|
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: 129.55 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 145 PCTPFGCLYLVQqATGDANFVS-----GKEVVVLGRSKIVGSPAAALFLWHHGTVTICHSKTPNLKEKCLRADILIVAIG 219
Cdd:cd05212 2 PCTPLFVSPVAK-AVKELLNKEgvrldGKKVLVVGRSGIVGAPLQCLLQRDGATVYSCDWKTIQLQSKVHDADVVVVGSP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17568735 220 RKHFVKADWIKPGAFVIDCGINvgddpnsrKIYGDVdteaAKEVAGFLTPVPGGVGPMTVAMLIRNTFEQAK 291
Cdd:cd05212 81 KPEKVPTEWIKPGATVINCSPT--------KLSGDD----VKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
7-124 |
9.05e-37 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 127.14 E-value: 9.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 7 SGLEYSKKVLHDVGQKIAKTREHhpNFHAVLAIVQVGNRSDSNVYINSKLKKAKEIGADGKLIKLPDTITQGDLKREIMA 86
Cdd:pfam00763 2 DGKAIAKKIREELKEEVAALKAG--GRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 17568735 87 LNHDNEIDGIIIQLPLDcKHeIDADSVIDLIDPLKDVD 124
Cdd:pfam00763 80 LNADPSVHGILVQLPLP-KH-IDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
119-285 |
3.64e-15 |
|
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: 72.46 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 119 PLKDVDGLTRINAGRLARGE-------LQRTIFPCTPFG---CLYLVQQATGDANF---VSGKEVVVLGRSKIVGSPAAA 185
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYHNIrfldpenRKKSILPCTPLAivkILEFLGIYNKILPYgnrLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 186 LFLWHHGTV---------------TICHSKTP-----NLKEKCL-RADILIVAIGRKHF-VKADWIKPGAFVidcgINVG 243
Cdd:cd01079 81 LLANDGARVysvdingiqvftrgeSIRHEKHHvtdeeAMTLDCLsQSDVVITGVPSPNYkVPTELLKDGAIC----INFA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17568735 244 DDPNsrkiygdvDTEAAKEVAGFLTPVpggVGPMTVAMLIRN 285
Cdd:cd01079 157 SIKN--------FEPSVKEKASIYVPS---IGKVTIAMLLRN 187
|
|
| NAD_bind_amino_acid_DH |
cd05191 |
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ... |
146-239 |
7.49e-04 |
|
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133449 [Multi-domain] Cd Length: 86 Bit Score: 37.74 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17568735 146 CTPFGCLYLVQQATGDANF-VSGKEVVVLGRsKIVGSPAAALFLWHHG-TVTICHSktpnlkekclraDILIVA--IGRK 221
Cdd:cd05191 1 ATAAGAVALLKAAGKVTNKsLKGKTVVVLGA-GEVGKGIAKLLADEGGkKVVLCDR------------DILVTAtpAGVP 67
|
90
....*....|....*....
gi 17568735 222 HF-VKADWIKPGAFVIDCG 239
Cdd:cd05191 68 VLeEATAKINEGAVVIDLA 86
|
|
| |
