|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
15-362 |
0e+00 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 507.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 15 ARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELAT 94
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 95 VRACQTMGTGMMLSSWATSSIEEVAEAGpEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNR 174
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 175 FKLPPQLRMKNFEtnDLAFSPKGNF-----GDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVK 249
Cdd:pfam01070 160 FTLPPRLTPRNLL--DLALHPRWALgvlrrGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 250 HGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGV 329
Cdd:pfam01070 238 AGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGV 317
|
330 340 350
....*....|....*....|....*....|...
gi 2203519018 330 QDVLEILKEEFRLAMALSGCQNVKVIDKTLVRK 362
Cdd:pfam01070 318 AHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
9-357 |
7.50e-169 |
|
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.
Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 472.70 E-value: 7.50e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 9 SDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRf 168
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 169 ddvrnrfklppqlrmknfetndlafspkgnfgdnsglaeyvaqaidpsLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAV 248
Cdd:cd02809 159 ------------------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 249 KHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKG 328
Cdd:cd02809 191 DAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAG 270
|
330 340
....*....|....*....|....*....
gi 2203519018 329 VQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd02809 271 VAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
2-361 |
9.20e-165 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 464.61 E-value: 9.20e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 2 LPRLVCISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATA 81
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 82 MQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDT 161
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAP-APLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 162 PYLGNRFDDVRNRFKLPPQLRMKNFEtnDLAFSPKGNFGdNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRG 241
Cdd:COG1304 160 PVLGRRERDLREGFSQPPRLTPRNLL--EAATHPRWALG-LASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 242 DDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGL 321
Cdd:COG1304 237 EDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2203519018 322 AFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:COG1304 317 AAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
8-357 |
2.58e-141 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 405.65 E-value: 2.58e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 8 ISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAH 87
Cdd:PLN02493 6 VTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 88 VDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNR 167
Cdd:PLN02493 86 PDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 168 FDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEA 247
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 248 VKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEK 327
Cdd:PLN02493 242 IQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEA 321
|
330 340 350
....*....|....*....|....*....|
gi 2203519018 328 GVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02493 322 GVRKVLQMLRDEFELTMALSGCRSLKEISR 351
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
1-361 |
5.51e-138 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 397.28 E-value: 5.51e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 1 MLPRLVCISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGAT 80
Cdd:PLN02535 1 MADEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 81 AMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAeAGPEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVD 160
Cdd:PLN02535 81 AMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVA-SSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 161 TPYLGNRFDDVRNRFKLPpqlRMKNFETndlAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILR 240
Cdd:PLN02535 160 VPRLGRREADIKNKMISP---QLKNFEG---LLSTEVVSDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 241 GDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWG 320
Cdd:PLN02535 234 REDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYG 313
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2203519018 321 LAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:PLN02535 314 LAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVR 354
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
9-353 |
1.96e-129 |
|
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.
Pssm-ID: 239238 [Multi-domain] Cd Length: 344 Bit Score: 374.63 E-value: 1.96e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 9 SDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPE-ALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNR 167
Cdd:cd02922 81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPPdQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 168 FDDVRNRFKlppqlrmknfETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEA 247
Cdd:cd02922 161 ERDERLKAE----------EAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 248 VKHGVDGILVSNHGARQLDGVPATIDALPEIVE---AVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQ 324
Cdd:cd02922 231 AEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAY 310
|
330 340
....*....|....*....|....*....
gi 2203519018 325 GEKGVQDVLEILKEEFRLAMALSGCQNVK 353
Cdd:cd02922 311 GEEGVEKAIQILKDEIETTMRLLGVTSLD 339
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
9-360 |
1.74e-128 |
|
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.
