|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06854 |
PRK06854 |
adenylyl-sulfate reductase subunit alpha; |
14-661 |
0e+00 |
|
adenylyl-sulfate reductase subunit alpha;
Pssm-ID: 235879 [Multi-domain] Cd Length: 608 Bit Score: 1132.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 14 PLAEPELVELETDALIVGGGMGACGVAYEACRWADkhGVRVLLVDKAALERSGAVAQGLSAINTYLGKNE-PDDYVRMVR 92
Cdd:PRK06854 1 AMANPEVVEVDTDILIIGGGMAGCGAAFEAKEWAP--DLKVLIVEKANIKRSGAVAQGLSAINAYIGEGEtPEDYVRYVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 93 TDLMGLVREDLIFDLGRHVDDSVHLFEEWGLPCWIKKDGKnldgaeakkqgfslrkgdePVRSGRWQIMINGESYKCIVA 172
Cdd:PRK06854 79 KDLMGIVREDLVYDIARHVDSVVHLFEEWGLPIWKDENGK-------------------YVRRGRWQIMINGESYKPIVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 173 EAAKKALGeDRYMERVFIVKLLLDakvENRIAGAVGFSVRENKVYVIKANAICCACGGAVNVYRPRSTGEGMGRAWYPVW 252
Cdd:PRK06854 140 EAAKKALG-DNVLNRVFITDLLVD---DNRIAGAVGFSVRENKFYVFKAKAVIVATGGAAGIYRPRSPGEGRGRMWYPPF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 253 NAGSTYTMCAQVGAEMTMMENRFVPARFKDGYGPVGAWFLLFKAKATNAKGEDYCVTNRAMLKPYedRGYAKGQVIPTCL 332
Cdd:PRK06854 216 NTGSGYAMGIRAGAEMTTFENRFIPLRFKDGYGPVGAWFLLFKAKAVNALGEEYEAKNAAELKKY--VPYADYKPIPTCL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 333 RNHMMLREMREGRGPIYMDTATALQttfkeltpkeQKHLESEAWEDFLDMCVGQANLWACMNIKPEERGSEIMPTEPYLL 412
Cdd:PRK06854 294 RNYATVEENKAGRGPIYMDTEEALQ----------DKHLESELWEDFLDMTPGQALLWAAQNIEPEEENSEIMGTEPYIV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 413 GSHSGCCGIWVSGPDEEWVPEeykvradNGKVYNRMTTVNGLFTCADGVGASGHKFSSGSHAEGRIVGKQMVRWCVDHKD 492
Cdd:PRK06854 364 GSHSGASGYWVSGPEDWVPEE-------YKWGYNRMTTVEGLFAAGDVVGGSPHKFSSGSFAEGRIAAKAAVRYILDNKD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 493 FKPTLQLD-AEALKKEIYQPWYTYEQYKGASTDPVVNPNYITPHNFMMRLIKATDEYGGGVATLYTTSEKLLDTGFALLD 571
Cdd:PRK06854 437 EKPEIDDDqIEELKKEIYAPLERYEEFKDYSTDPDVNPNYISPEQLEERLQKIMDEYAGGISTNYTTNEKLLEIALELLE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 572 MLEEDSKKLAARDLHELLRCWEQYHRLWTVRLHMQHIRFRQESRYPGFYYRADFMGIDDSKWKCFVNSKYDPKTGETTVF 651
Cdd:PRK06854 517 MLEEDSEKLAARDLHELMRCWELKHRLLVAEAHIRHLLFRKETRWPGYYERADYPGKDDENWKCFVNSRYDPGTGEWTIR 596
|
650
....*....|
gi 2416254630 652 KRHYYQIIPD 661
Cdd:PRK06854 597 KLPYYQIIPE 606
|
|
| aprA |
TIGR02061 |
adenosine phosphosulphate reductase, alpha subunit; During dissimilatory sulfate reduction or ... |
26-659 |
0e+00 |
|
adenosine phosphosulphate reductase, alpha subunit; During dissimilatory sulfate reduction or sulfur oxidation, adenylylsulfate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulfite and AMP. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently bound FAD, and a beta subunit containing two [4Fe-4S] clusters. Described by this model is the alpha subunit of APS reductase, sharing common evolutionary origin with fumarate reductase/succinate dehydrogenase flavoproteins. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273946 [Multi-domain] Cd Length: 614 Bit Score: 1130.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 26 DALIVGGGMGACGVAYEACRWADKHGVRVLLVDKAALERSGAVAQGLSAINTYLG----KNEPDDYVRMVRTDLMGLVRE 101
