|
Name |
Accession |
Description |
Interval |
E-value |
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
59-619 |
0e+00 |
|
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441878 [Multi-domain] Cd Length: 531 Bit Score: 544.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 59 TTKYDFIVVGAGTAGCALAARLSENPRWRVLLLEAGGPENYAM-DIPI-VAHLLQLGEINWKYKTEPSnsycLAMNNNRC 136
Cdd:COG2303 2 LEEYDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRDDDPLiRMPAgYAKLLGNPRYDWRYETEPQ----PGLNGRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 137 NWPRGKVMGGSSVLNYMMYTRGNRRDYDRWARLGNPGWSYEEVLPYFKKYEGSVVPDADenLVGRNGPVKVSYSETRTRI 216
Cdd:COG2303 78 YWPRGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGADA--YHGRSGPLPVSDPPLPNPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 217 ADAFVGATQDAGLPRG-DYNGDKQIRVSYLQANIYNETRWSSNRAYLYPIKgKRRNLHVKKNALVTKILIDpqTKSAFGI 295
Cdd:COG2303 156 SDAFIEAAEELGIPRAdDFNGGACEGCGFCQVTCRNGARWSAARAYLPPAL-KRPNLTVRTGALVTRILFD--GGRATGV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 296 IVKMDGKMQKILARKEVILSAGAINTPQLLMLSGVGPAKHLREMGIKPLADL-AVGYNLQDHIAPAISFLCN-VSSLQTS 373
Cdd:COG2303 233 EYRDDGEEHTVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLpGVGRNLQDHLEVSVVFRFKePVTLNKS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 374 EMFRSEAMSDFLKGRGVLRIpGGVEAISFYALDDARnpdAWADMELFVVGGGlqtnlalrlalgiqsniYETMFGELERQ 453
Cdd:COG2303 313 LRKARIGLQYLLTRSGPLTS-NVAEAGGFFRSDPGL---ERPDLQFHFLPLG-----------------LTPRWGKKALH 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 454 SANGFLIFPMILRAKSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQAVSLLDMPAFKAIgahllekRIPNCAK 533
Cdd:COG2303 372 DGHGFTAHVEQLRPESRGRVTLDSADPLGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPY-------RGEEILP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 534 YKWKSSAYWACYARHFTFTIYHYSGTAKMGPrsDPSAVVDARLRVHGIDKLRVVDASIMPYLISGHPNGPVYLIAEKAAD 613
Cdd:COG2303 445 GPDVQSDEELAFIRARAYTIYHPVGTCRMGT--DPDSVVDPRLRVHGVENLRVVDASVMPTITSGNTNAPTIMLAEKAAD 522
|
....*.
gi 18859995 614 MIKEDH 619
Cdd:COG2303 523 MILGDY 528
|
|
| PRK02106 |
PRK02106 |
choline dehydrogenase; Validated |
59-616 |
3.06e-141 |
|
choline dehydrogenase; Validated
Pssm-ID: 235000 [Multi-domain] Cd Length: 560 Bit Score: 422.32 E-value: 3.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 59 TTKYDFIVVGAGTAGCALAARLSENPRWRVLLLEAGGPeNYAMDIPI-----VAHLLQLGEINWKYKTEPSNSyclaMNN 133
Cdd:PRK02106 3 TMEYDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGP-DYRWDFFIqmpaaLAFPLQGKRYNWAYETEPEPH----MNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 134 NRCNWPRGKVMGGSSVLNYMMYTRGNRRDYDRWARL-GNPGWSYEEVLPYFKKYEGSVVPDADenLVGRNGPVKVSYSET 212
Cdd:PRK02106 78 RRMECPRGKVLGGSSSINGMVYIRGNAMDYDNWAELpGLEGWSYADCLPYFKKAETRDGGEDD--YRGGDGPLSVTRGKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 213 RTR-IADAFVGATQDAGLPR-GDYNGDKQIRVSYLQANIYNETRWSSNRAYLYPIKgKRRNLHVKKNALVTKILIDPqtK 290
Cdd:PRK02106 156 GTNpLFQAFVEAGVQAGYPRtDDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPAL-KRPNLTIVTHALTDRILFEG--K 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 291 SAFGIIVKMDGKMQKILARKEVILSAGAINTPQLLMLSGVGPAKHLREMGIKPLADLA-VGYNLQDHIAPAISFLCN--V 367