Pssm-ID: 239448 [Multi-domain] Cd Length: 383 Bit Score: 373.54 E-value: 1.74e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 9 SDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHV 88
Cdd:cd03332 22 ERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 89 DGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRF 168
Cdd:cd03332 102 DAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 169 DDVRNRFKlpPQLRMKNFE--TNDLAF------SPKGNFGDNSGLAEYVAQAI----DPSLSWDDIKWLRRLTSLPIVVK 236
Cdd:cd03332 182 RDLDLGYL--PFLRGIGIAnyFSDPVFrkklaePVGEDPEAPPPMEAAVARFVsvfsGPSLTWEDLAFLREWTDLPIVLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 237 GILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRP 316
Cdd:cd03332 260 GILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRP 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2203519018 317 IIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV 360
Cdd:cd03332 340 YAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
51-357 |
1.87e-127 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 370.59 E-value: 1.87e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 51 PRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQ 130
Cdd:PLN02979 48 PRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 131 LYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVA 210
Cdd:PLN02979 127 LYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 211 QAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFL 290
Cdd:PLN02979 204 GQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFL 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203519018 291 DGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02979 284 DGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR 350
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
10-358 |
1.28e-116 |
|
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240088 [Multi-domain] Cd Length: 351 Bit Score: 342.50 E-value: 1.28e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 10 DYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVD 89
Cdd:cd04737 10 DLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 90 GELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFD 169
Cdd:cd04737 90 GEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGGNREA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 170 DVRNRFKLPpqLRMKNFEtNDLAFSPKGnfgdnSGLAEYVAQAiDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVK 249
Cdd:cd04737 170 DIRNKFQFP--FGMPNLN-HFSEGTGKG-----KGISEIYAAA-KQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 250 HGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGV 329
Cdd:cd04737 241 AGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGV 320
|
330 340
....*....|....*....|....*....
gi 2203519018 330 QDVLEILKEEFRLAMALSGCQNVKVIDKT 358
Cdd:cd04737 321 ASVLEHLNKELKIVMQLAGTRTIEDVKRT 349
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
10-357 |
1.11e-91 |
|
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240087 Cd Length: 361 Bit Score: 279.02 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 10 DYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVD 89
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 90 GELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYIYKdREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFD 169
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDL-WFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 170 DVRNRFKLP--------------PQLRMKNFETNDLAfspKGNFG--DNSGLAEYVA---QAIDPSLSWDDIKWLRRLTS 230
Cdd:cd04736 160 DLRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPQ---LANFAsdDAIDVEVQAAlmsRQMDASFNWQDLRWLRDLWP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 231 LPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVegKVEVFLDGGVRKGTDVLKALALGARA 310
Cdd:cd04736 237 HKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2203519018 311 VFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd04736 315 VLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
7-366 |
4.09e-90 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 275.75 E-value: 4.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 7 CISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPIC---VGATAMq 83
Cdd:PRK11197 5 AASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVAlapVGLTGM- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 84 cMAHvDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPY 163
Cdd:PRK11197 84 -YAR-RGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPM-WFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 164 LGNRFDDVRNRFKLPP-------QLRMKNFETNDLAFSPK----GN----FGDNSGLAEYVAQA---IDPSLSWDDIKWL 225
Cdd:PRK11197 161 PGARYRDAHSGMSGPNaamrrylQAVTHPQWAWDVGLNGRphdlGNisayLGKPTGLEDYIGWLgnnFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 226 RRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALA 305
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203519018 306 LGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLA 366
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGNAA 381
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
56-353 |
2.00e-19 |
|
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.
Pssm-ID: 239205 [Multi-domain] Cd Length: 326 Bit Score: 87.94 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 56 NVADIDLSTSVLGQRVSMPICVGAtamqcM-------AHVDGELAtvRACQTMGTGMMLSS----------WATSSIeeV 118
Cdd:cd02811 36 DLDDIDLSTEFLGKRLSAPLLISA-----MtggsekaKEINRNLA--EAAEELGIAMGVGSqraaledpelAESFTV--V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 119 AEAGPEALRWMQLYIYKDREVSSQLVKRAEQM-GYKAIFVTVdtpylgnrfddvrNrfklPPQlrmknfEtndlAFSPKG 197
Cdd:cd02811 107 REAPPNGPLIANLGAVQLNGYGVEEARRAVEMiEADALAIHL-------------N----PLQ------E----AVQPEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 198 --NFgdnSGLaeyvaqaidpslsWDDIKWLRRLTSLPIVVK----GILRgDDAQEAVKHGVDGILVSNHG---------A 262
Cdd:cd02811 160 drDF---RGW-------------LERIEELVKALSVPVIVKevgfGISR-ETAKRLADAGVKAIDVAGAGgtswarvenY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 263 RQLD------------GVPaTIDALPEIVEAVEgKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIwGLAFQGEKGVQ 330
Cdd:cd02811 223 RAKDsdqrlaeyfadwGIP-TAASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVI 299
|
330 340
....*....|....*....|...
gi 2203519018 331 DVLEILKEEFRLAMALSGCQNVK 353
Cdd:cd02811 300 ETIEQIIEELRTAMFLTGAKNLA 322
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
204-315 |
1.94e-09 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 56.83 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 204 GLAEYVAQAIDPSLSWDDIKWLR-RLTSLPIVVKGILRGDDAQEAVK-HGVDGILVSNHGARQLDGVPATIDALPEIVEA 281
Cdd:cd04722 87 GVEIHGAVGYLAREDLELIRELReAVPDVKVVVKLSPTGELAAAAAEeAGVDEVGLGNGGGGGGGRDAVPIADLLLILAK 166
|
90 100 110
....*....|....*....|....*....|....