Cdd:TIGR02061 1 DLLIVGGGMGGCGAAFEAVYWGDKKGLKIVLVEKANLERSGAVAQGLSAINTYLGtrfgENNAEDYVRYVRTDLMGLVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 102 DLIFDLGRHVDDSVHLFEEWGLPCWIK-KDGKnldgaeakkqgfslrkgdePVRSGRWQIMINGESYKCIVAEAAKKALG 180
Cdd:TIGR02061 81 DLIFDMARHVDDSVHLFEEWGLPLWIKpEDGK-------------------YVREGRWQIMIHGESYKPIVAEAAKNALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 181 EdrYMERVFIVKLLLDAKVENRIAGAVGFSVRENKVYVIKANAICCACGGAVNVYRPRSTGEGMGRAWYPVWNAGSTYTM 260
Cdd:TIGR02061 142 D--IFERIFIVKLLLDKNTPNRIAGAVGFNVRANEVHVFKAKTVIVAAGGAVNVYRPRSVGEGAGRAWYAVWNAGSTYTM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 261 CAQVGAEMTMMENRFVPARFKDGYGPVGAWFLLFKAKATNAKGEDYCVTNRAMLKPYEDRGYAKGQVIPTCLRNHMMLRE 340
Cdd:TIGR02061 220 CAQAGAEMTQMENRFVPARFKDGYGPVGAWFLLFKAKATNGKGEEYCATNRAMLKPYEGRGYAKPHVIPTCLRNHMMLRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 341 MREGRGPIYMDTATALQTTFKElTPKEQKHLESEAWEDFLDMCVGQANLWACMNIKPEERGSEIMPTEPYLLGSHSGCCG 420
Cdd:TIGR02061 300 MREGRGPIYMDTKEALQDPFAT-DKKQQKHLEEEAWEDFLDMTVGQANLWAATNVDPEERGSEIMPTEPYLMGSHSGCCG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 421 IWVSGPdEEWVPEEYKVRAdnGKVYNRMTTVNGLFTCADGVGASGHKFSSGSHAEGRIVGKQMVRWCVDHKDFKPTLQLD 500
Cdd:TIGR02061 379 IWVSGP-EDWVPEEYKVRA--AKVYNRMTTVEGLFTCGDGVGASPHKFSSGSFTEGRIAAKAAVRWILDHKDFKPEFDAT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 501 AEALKKEIYQPWYTYEQYKGASTDPVVNPNYITPHNFMMRLIKATDEYGGGVATLYTTSEKLLDTGFALLDMLEEDSKKL 580
Cdd:TIGR02061 456 AEELKKEIYRPMENYEVYKNASTAPVVNPNYINPKQGLMRLQKCMDEYGGGVTTYYMTNEALLDTGLKLMAMLEEDLEKL 535
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2416254630 581 AARDLHELLRCWEQYHRLWTVRLHMQHIRFRQESRYPGFYYRADFMGIDDSKWKCFVNSKYDPKTGETTVFKRHYYQII 659
Cdd:TIGR02061 536 AARDLHELLRAWELYHRLWTVEAHMQHILFRKETRWPGYYYRADFLGLDDENWKCFVNSKYDPATGETTIEKKPYYQII 614
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
22-272 |
2.50e-16 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 81.80 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 22 ELETDALIVGGGMGACGVAYEACRwadkHGVRVLLVDKAALERSG-AVAQG-LSAINTYLGKNEPDDYVRMVRTDLM--- 96
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAE----AGLKVLVLEKVPPRGGHtAAAQGgINAAGTNVQKAAGEDSPEEHFYDTVkgg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 97 -GLVREDLIFDLGRHVDDSVHLFEEWGLPcWIKKDGKNLDGAEAKKQGFSLRKGDepvRSGRwqimingesykCIVAEAA 175
Cdd:COG1053 77 dGLADQDLVEALAEEAPEAIDWLEAQGVP-FSRTPDGRLPQFGGHSVGRTCYAGD---GTGH-----------ALLATLY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 176 KKALGED-RYMERVFIVKLLLDakvENRIAGAVGFSvRENKVYVIKANAICCACGGAVNVYRPRSTGEGMGRAWYPVWNA 254
Cdd:COG1053 142 QAALRLGvEIFTETEVLDLIVD---DGRVVGVVARD-RTGEIVRIRAKAVVLATGGFGRNYEMRAEYLPEAEGALSTNAP 217
|
250 260
....*....|....*....|.
