|
Name |
Accession |
Description |
Interval |
E-value |
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
11-337 |
2.85e-172 |
|
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: 481.23 E-value: 2.85e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 11 RKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:cd02811 1 RKDEHLELCLEENVESGGSTGFDDVRLVHNALPELDLDDIDLSTEFLGKRLSAPLLISAMTGGSEKAKEINRNLAEAAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 91 AGIAMGLGSMRVLLTEPDTIKTFAVRHIA-PDIPLLANIGAIQLNyGVTPKECQYLVDAIKADALILHLNVLQELTQPEG 169
Cdd:cd02811 81 LGIAMGVGSQRAALEDPELAESFTVVREApPNGPLIANLGAVQLN-GYGVEEARRAVEMIEADALAIHLNPLQEAVQPEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 170 NRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSlQNRIASSFINW 249
Cdd:cd02811 160 DRDFRGWLERIEELVKALSVPVIVKEVGFGISRETAKRLADAGVKAIDVAGAGGTSWARVENYRAKDS-DQRLAEYFADW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 250 GIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAADTSERLLSEEIQLIIEQLKITMLCTGS 329
Cdd:cd02811 239 GIPTAASLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALEGEEAVIETIEQIIEELRTAMFLTGA 318
|
....*...
gi 504205390 330 RTLKDLAK 337
Cdd:cd02811 319 KNLAELKQ 326
|
|
| IPP_isom_2 |
TIGR02151 |
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP ... |
10-340 |
4.86e-163 |
|
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP isomerase) interconverts isopentenyl diphosphate and dimethylallyl diphosphate. This model represents the type 2 enzyme. FMN, NADPH, and Mg2+ are required by this form, which lacks homology to the type 1 enzyme (TIGR02150). IPP is precursor to many compounds, including enzyme cofactors, sterols, and isoprenoids. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273999 Cd Length: 333 Bit Score: 458.27 E-value: 4.86e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 10 ERKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQ 89
Cdd:TIGR02151 1 ERKDEHIELCLKQNVEYGGSTGFDDITLIHNALPEINLDDIDLTTEFLGKRLKAPFYINAMTGGSEEAGKINRNLARAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 90 KAGIAMGLGSMRVLLTEPDTIKTF-AVRHIAPDIPLLANIGAIQLNYGVtPKECQYLVDAIKADALILHLNVLQELTQPE 168
Cdd:TIGR02151 81 ELGIPMGVGSQRAALKDPETADTFeVVREEAPNGPLIANIGAPQLVEGG-PEEAQEAIDMIEADALAIHLNVLQELVQPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 169 GNRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSLQnriASSFIN 248
Cdd:TIGR02151 160 GDRNFKGWLEKIAEICSQLSVPVIVKEVGFGISKEVAKLLADAGVSAIDVAGAGGTSWAQVENYRAKGSNL---ASFFND 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 249 WGIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAA-DTSERLLSEEIQLIIEQLKITMLCT 327
Cdd:TIGR02151 237 WGIPTAASLLEVRSDAPDAPIIASGGLRTGLDVAKAIALGADAVGMARPFLKAAlDEGEEAVIEEIELIIEELKVAMFLT 316
|
330
....*....|...