gi 2203519018 282 VEGKVEVFLDGGVRKGTDVLKALALGARAVFVGR 315
Cdd:cd04722 167 RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
232-316 |
1.08e-08 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 56.19 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 232 PIVVK---GILRGDDAQEAVKHGVDGILVSNH----GA-----RQLDGVPaTIDALPEIVEAV--EG---KVEVFLDGGV 294
Cdd:pfam01645 204 PISVKlvsGHGVGTIAAGVAKAGADIILIDGYdggtGAspktsIKHAGLP-WELALAEAHQTLkeNGlrdRVSLIADGGL 282
|
90 100
....*....|....*....|..
gi 2203519018 295 RKGTDVLKALALGARAVFVGRP 316
Cdd:pfam01645 283 RTGADVAKAAALGADAVYIGTA 304
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
222-315 |
1.26e-08 |
|
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.
Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 56.01 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 222 IKWLRRLT-SLPIVVK---GILRGDDAqEAVKHG-VDGILVSNH----GARQL---D--GVPaTIDALPEIVEA-----V 282
Cdd:cd02808 205 IEDLREATgGKPIGVKlvaGHGEGDIA-AGVAAAgADFITIDGAeggtGAAPLtfiDhvGLP-TELGLARAHQAlvkngL 282
|
90 100 110
....*....|....*....|....*....|...
gi 2203519018 283 EGKVEVFLDGGVRKGTDVLKALALGARAVFVGR 315
Cdd:cd02808 283 RDRVSLIASGGLRTGADVAKALALGADAVGIGT 315
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
242-314 |
2.03e-06 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 48.25 E-value: 2.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203519018 242 DDAQEAVKHGVDGILVSN-----HGARQLDGvpaTIDALPEIVEAVegKVEVFLDGGVRKGTDVLKALALGARAVFVG 314
Cdd:cd04730 113 EEARKAEAAGADALVAQGaeaggHRGTFDIG---TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
244-314 |
9.99e-06 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 46.64 E-value: 9.99e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203519018 244 AQEAVKHGVDGILVSNHGA---RQLDGVPaTIDALPEIVEAVegKVEVFLDGGVRKGTDVLKALALGARAVFVG 314
Cdd:COG2070 117 ARKAEKAGADAVVAEGAEAgghRGADEVS-TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 187
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
222-316 |
4.50e-05 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 44.82 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 222 IKWLRRL-TSLPIVVKGILRGDDAQEAVKHGVDGILV-----SNHGARQLDGV--P-ATidALPEIVEAVEG-KVEVFLD 291
Cdd:cd00381 126 IKFIKKKyPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgvPqAT--AVADVAAAARDyGVPVIAD 203
|
90 100
....*....|....*....|....*
gi 2203519018 292 GGVRKGTDVLKALALGARAVFVGRP 316
Cdd:cd00381 204 GGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
215-257 |
9.27e-03 |
|
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 36.76 E-value: 9.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2203519018 215 PSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILV 257
Cdd:pfam02581 134 PPLGLEGLKAIAEAVEIPVVAIGGITPENVPEVIEAGADGVAV 176
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
223-319 |
9.61e-03 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 37.33 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 223 KWLRRLTSLPIVVK--GILRGDDAQEAVK----HGVDGILVSNH-GARQLD-------------GV------PATIDALP 276
Cdd:cd02810 155 KAVKAAVDIPLLVKlsPYFDLEDIVELAKaaerAGADGLTAINTiSGRVVDlktvgpgpkrgtgGLsgapirPLALRWVA 234
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2203519018 277 EIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIW 319
Cdd:cd02810 235 RLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMW 277
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
222-315 |
9.63e-03 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 37.75 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203519018 222 IKWLR-RLTSLPIVVKGILRGDDAQEAVKHGVDGI-------------LVSnhGArqldGVPaTIDALPEIVEAVEG-KV 286
Cdd:pfam00478 252 VKWIKkKYPDVQVIAGNVATAEGAKALIEAGADAVkvgigpgsicttrVVA--GV----GVP-QLTAIYDVAEAAKKyGV 324
|
90 100
....*....|....*....|....*....
gi 2203519018 287 EVFLDGGVRKGTDVLKALALGARAVFVGR 315
Cdd:pfam00478 325 PVIADGGIKYSGDIVKALAAGADAVMLGS 353
|
|
| |