gi 2416254630 255 GST---YTMCAQVGAEMTMME 272
Cdd:COG1053 218 GNTgdgIAMALRAGAALADME 238
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
26-413 |
2.64e-08 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 56.53 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 26 DALIVGGGMGACGVAYEACRwadkHGVRVLLVDKAALERSGAV-AQGLSAINTYLGKNEPDDYVRMvRTDLMGLVRE--- 101
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAE----AGLKVAVVEKGQPFGGATAwSSGGIDALGNPPQGGIDSPELH-PTDTLKGLDElad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 102 -DLIFDLGRHVDDSVHLFEEWGLPcWIKKDGKNLDGAEAKKQGFSLRKGdePVRSGRWQIMINGesyKCIVAEAAKKALG 180
Cdd:pfam00890 76 hPYVEAFVEAAPEAVDWLEALGVP-FSRTEDGHLDLRPLGGLSATWRTP--HDAADRRRGLGTG---HALLARLLEGLRK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 181 EDR-YMERVFIVKLLLDakvENRIAGAVGFSVRENKVYVIKAN-AICCACGGavnvyRPRSTGEGMGRAWY-----PVWN 253
Cdd:pfam00890 150 AGVdFQPRTAADDLIVE---DGRVTGAVVENRRNGREVRIRAIaAVLLATGG-----FGRLAELLLPAAGYadttnPPAN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 254 AGSTYTMCAQVGAEMT---MMENRFVP-----------ARFKDGYGPVGAWFllfkakatNAKGEDYCVTnramLKPYED 319
Cdd:pfam00890 222 TGDGLALALRAGAALTddlMEFVQFHPtslvgirlgsgLLIEALRGEGGILV--------NKDGRRFMNE----LASRDV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 320 RGYAkgqviptclrnhMMLREMREGRGP-IYMDT-----ATALQTTFkeltpkeqkhleseawEDFLDMCVGQAnlwacm 393
Cdd:pfam00890 290 VSRA------------ITRNEIDEGRGAnVYLDAsgsldAEGLEATL----------------PAINEEAIFGL------ 335
|
410 420
....*....|....*....|
gi 2416254630 394 NIKPEERGSEIMPTEPYLLG 413
Cdd:pfam00890 336 DVDPYDRPIPVFPAQHYTMG 355
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06854 |
PRK06854 |
adenylyl-sulfate reductase subunit alpha; |
14-661 |
0e+00 |
|
adenylyl-sulfate reductase subunit alpha;
Pssm-ID: 235879 [Multi-domain] Cd Length: 608 Bit Score: 1132.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 14 PLAEPELVELETDALIVGGGMGACGVAYEACRWADkhGVRVLLVDKAALERSGAVAQGLSAINTYLGKNE-PDDYVRMVR 92
Cdd:PRK06854 1 AMANPEVVEVDTDILIIGGGMAGCGAAFEAKEWAP--DLKVLIVEKANIKRSGAVAQGLSAINAYIGEGEtPEDYVRYVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 93 TDLMGLVREDLIFDLGRHVDDSVHLFEEWGLPCWIKKDGKnldgaeakkqgfslrkgdePVRSGRWQIMINGESYKCIVA 172
Cdd:PRK06854 79 KDLMGIVREDLVYDIARHVDSVVHLFEEWGLPIWKDENGK-------------------YVRRGRWQIMINGESYKPIVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 173 EAAKKALGeDRYMERVFIVKLLLDakvENRIAGAVGFSVRENKVYVIKANAICCACGGAVNVYRPRSTGEGMGRAWYPVW 252
Cdd:PRK06854 140 EAAKKALG-DNVLNRVFITDLLVD---DNRIAGAVGFSVRENKFYVFKAKAVIVATGGAAGIYRPRSPGEGRGRMWYPPF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 253 NAGSTYTMCAQVGAEMTMMENRFVPARFKDGYGPVGAWFLLFKAKATNAKGEDYCVTNRAMLKPYedRGYAKGQVIPTCL 332
Cdd:PRK06854 216 NTGSGYAMGIRAGAEMTTFENRFIPLRFKDGYGPVGAWFLLFKAKAVNALGEEYEAKNAAELKKY--VPYADYKPIPTCL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 333 RNHMMLREMREGRGPIYMDTATALQttfkeltpkeQKHLESEAWEDFLDMCVGQANLWACMNIKPEERGSEIMPTEPYLL 412