gi 504205390 328 GSRTLKDLAKAEI 340
Cdd:TIGR02151 317 GAKTIAELKKVPL 329
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
14-342 |
2.53e-68 |
|
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: 218.08 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 14 DHIEINLtkNVESTLK---SGFESIQFIHNALpeINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:COG1304 24 DYIDGGA--GDEVTLRrnrAAFDRVRLRPRVL--EDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 91 AGIAMGLGSMRVlltepDTIKTfaVRHIAPDIPLlanigaIQLN----YGVTpKECQYLVDAIKADALILHLNV------ 160
Cdd:COG1304 100 AGIPMGLSTQST-----TSLEE--VAAAAPAPLW------FQLYvpkdRGFT-DDLLRRAEAAGADALVLTVDTpvlgrr 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 161 ---LQE-LTQPEGNR--------------------------------NWEKllpkIREVVNYLSIPVIVKEVgygLSKKV 204
Cdd:COG1304 166 erdLREgFSQPPRLTprnlleaathprwalglaslaawldtnfdpslTWDD----IAWLRERWPGPLIVKGV---LSPED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 205 AESLIDAGVKVLDIAGSGGTswsQVEAyratnslqnriassfinwGIPTLDSLKMVRE-VSKDIPIITSGGLKSGIDGAK 283
Cdd:COG1304 239 ARRAVDAGVDGIDVSNHGGR---QLDG------------------GPPTIDALPEIRAaVGGRIPVIADGGIRRGLDVAK 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 284 AIRIGANIFGLAGQFLKA-ADTSERLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEIRL 342
Cdd:COG1304 298 ALALGADAVGLGRPFLYGlAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
25-342 |
1.18e-13 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 71.02 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 25 ESTLK---SGFESIQFIHNALPEINydSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQKAGIAMGLGSM- 100
Cdd:pfam01070 20 EVTLRrnrAAFDRIRLRPRVLRDVS--NRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVLSTVs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 101 -----RV-------------LLTEPDTIKTFAVRHIAP---------DIPLLAN-----IGAIQLNYGVTPKE------- 141
Cdd:pfam01070 98 stsleEVaaaaggplwfqlyVPRDRELTEDLLERAEAAgykalvltvDTPVLGRrerdlRNGFTLPPRLTPRNlldlalh 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 142 CQYLVDAIKADALILHLNVLQEltQPEGNRNWEkllpKIREVVNYLSIPVIVKEVgygLSKKVAESLIDAGVKVLDIAGS 221
Cdd:pfam01070 178 PRWALGVLRRGGAGGAAAFVGS--QFDPALTWD----DLAWLRERWKGPLVVKGI---LSPEDAKRAVEAGVDGIVVSNH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 222 GGtswsqveayRATNSlqnriassfinwGIPTLDSL-KMVREVSKDIPIITSGGLKSGIDGAKAIRIGAN--------IF 292
Cdd:pfam01070 249 GG---------RQLDG------------APATIDALpEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADavllgrpfLY 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 504205390 293 GLAgqfLKAADTSERLLseeiQLIIEQLKITMLCTGSRTLKDLAKAEIRL 342
Cdd:pfam01070 308 GLA---AGGEAGVAHAL----EILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
258-341 |
2.64e-04 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 42.52 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 258 KMVREVSKDIPIITSGGLKSGIDGAKAIRIGAN--------IFGLAGqflKAADTSERLlseeIQLIIEQLKITMLCTGS 329
Cdd:PLN02535 270 EVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQavlvgrpvIYGLAA---KGEDGVRKV----IEMLKDELEITMALSGC 342
|
90
....*....|..
gi 504205390 330 RTLKDLAKAEIR 341
Cdd:PLN02535 343 PSVKDITRSHVR 354
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
11-337 |
2.85e-172 |
|
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: 481.23 E-value: 2.85e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 11 RKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:cd02811 1 RKDEHLELCLEENVESGGSTGFDDVRLVHNALPELDLDDIDLSTEFLGKRLSAPLLISAMTGGSEKAKEINRNLAEAAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 91 AGIAMGLGSMRVLLTEPDTIKTFAVRHIA-PDIPLLANIGAIQLNyGVTPKECQYLVDAIKADALILHLNVLQELTQPEG 169
Cdd:cd02811 81 LGIAMGVGSQRAALEDPELAESFTVVREApPNGPLIANLGAVQLN-GYGVEEARRAVEMIEADALAIHLNPLQEAVQPEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 170 NRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSlQNRIASSFINW 249
Cdd:cd02811 160 DRDFRGWLERIEELVKALSVPVIVKEVGFGISRETAKRLADAGVKAIDVAGAGGTSWARVENYRAKDS-DQRLAEYFADW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 250 GIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAADTSERLLSEEIQLIIEQLKITMLCTGS 329
Cdd:cd02811 239 GIPTAASLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALEGEEAVIETIEQIIEELRTAMFLTGA 318
|
....*...