Cdd:PRK02106 233 RAVGVEYERGGGRETARARREVILSAGAINSPQLLQLSGIGPAEHLKELGIPVVHDLPgVGENLQDHLEVYIQYECKqpV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 368 SSLQTSEMFRSEAM-------------SDFLKGRGVLRIPGGVE--AISFYAL-----DDARNPdawadmelfVVGGGLQ 427
Cdd:PRK02106 313 SLYPALKWWNKPKIgaewlftgtglgaSNHFEAGGFIRSRAGVDwpNIQYHFLpvairYDGSNA---------VKGHGFQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 428 tnlalrlalgiqsniyetmfgelerqsangFLIFPMilRAKSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQA 507
Cdd:PRK02106 384 ------------------------------AHVGPM--RSPSRGSVKLKSADPRAHPSILFNYMSTEQDWREFRDAIRLT 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 508 VSLLDMPAFKAI-------GAHLlekripncakykwKSSAYWACYARHFTFTIYHYSGTAKMGPrsDPSAVVDARLRVHG 580
Cdd:PRK02106 432 REIMAQPALDPYrgreispGADV-------------QTDEEIDAFVREHAETAYHPSCTCKMGT--DPMAVVDPEGRVHG 496
|
570 580 590
....*....|....*....|....*....|....*.
gi 18859995 581 IDKLRVVDASIMPYLISGHPNGPVYLIAEKAADMIK 616
Cdd:PRK02106 497 VEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIR 532
|
|
| betA |
TIGR01810 |
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied ... |
63-616 |
4.51e-113 |
|
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. This enzymatic system can be found in both gram-positive and gram-negative bacteria. As in Escherichia coli, Staphylococcus xylosus, and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 273814 [Multi-domain] Cd Length: 532 Bit Score: 348.79 E-value: 4.51e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 63 DFIVVGAGTAGCALAARLSENPRWRVLLLEAGGPEnYAMDIPI-----VAHLLQLGEINWKYKTEPSNSyclaMNNNRCN 137
Cdd:TIGR01810 1 DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGSD-YPWDLLIqmpaaLAYPAGNKRYNWIYETEPEPH----MNNRRVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 138 WPRGKVMGGSSVLNYMMYTRGNRRDYDRWAR-LGNPGWSYEEVLPYFKKYEGSVVpdADENLVGRNGPVKVSYSETRTRI 216
Cdd:TIGR01810 76 HARGKVLGGSSSINGMIYQRGNPMDYEKWAKpEGMESWDYADCLPYYKRLETTFG--GEKPYRGHDGPIKVRRGPADNPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 217 ADAFVGATQDAGLPRG-DYNGDKQIRVSYLQANIYNETRWSSNRAYLYPIKgKRRNLHVKKNALVTKILIDpqTKSAFGI 295
Cdd:TIGR01810 154 FQAFIEAGVEAGYNKTpDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAM-KRPNLEVQTRAFVTKINFE--GNRATGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 296 IVKMDGKMQKILARKEVILSAGAINTPQLLMLSGVGPAKHLREMGIKPLADL-AVGYNLQDHIAPAISFLCNVS-SLQTS 373
Cdd:TIGR01810 231 EFKKGGRKEHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRIHLpGVGENLQDHLEVYVQHACKQPvSLYPS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 374 --EMFRSEAMSDFLKGRGVLRIPGGVEAISFY-ALDDARNPDawadmelfvvgggLQTNLalrLALGIQSNIYETMfgel 450
Cdd:TIGR01810 311 lnWLKQPFIGAQWLFGRKGAGASNHFEGGGFVrSNDDVDYPN-------------IQYHF---LPVAIRYDGTKAP---- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 451 erqSANGFLIFPMILRAKSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQAVSLLDMPAFKAIGAHLLEKRiPN 530
Cdd:TIGR01810 371 ---KAHGFQVHVGPMYSNSRGHVKIKSKDPFEKPEIVFNYMSHEEDWREFREAIRVTREILKQKALDPYRGGEISPG-PE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 531 CakykwKSSAYWACYARHFTFTIYHYSGTAKMGPRSDPSAVVDARLRVHGIDKLRVVDASIMPYLISGHPNGPVYLIAEK 610
Cdd:TIGR01810 447 V-----QTDEEIDEFVRRHGETALHPCGTCKMGPASDEMSVVDPETRVHGMEGLRVVDASIMPRITNGNLNAPVIMMGEK 521
|
....*.