Cdd:PRK06854 294 RNYATVEENKAGRGPIYMDTEEALQ----------DKHLESELWEDFLDMTPGQALLWAAQNIEPEEENSEIMGTEPYIV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 413 GSHSGCCGIWVSGPDEEWVPEeykvradNGKVYNRMTTVNGLFTCADGVGASGHKFSSGSHAEGRIVGKQMVRWCVDHKD 492
Cdd:PRK06854 364 GSHSGASGYWVSGPEDWVPEE-------YKWGYNRMTTVEGLFAAGDVVGGSPHKFSSGSFAEGRIAAKAAVRYILDNKD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 493 FKPTLQLD-AEALKKEIYQPWYTYEQYKGASTDPVVNPNYITPHNFMMRLIKATDEYGGGVATLYTTSEKLLDTGFALLD 571
Cdd:PRK06854 437 EKPEIDDDqIEELKKEIYAPLERYEEFKDYSTDPDVNPNYISPEQLEERLQKIMDEYAGGISTNYTTNEKLLEIALELLE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 572 MLEEDSKKLAARDLHELLRCWEQYHRLWTVRLHMQHIRFRQESRYPGFYYRADFMGIDDSKWKCFVNSKYDPKTGETTVF 651
Cdd:PRK06854 517 MLEEDSEKLAARDLHELMRCWELKHRLLVAEAHIRHLLFRKETRWPGYYERADYPGKDDENWKCFVNSRYDPGTGEWTIR 596
|
650
....*....|
gi 2416254630 652 KRHYYQIIPD 661
Cdd:PRK06854 597 KLPYYQIIPE 606
|
|
| aprA |
TIGR02061 |
adenosine phosphosulphate reductase, alpha subunit; During dissimilatory sulfate reduction or ... |
26-659 |
0e+00 |
|
adenosine phosphosulphate reductase, alpha subunit; During dissimilatory sulfate reduction or sulfur oxidation, adenylylsulfate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulfite and AMP. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently bound FAD, and a beta subunit containing two [4Fe-4S] clusters. Described by this model is the alpha subunit of APS reductase, sharing common evolutionary origin with fumarate reductase/succinate dehydrogenase flavoproteins. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273946 [Multi-domain] Cd Length: 614 Bit Score: 1130.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 26 DALIVGGGMGACGVAYEACRWADKHGVRVLLVDKAALERSGAVAQGLSAINTYLG----KNEPDDYVRMVRTDLMGLVRE 101
Cdd:TIGR02061 1 DLLIVGGGMGGCGAAFEAVYWGDKKGLKIVLVEKANLERSGAVAQGLSAINTYLGtrfgENNAEDYVRYVRTDLMGLVRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 102 DLIFDLGRHVDDSVHLFEEWGLPCWIK-KDGKnldgaeakkqgfslrkgdePVRSGRWQIMINGESYKCIVAEAAKKALG 180
Cdd:TIGR02061 81 DLIFDMARHVDDSVHLFEEWGLPLWIKpEDGK-------------------YVREGRWQIMIHGESYKPIVAEAAKNALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 181 EdrYMERVFIVKLLLDAKVENRIAGAVGFSVRENKVYVIKANAICCACGGAVNVYRPRSTGEGMGRAWYPVWNAGSTYTM 260
Cdd:TIGR02061 142 D--IFERIFIVKLLLDKNTPNRIAGAVGFNVRANEVHVFKAKTVIVAAGGAVNVYRPRSVGEGAGRAWYAVWNAGSTYTM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 261 CAQVGAEMTMMENRFVPARFKDGYGPVGAWFLLFKAKATNAKGEDYCVTNRAMLKPYEDRGYAKGQVIPTCLRNHMMLRE 340
Cdd:TIGR02061 220 CAQAGAEMTQMENRFVPARFKDGYGPVGAWFLLFKAKATNGKGEEYCATNRAMLKPYEGRGYAKPHVIPTCLRNHMMLRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 341 MREGRGPIYMDTATALQTTFKElTPKEQKHLESEAWEDFLDMCVGQANLWACMNIKPEERGSEIMPTEPYLLGSHSGCCG 420