gi 504205390 330 RTLKDLAK 337
Cdd:cd02811 319 KNLAELKQ 326
|
|
| IPP_isom_2 |
TIGR02151 |
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP ... |
10-340 |
4.86e-163 |
|
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP isomerase) interconverts isopentenyl diphosphate and dimethylallyl diphosphate. This model represents the type 2 enzyme. FMN, NADPH, and Mg2+ are required by this form, which lacks homology to the type 1 enzyme (TIGR02150). IPP is precursor to many compounds, including enzyme cofactors, sterols, and isoprenoids. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273999 Cd Length: 333 Bit Score: 458.27 E-value: 4.86e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 10 ERKQDHIEINLTKNVESTLKSGFESIQFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQ 89
Cdd:TIGR02151 1 ERKDEHIELCLKQNVEYGGSTGFDDITLIHNALPEINLDDIDLTTEFLGKRLKAPFYINAMTGGSEEAGKINRNLARAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 90 KAGIAMGLGSMRVLLTEPDTIKTF-AVRHIAPDIPLLANIGAIQLNYGVtPKECQYLVDAIKADALILHLNVLQELTQPE 168
Cdd:TIGR02151 81 ELGIPMGVGSQRAALKDPETADTFeVVREEAPNGPLIANIGAPQLVEGG-PEEAQEAIDMIEADALAIHLNVLQELVQPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 169 GNRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSLQnriASSFIN 248
Cdd:TIGR02151 160 GDRNFKGWLEKIAEICSQLSVPVIVKEVGFGISKEVAKLLADAGVSAIDVAGAGGTSWAQVENYRAKGSNL---ASFFND 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 249 WGIPTLDSLKMVREVSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKAA-DTSERLLSEEIQLIIEQLKITMLCT 327
Cdd:TIGR02151 237 WGIPTAASLLEVRSDAPDAPIIASGGLRTGLDVAKAIALGADAVGMARPFLKAAlDEGEEAVIEEIELIIEELKVAMFLT 316
|
330
....*....|...
gi 504205390 328 GSRTLKDLAKAEI 340
Cdd:TIGR02151 317 GAKTIAELKKVPL 329
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
14-342 |
2.53e-68 |
|
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: 218.08 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 14 DHIEINLtkNVESTLK---SGFESIQFIHNALpeINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQK 90
Cdd:COG1304 24 DYIDGGA--GDEVTLRrnrAAFDRVRLRPRVL--EDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 91 AGIAMGLGSMRVlltepDTIKTfaVRHIAPDIPLlanigaIQLN----YGVTpKECQYLVDAIKADALILHLNV------ 160
Cdd:COG1304 100 AGIPMGLSTQST-----TSLEE--VAAAAPAPLW------FQLYvpkdRGFT-DDLLRRAEAAGADALVLTVDTpvlgrr 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 161 ---LQE-LTQPEGNR--------------------------------NWEKllpkIREVVNYLSIPVIVKEVgygLSKKV 204
Cdd:COG1304 166 erdLREgFSQPPRLTprnlleaathprwalglaslaawldtnfdpslTWDD----IAWLRERWPGPLIVKGV---LSPED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 205 AESLIDAGVKVLDIAGSGGTswsQVEAyratnslqnriassfinwGIPTLDSLKMVRE-VSKDIPIITSGGLKSGIDGAK 283
Cdd:COG1304 239 ARRAVDAGVDGIDVSNHGGR---QLDG------------------GPPTIDALPEIRAaVGGRIPVIADGGIRRGLDVAK 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 284 AIRIGANIFGLAGQFLKA-ADTSERLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEIRL 342
Cdd:COG1304 298 ALALGADAVGLGRPFLYGlAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
25-342 |
1.18e-13 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 71.02 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 25 ESTLK---SGFESIQFIHNALPEINydSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQKAGIAMGLGSM- 100
Cdd:pfam01070 20 EVTLRrnrAAFDRIRLRPRVLRDVS--NRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVLSTVs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 101 -----RV-------------LLTEPDTIKTFAVRHIAP---------DIPLLAN-----IGAIQLNYGVTPKE------- 141
Cdd:pfam01070 98 stsleEVaaaaggplwfqlyVPRDRELTEDLLERAEAAgykalvltvDTPVLGRrerdlRNGFTLPPRLTPRNlldlalh 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 142 CQYLVDAIKADALILHLNVLQEltQPEGNRNWEkllpKIREVVNYLSIPVIVKEVgygLSKKVAESLIDAGVKVLDIAGS 221
Cdd:pfam01070 178 PRWALGVLRRGGAGGAAAFVGS--QFDPALTWD----DLAWLRERWKGPLVVKGI---LSPEDAKRAVEAGVDGIVVSNH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 222 GGtswsqveayRATNSlqnriassfinwGIPTLDSL-KMVREVSKDIPIITSGGLKSGIDGAKAIRIGAN--------IF 292
Cdd:pfam01070 249 GG---------RQLDG------------APATIDALpEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADavllgrpfLY 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 504205390 293 GLAgqfLKAADTSERLLseeiQLIIEQLKITMLCTGSRTLKDLAKAEIRL 342
Cdd:pfam01070 308 GLA---AGGEAGVAHAL----EILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
25-335 |
7.59e-10 |
|
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: 59.00 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 25 ESTLK---SGFESIQFIHNALPEInyDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAHVAQKAGIAMGLGSMr 101
Cdd:cd02809 26 EVTLRrnrAAFDRIRLRPRVLRDV--SKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPDGELATARAAAAAGIPFTLSTV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 102 vlltepdtiKTFAVRHIAPDIPLLANIgaiQLNYGVTPKECQYLVD---AIKADALILHLNvlqelTQPEGNR-NWEKll 177
Cdd:cd02809 103 ---------STTSLEEVAAAAPGPRWF---QLYVPRDREITEDLLRraeAAGYKALVLTVD-----TPVLGRRlTWDD-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 178 pkIREVVNYLSIPVIVKEVgygLSKKVAESLIDAGVK----------VLDIAgsggtswsqveayratnslqnriassfi 247
Cdd:cd02809 164 --LAWLRSQWKGPLILKGI---LTPEDALRAVDAGADgivvsnhggrQLDGA---------------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 248 nwgIPTLDSLKMVRE-VSKDIPIITSGGLKSGIDGAKAIRIGAN--------IFGLAGQflkAADTSERLLseeiQLIIE 318
Cdd:cd02809 211 ---PATIDALPEIVAaVGGRIEVLLDGGIRRGTDVLKALALGADavligrpfLYGLAAG---GEAGVAHVL----EILRD 280
|
330
....*....|....*..
gi 504205390 319 QLKITMLCTGSRTLKDL 335
Cdd:cd02809 281 ELERAMALLGCASLADL 297
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
46-340 |
1.83e-08 |
|
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: 55.14 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 46 NYDSVNTTTTFLGKSLQAPILISSMTGgttrardinYRLAHVAQKAGIAMGLGSMRVLLTepdtIKTFAVRHIaPDIPLL 125
Cdd:cd04737 56 GVESPDTSTELLGIKLKTPIIMAPIAA---------HGLAHATGEVATARGMAEVGSLFS----ISTYSNTSL-EEIAKA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 126 ANIGA--IQLNYGVTPKECQYLVDAIKAD---ALILH----------------------LNVLQELTQPEG-----NRNW 173
Cdd:cd04737 122 SNGGPkwFQLYMSKDDGFNRSLLDRAKAAgakAIILTadatvggnreadirnkfqfpfgMPNLNHFSEGTGkgkgiSEIY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 174 E----KLLPK-IREVVNYLSIPVIVKEVgygLSKKVAESLIDAGVKVLDIAGSGGTSwsqveayratnslqnriassfIN 248
Cdd:cd04737 202 AaakqKLSPAdIEFIAKISGLPVIVKGI---QSPEDADVAINAGADGIWVSNHGGRQ---------------------LD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 249 WGIPTLDSLKMVRE-VSKDIPIITSGGLKSGIDGAKAIRIGAN--------IFGLA-GQFLKAADTSERLLSEeiqliie 318
Cdd:cd04737 258 GGPASFDSLPEIAEaVNHRVPIIFDSGVRRGEHVFKALASGADavavgrpvLYGLAlGGAQGVASVLEHLNKE------- 330
|
330 340
....*....|....*....|..
gi 504205390 319 qLKITMLCTGSRTLKDLAKAEI 340
Cdd:cd04737 331 -LKIVMQLAGTRTIEDVKRTFL 351
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
119-296 |
2.73e-08 |
|
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: 53.36 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 119 APDIPLLANIGAIqlNYGVTPKECQYLVDAIKADALILHLNVLQELtqpegnRNWEKLLPKIREVvnYLSIPVIVKEVGY 198
Cdd:cd04722 55 ETDLPLGVQLAIN--DAAAAVDIAAAAARAAGADGVEIHGAVGYLA------REDLELIRELREA--VPDVKVVVKLSPT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 199 GlsKKVAESLIDAGVKVLDIAGSGGTSWSQVEAyratnslqnriassfinwgiPTLDSLKMVREVSKDIPIITSGGLKSG 278
Cdd:cd04722 125 G--ELAAAAAEEAGVDEVGLGNGGGGGGGRDAV--------------------PIADLLLILAKRGSKVPVIAGGGINDP 182
|
170
....*....|....*...