Cdd:TIGR02061 300 MREGRGPIYMDTKEALQDPFAT-DKKQQKHLEEEAWEDFLDMTVGQANLWAATNVDPEERGSEIMPTEPYLMGSHSGCCG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 421 IWVSGPdEEWVPEEYKVRAdnGKVYNRMTTVNGLFTCADGVGASGHKFSSGSHAEGRIVGKQMVRWCVDHKDFKPTLQLD 500
Cdd:TIGR02061 379 IWVSGP-EDWVPEEYKVRA--AKVYNRMTTVEGLFTCGDGVGASPHKFSSGSFTEGRIAAKAAVRWILDHKDFKPEFDAT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 501 AEALKKEIYQPWYTYEQYKGASTDPVVNPNYITPHNFMMRLIKATDEYGGGVATLYTTSEKLLDTGFALLDMLEEDSKKL 580
Cdd:TIGR02061 456 AEELKKEIYRPMENYEVYKNASTAPVVNPNYINPKQGLMRLQKCMDEYGGGVTTYYMTNEALLDTGLKLMAMLEEDLEKL 535
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2416254630 581 AARDLHELLRCWEQYHRLWTVRLHMQHIRFRQESRYPGFYYRADFMGIDDSKWKCFVNSKYDPKTGETTVFKRHYYQII 659
Cdd:TIGR02061 536 AARDLHELLRAWELYHRLWTVEAHMQHILFRKETRWPGYYYRADFLGLDDENWKCFVNSKYDPATGETTIEKKPYYQII 614
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
17-653 |
5.69e-39 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 151.36 E-value: 5.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 17 EPELVELETDALIVGGGMGACGVAYEAcRWADKhGVRVLLVDKAALERSGAVAQGLSAINTYL--GKNEPDDYVRMVRTD 94
Cdd:PRK08275 2 AMNTQEVETDILVIGGGTAGPMAAIKA-KERNP-ALRVLLLEKANVKRSGAISMGMDGLNNAVipGHATPEQYTKEITIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 95 LMGLVREDLIFDLGRHVDDSVHLFEEWGLPcwIKKDGKnldgaeakkqgfslrkGDEPVRS----GRWQI-MINGESYKC 169
Cdd:PRK08275 80 NDGIVDQKAVYAYAEHSFETIQQLDRWGVK--FEKDET----------------GDYAVKKvhhmGSYVLpMPEGHDIKK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 170 IVAEAAKKAlgEDRYMERVFIVKLLLDAkvENRIAGAVGFSVRENKVYVIKANAICCACGGAVNVYRPrSTGEGMGRAWY 249
Cdd:PRK08275 142 VLYRQLKRA--RVLITNRIMATRLLTDA--DGRVAGALGFDCRTGEFLVIRAKAVILCCGAAGRLGLP-ASGYLFGTYEN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 250 PVwNAGSTYTMCAQVGAEMTMMENRFVPARFKDGYGPVGAWFLL-FKAKATNAKGEDYCvtnramlkpyeDRGYAKGQvi 328
Cdd:PRK08275 217 PT-NAGDGYAMAYHAGAELANLECFQINPLIKDYNGPACAYVTGpLGGYTANAKGERFI-----------ECDYWSGQ-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 329 ptclrnhMML---REMREGRGPIYMDTatalqttfkeltpkeqKHLESEA---WEDFLDMCV----GQANLWACMNIKpe 398
Cdd:PRK08275 283 -------MMWefyQELQSGNGPVFLKL----------------DHLAEETiqtIETILHTNErpsrGRFHEGRGTDYR-- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 399 ERGSEIMPTEPYLLGSHSGcCGIWVsgpDEewvpeeykvradngkvyNRMTTVNGLFTCADgVGASGHKFSSGSHAEGRI 478
Cdd:PRK08275 338 QQMVEMHISEIGFCSGHSA-SGVWV---NE-----------------KAETTVPGLYAAGD-MASVPHNYMLGAFTYGWF 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 479 VGKQMVRWCVDHkDFKPTLQLDAEALKKEIYQpwytyeqykgastdPVVNPNYITPHNFMMRLIKATDEYgggVATLYTT 558
Cdd:PRK08275 396 AGENAAEYVAGR-DLPEVDAAQVEAERARVLA--------------PLHREDGLPPAQVEYKLRRLVNDY---LQPPKVT 457
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 559 SEklLDTGFALLDMLEEDSKKLAARDLHELLRCWEqyhrlwtvrlhMQHIR-----------FRQESRYPGFYYRADFMG 627
Cdd:PRK08275 458 RK--MEIGLQRFAEIREDLERIKARDPHELMRALE-----------VSSIRdcaemaaraslFRTESRWGLYHYRVDFPE 524
|
650 660
....*....|....*....|....*.