gi 504205390 279 IDGAKAIRIGANIFGLAG 296
Cdd:cd04722 183 EDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
179-301 |
1.73e-06 |
|
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: 49.08 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 179 KIREVVNYlsIPVIVKEVGYGLskkvaESLIDAGVK-----VLDIAGS-GGTSWSQVEayratnslqnriassFIN-WGI 251
Cdd:cd02808 207 DLREATGG--KPIGVKLVAGHG-----EGDIAAGVAaagadFITIDGAeGGTGAAPLT---------------FIDhVGL 264
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504205390 252 PTLDSLKMVRE------VSKDIPIITSGGLKSGIDGAKAIRIGANIFGLAGQFLKA 301
Cdd:cd02808 265 PTELGLARAHQalvkngLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIA 320
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
119-295 |
1.25e-04 |
|
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: 43.11 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 119 APDIPLLANIGAIQLNYGVtpkECQYLVDAIKADALILHLNVLQELTQPEGNRNWEKLLPKIREVVNYLSIPVIVKeVGY 198
Cdd:cd02810 96 FPGQPLIASVGGSSKEDYV---ELARKIERAGAKALELNLSCPNVGGGRQLGQDPEAVANLLKAVKAAVDIPLLVK-LSP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 199 GLSKKVAESLidagVKVLDIAGsggtswsqVEAYRATNSLQNRIASSfINWGIPTLD-------------SLKMVREVS- 264
Cdd:cd02810 172 YFDLEDIVEL----AKAAERAG--------ADGLTAINTISGRVVDL-KTVGPGPKRgtgglsgapirplALRWVARLAa 238
|
170 180 190
....*....|....*....|....*....|....
gi 504205390 265 ---KDIPIITSGGLKSGIDGAKAIRIGANIFGLA 295
Cdd:cd02810 239 rlqLDIPIIGVGGIDSGEDVLEMLMAGASAVQVA 272
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
258-341 |
2.64e-04 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 42.52 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 258 KMVREVSKDIPIITSGGLKSGIDGAKAIRIGAN--------IFGLAGqflKAADTSERLlseeIQLIIEQLKITMLCTGS 329
Cdd:PLN02535 270 EVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQavlvgrpvIYGLAA---KGEDGVRKV----IEMLKDELEITMALSGC 342
|
90
....*....|..
gi 504205390 330 RTLKDLAKAEIR 341
Cdd:PLN02535 343 PSVKDITRSHVR 354
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
190-295 |
9.40e-04 |
|
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: 40.78 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 190 PVIVK---EVGYGLskkVAESLIDAGVKVLDIAG-SGGTSWSQVeayratnslqnriaSSFINWGIPTLDSLKMVREVSK 265
Cdd:pfam01645 204 PISVKlvsGHGVGT---IAAGVAKAGADIILIDGyDGGTGASPK--------------TSIKHAGLPWELALAEAHQTLK 266
|
90 100 110
....*....|....*....|....*....|....*.
gi 504205390 266 D------IPIITSGGLKSGIDGAKAIRIGANIFGLA 295
Cdd:pfam01645 267 EnglrdrVSLIADGGLRTGADVAKAAALGADAVYIG 302
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
66-293 |
1.24e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 39.62 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 66 LISSMTGGTTRARDINyRLAHVAQKAGIAmglgsmrVLLTEPDTIKTfAVRHIAP-DIPLLANIGAiqlNYGVTPKEC-- 142
Cdd:cd00945 1 IDLTLLHPDATLEDIA-KLCDEAIEYGFA-------AVCVNPGYVRL-AADALAGsDVPVIVVVGF---PTGLTTTEVkv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 143 QYLVDAIK--ADALILHLNVLQELtqpegNRNWEKLLPKIREVVNYLSIPVIVK---EVGYGLSK----KVAESLIDAG- 212
Cdd:cd00945 69 AEVEEAIDlgADEIDVVINIGSLK-----EGDWEEVLEEIAAVVEAADGGLPLKvilETRGLKTAdeiaKAARIAAEAGa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 213 --VKVldiagsgGTSWSQVEAyratnslqnriassfinwgipTLDSLK-MVREVSKDIPIITSGGLKSGIDGAKAIRIGA 289
Cdd:cd00945 144 dfIKT-------STGFGGGGA---------------------TVEDVKlMKEAVGGRVGVKAAGGIKTLEDALAAIEAGA 195
|
....
gi 504205390 290 NIFG 293
Cdd:cd00945 196 DGIG 199
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
257-320 |
1.55e-03 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B 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.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 39.84 E-value: 1.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504205390 257 LKMVREVSK--DIPIITSGGLKSGID-------GAKAIRIGANIFGLAGQFLKAADTSERLLSEEIQLIIEQL 320
Cdd:cd04740 220 LRMVYQVYKavEIPIIGVGGIASGEDaleflmaGASAVQVGTANFVDPEAFKEIIEGLEAYLDEEGIKSIEEL 292
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
189-340 |
1.90e-03 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 39.71 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 189 IPVIVKEVGYGLSKKVAeslIDAGVKVLDIAGSGGTSWSQVEAyratnslqnriassfinwgipTLDSLK-MVREVSKDI 267
Cdd:PLN02979 224 LPILVKGVLTGEDARIA---IQAGAAGIIVSNHGARQLDYVPA---------------------TISALEeVVKATQGRI 279
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504205390 268 PIITSGGLKSGIDGAKAIRIGAN-IFGLAGQFLKAADTSERLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEI 340
Cdd:PLN02979 280 PVFLDGGVRRGTDVFKALALGASgIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 353
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
180-299 |
3.17e-03 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 39.09 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 180 IREVVNyLSIPVIVK-----EVGYGL----SKKVAESLIDAGVKVLDIagSGGTSWSQVEAYRATNSLQNRIassfinwg 250
Cdd:cd02803 201 VREAVG-PDFPVGVRlsaddFVPGGLtleeAIEIAKALEEAGVDALHV--SGGSYESPPPIIPPPYVPEGYF-------- 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 504205390 251 iptLDSLKMVREVSkDIPIITSGGLKSGIDGAKAIRIG-ANIFGLAGQFL 299
Cdd:cd02803 270 ---LELAEKIKKAV-KIPVIAVGGIRDPEVAEEILAEGkADLVALGRALL 315
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
188-340 |
4.49e-03 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 38.56 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 188 SIPVIVKEVGYGLSKKVAeslIDAGVKVLDIAGSGGTSWSQVEAyratnslqnriassfinwgipTLDSLK-MVREVSKD 266
Cdd:PLN02493 224 KLPILVKGVLTGEDARIA---IQAGAAGIIVSNHGARQLDYVPA---------------------TISALEeVVKATQGR 279
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504205390 267 IPIITSGGLKSGIDGAKAIRIGAN-IF-GLAGQFLKAADtSERLLSEEIQLIIEQLKITMLCTGSRTLKDLAKAEI 340
Cdd:PLN02493 280 IPVFLDGGVRRGTDVFKALALGASgIFiGRPVVFSLAAE-GEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 354
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
257-292 |
5.10e-03 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 38.21 E-value: 5.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 504205390 257 LKMVREVSK--DIPIITSGGLKSGID-------GAKAIRIGANIF 292
Cdd:PRK07259 223 LRMVYQVYQavDIPIIGMGGISSAEDaiefimaGASAVQVGTANF 267
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
185-290 |
8.96e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 37.64 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504205390 185 NYLSIPVIVKEVgygLSKKVAESLIDAGVKVLDIA-GSGGTSWSQVeayratnslqnrIASSfinwGIPTLDSLKMVREV 263
Cdd:PTZ00314 279 NYPHVDIIAGNV---VTADQAKNLIDAGADGLRIGmGSGSICITQE------------VCAV----GRPQASAVYHVARY 339
|
90 100
....*....|....*....|....*....
gi 504205390 264 SKD--IPIITSGGLKSGIDGAKAIRIGAN 290
Cdd:PTZ00314 340 ARErgVPCIADGGIKNSGDICKALALGAD 368
|
|
|