gi 2416254630 628 IDDSKWKCFVNSKYDpKTGETTVFKR 653
Cdd:PRK08275 525 RNDAEWFCHTHLRKD-EDGRMVSFKR 549
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
18-653 |
1.09e-20 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 97.23 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 18 PEL---VELETDALIVGGGMGACGVAYEACrwadKHGVRVLLVDKAALERSGAVAQGLSAINTYL--GKNEPDDYVRMVR 92
Cdd:PRK13800 4 PALtdaLRLDCDVLVIGGGTAGTMAALTAA----EHGANVLLLEKAHVRHSGALAMGMDGVNNAVipGKAEPEDYVAEIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 93 TDLMGLVREDLIFDLGRHVDDSVHLFEEWGLpcwikKDGKNLDGAEAKKQGFslrkgdepvRSGRWQI-MINGESYKciv 171
Cdd:PRK13800 80 RANDGIVNQRTVYQTATRGFAMVQRLERYGV-----KFEKDEHGEYAVRRVH---------RSGSYVLpMPEGKDVK--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 172 aEAAKKALGEDRYMERVFIVKLLLDAKV---ENRIAGAVGFSVRENKVYVIKANAICCACGGAVNVYRPRStGEGMGRAW 248
Cdd:PRK13800 143 -KALYRVLRQRSMRERIRIENRLMPVRVlteGGRAVGAAALNTRTGEFVTVGAKAVILATGPCGRLGLPAS-GYLYGTYE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 249 YPVwNAGSTYTMCAQVGAEMTMMENRFVPARFKDGYGPVGAWFL-LFKAKATNAKGEDYCvtnramlkpyeDRGYAKGQv 327
Cdd:PRK13800 221 NPT-NAGDGYSMAYHAGAELSGIECFQINPLIKDYNGPACAYVAnPFGGYQVNAQGERFV-----------DSDYWSGQ- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 328 iptclrnhMML---REMREGRGPIYM-------DTATALQTTFKELTPKEQKHLESEAWEDFLDMCVGqanlwacMNIkp 397
Cdd:PRK13800 288 --------MMAevkREIESARGPIYLkvshlpeETLSALESILHTTERPTRGTFHANRGHDYRTHDIE-------MHI-- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 398 eergSEIMptepyLLGSHSGcCGIWVsgpDEewvpeeykvradngkvyNRMTTVNGLFTCADgVGASGHKFSSGSHAEGR 477
Cdd:PRK13800 351 ----SEIG-----LCSGHSA-SGVWV---DE-----------------HARTTVPGLYAAGD-LACVPHNYMIGAFVFGD 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 478 IVGKQMVRWCvdhKDFKPTLQLDAEALKKE---IYQPWytyeQYKGASTDPVVNpnyitphnfmMRLIKATDEYgggVAT 554
Cdd:PRK13800 400 LAGAHAAGTL---AEVPAPGELPADQLAEAhelIYRPL----RHPDGPPQPQVE----------YKLRRFVNDY---VAP 459
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 555 LYTTSEklLDTGFALLDMLEEDSKKLAARDLHELLRCWEQYHRLWTVRLHMQHIRFRQESRYPGFYYRADFMGIDDSKWK 634
Cdd:PRK13800 460 PKTAAK--LSIAVETFERMAAEIAGMGARTPHELMRCAEVSFIRDCAEMAARSSLTRTESRWGLYHDRADLPERDDASWG 537
|
650
....*....|....*....
gi 2416254630 635 CFVNSKYDPkTGETTVFKR 653
Cdd:PRK13800 538 YHLNLRKGD-DGEMEFLKR 555
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
22-272 |
2.50e-16 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 81.80 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 22 ELETDALIVGGGMGACGVAYEACRwadkHGVRVLLVDKAALERSG-AVAQG-LSAINTYLGKNEPDDYVRMVRTDLM--- 96
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAE----AGLKVLVLEKVPPRGGHtAAAQGgINAAGTNVQKAAGEDSPEEHFYDTVkgg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 97 -GLVREDLIFDLGRHVDDSVHLFEEWGLPcWIKKDGKNLDGAEAKKQGFSLRKGDepvRSGRwqimingesykCIVAEAA 175
Cdd:COG1053 77 dGLADQDLVEALAEEAPEAIDWLEAQGVP-FSRTPDGRLPQFGGHSVGRTCYAGD---GTGH-----------ALLATLY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 176 KKALGED-RYMERVFIVKLLLDakvENRIAGAVGFSvRENKVYVIKANAICCACGGAVNVYRPRSTGEGMGRAWYPVWNA 254
Cdd:COG1053 142 QAALRLGvEIFTETEVLDLIVD---DGRVVGVVARD-RTGEIVRIRAKAVVLATGGFGRNYEMRAEYLPEAEGALSTNAP 217
|
250 260
....*....|....*....|.
gi 2416254630 255 GST---YTMCAQVGAEMTMME 272
Cdd:COG1053 218 GNTgdgIAMALRAGAALADME 238
|
|
| NadB |
COG0029 |
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ... |
22-276 |
1.71e-10 |
|
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439800 [Multi-domain] Cd Length: 521 Bit Score: 63.97 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 22 ELETDALIVGGGMGACGVAYEACRwadkHGvRVLLVDKAALERSG-AVAQGlsAINTYLGKNE-PDDYVR---------- 89
Cdd:COG0029 2 RLKTDVLVIGSGIAGLSAALKLAE----RG-RVTLLTKGELGESNtRWAQG--GIAAVLDPGDsPELHIAdtlaagaglc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 90 ---MVRTdlmgLVRE------DLI-----FDlgRHVDDSVHLfeewglpcwikkdgknldGAEAkkqGFS----LRKGDe 151
Cdd:COG0029 75 dpeAVRV----LVEEgperirELIelgvpFD--RDEDGELAL------------------TREG---GHSrrriLHAGD- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 152 pvRSGRwQIMingesykcivaEAAKKALGED---RYMERVFIVKLLLDAkvENRIAGAVGFSVRENKVYVIKANAICCAC 228
Cdd:COG0029 127 --ATGR-EIE-----------RALLEAVRAHpniTVLENHFAVDLITDA--DGRCVGAYVLDEKTGEVETIRAKAVVLAT 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2416254630 229 GGAVNVYR-----PRSTGEGMGrawypvwnagstytMCAQVGAEMTMMEnrFV 276
Cdd:COG0029 191 GGAGQLYAyttnpDVATGDGIA--------------MAYRAGARLADME--FV 227
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
26-413 |
2.64e-08 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 56.53 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 26 DALIVGGGMGACGVAYEACRwadkHGVRVLLVDKAALERSGAV-AQGLSAINTYLGKNEPDDYVRMvRTDLMGLVRE--- 101
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAE----AGLKVAVVEKGQPFGGATAwSSGGIDALGNPPQGGIDSPELH-PTDTLKGLDElad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 102 -DLIFDLGRHVDDSVHLFEEWGLPcWIKKDGKNLDGAEAKKQGFSLRKGdePVRSGRWQIMINGesyKCIVAEAAKKALG 180
Cdd:pfam00890 76 hPYVEAFVEAAPEAVDWLEALGVP-FSRTEDGHLDLRPLGGLSATWRTP--HDAADRRRGLGTG---HALLARLLEGLRK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 181 EDR-YMERVFIVKLLLDakvENRIAGAVGFSVRENKVYVIKAN-AICCACGGavnvyRPRSTGEGMGRAWY-----PVWN 253
Cdd:pfam00890 150 AGVdFQPRTAADDLIVE---DGRVTGAVVENRRNGREVRIRAIaAVLLATGG-----FGRLAELLLPAAGYadttnPPAN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 254 AGSTYTMCAQVGAEMT---MMENRFVP-----------ARFKDGYGPVGAWFllfkakatNAKGEDYCVTnramLKPYED 319
Cdd:pfam00890 222 TGDGLALALRAGAALTddlMEFVQFHPtslvgirlgsgLLIEALRGEGGILV--------NKDGRRFMNE----LASRDV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 320 RGYAkgqviptclrnhMMLREMREGRGP-IYMDT-----ATALQTTFkeltpkeqkhleseawEDFLDMCVGQAnlwacm 393
Cdd:pfam00890 290 VSRA------------ITRNEIDEGRGAnVYLDAsgsldAEGLEATL----------------PAINEEAIFGL------ 335
|
410 420
....*....|....*....|
gi 2416254630 394 NIKPEERGSEIMPTEPYLLG 413
Cdd:pfam00890 336 DVDPYDRPIPVFPAQHYTMG 355
|
|
| sdhA |
PRK06263 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
22-272 |
8.79e-06 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 235758 [Multi-domain] Cd Length: 543 Bit Score: 48.82 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 22 ELETDALIVGGGMGACGVAYEAcrwadKHGVRVLLVDKAALERSG--AVAQGlsaintylGKN---EPDDYVRMVRTDLM 96
Cdd:PRK06263 5 IMITDVLIIGSGGAGARAAIEA-----ERGKNVVIVSKGLFGKSGctVMAEG--------GYNavlNPEDSFEKHFEDTM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 97 G----LVREDLIFDLGRHVDDSVHLFEEWGLPCWIKKDGKNldgAEAKKQGFSLRK----GDepvRSGRwQIMINGESYk 168
Cdd:PRK06263 72 KggayLNDPKLVEILVKEAPKRLKDLEKFGALFDRTEDGEI---AQRPFGGQSFNRtcyaGD---RTGH-EMMMGLMEY- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 169 cIVAEAAKKalgedryMERVFIVKLLLDakvENR-IAGAVGFSVRENKVYVIKANAICCACGGAVNVYrPRSTGegmgra 247
Cdd:PRK06263 144 -LIKERIKI-------LEEVMAIKLIVD---ENReVIGAIFLDLRNGEIFPIYAKATILATGGAGQLY-PITSN------ 205
|
250 260
....*....|....*....|....*
gi 2416254630 248 wyPVWNAGSTYTMCAQVGAEMTMME 272
Cdd:PRK06263 206 --PIQKTGDGFAIAYRAGAELIDME 228
|
|
| PRK09231 |
PRK09231 |
fumarate reductase flavoprotein subunit; Validated |
183-248 |
2.84e-04 |
|
fumarate reductase flavoprotein subunit; Validated
Pssm-ID: 236421 [Multi-domain] Cd Length: 582 Bit Score: 43.85 E-value: 2.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2416254630 183 RYMERvFIVKLLLDakvENRIAGAVGFSVRENKVYVIKANAICCACGGAVNVYRPRS-----TGEGMGRAW 248
Cdd:PRK09231 151 RFDEH-FVLDILVD---DGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVYRYNTnggivTGDGMGMAY 217
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
24-131 |
4.73e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 42.97 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 24 ETDALIVGGG-MGACgVAYEACRwadkHGVRVLLVDKAALER--SGAvAQGLsaINTYLGKNEPDDYVRMVRtDLMGLVR 100
Cdd:COG0665 2 TADVVVIGGGiAGLS-TAYHLAR----RGLDVTVLERGRPGSgaSGR-NAGQ--LRPGLAALADRALVRLAR-EALDLWR 72
|
90 100 110
....*....|....*....|....*....|.
gi 2416254630 101 EdlifdlgrhvddsvhLFEEWGLPCWIKKDG 131
Cdd:COG0665 73 E---------------LAAELGIDCDFRRTG 88
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
26-120 |
6.19e-04 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 42.38 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416254630 26 DALIVGGGMGACGVAYEACRwadkHGVRVLLVDKAALERSGA--VAQGLsaINTYLGKNEPDDYVRMVR--TDLMGLVRE 101
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELAR----RGLSVTLLERGDDPGSGAsgRNAGL--IHPGLRYLEPSELARLALeaLDLWEELEE 74
|
90
....*....|....*....
gi 2416254630 102 DLIFDLGRHVDDSVHLFEE 120
Cdd:pfam01266 75 ELGIDCGFRRCGVLVLARD 93
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
24-74 |
9.08e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 38.77 E-value: 9.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2416254630 24 ETDALIVGGGMGacGVAyeACRWADKHGVRVLLVDKAALERSGAVAQGLSA 74
Cdd:COG0654 3 RTDVLIVGGGPA--GLA--LALALARAGIRVTVVERAPPPRPDGRGIALSP 49
|
|
| |