gi 18859995 611 AADMIK 616
Cdd:TIGR01810 522 AADIIR 527
|
|
| GMC_oxred_N |
pfam00732 |
GMC oxidoreductase; This family of proteins bind FAD as a cofactor. |
132-356 |
2.19e-46 |
|
GMC oxidoreductase; This family of proteins bind FAD as a cofactor.
Pssm-ID: 366272 [Multi-domain] Cd Length: 218 Bit Score: 162.84 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 132 NNNRCNWPRGKVMGGSSVLNYMMYTRGNRRDYDRWARL-GNPGWSYEEVLPYFKKYEG--SVVPDADENLvGRNgpvkvs 208
Cdd:pfam00732 15 NGRRMILPAGSTVGGGSSVNWSACIRTPAAVLDEWASEfGLEGWGYDDYLPYMDKVEGplGVTTKGIEES-PLN------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 209 ysetrtriaDAFVGATQDAGLP----RGDYNGDKQIRVSYLQANiyNETRWSSNRAYLYPikGKRRNLHVKKNALVTKIL 284
Cdd:pfam00732 88 ---------QALLKAAEELGYPveavPRNSNGCHYCGFCGLGCP--TGAKQSTARTWLRP--ALERNLRILTGAKAEKII 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859995 285 IDPQTKSAFGI-IVKMDGK-MQKILARKEVILSAGAINTPQLLMLSGVGPAKHlremgikpladlAVGYNLQDH 356
Cdd:pfam00732 155 ILGRGGRAVGVeARDGGGGiKRLITAAKEVVVAAGALNTPPLLLRSGLGKNPH------------PVGKNLQLH 216
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
59-619 |
0e+00 |
|
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441878 [Multi-domain] Cd Length: 531 Bit Score: 544.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 59 TTKYDFIVVGAGTAGCALAARLSENPRWRVLLLEAGGPENYAM-DIPI-VAHLLQLGEINWKYKTEPSnsycLAMNNNRC 136
Cdd:COG2303 2 LEEYDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRDDDPLiRMPAgYAKLLGNPRYDWRYETEPQ----PGLNGRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 137 NWPRGKVMGGSSVLNYMMYTRGNRRDYDRWARLGNPGWSYEEVLPYFKKYEGSVVPDADenLVGRNGPVKVSYSETRTRI 216
Cdd:COG2303 78 YWPRGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGADA--YHGRSGPLPVSDPPLPNPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 217 ADAFVGATQDAGLPRG-DYNGDKQIRVSYLQANIYNETRWSSNRAYLYPIKgKRRNLHVKKNALVTKILIDpqTKSAFGI 295
Cdd:COG2303 156 SDAFIEAAEELGIPRAdDFNGGACEGCGFCQVTCRNGARWSAARAYLPPAL-KRPNLTVRTGALVTRILFD--GGRATGV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 296 IVKMDGKMQKILARKEVILSAGAINTPQLLMLSGVGPAKHLREMGIKPLADL-AVGYNLQDHIAPAISFLCN-VSSLQTS 373
Cdd:COG2303 233 EYRDDGEEHTVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLpGVGRNLQDHLEVSVVFRFKePVTLNKS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 374 EMFRSEAMSDFLKGRGVLRIpGGVEAISFYALDDARnpdAWADMELFVVGGGlqtnlalrlalgiqsniYETMFGELERQ 453
Cdd:COG2303 313 LRKARIGLQYLLTRSGPLTS-NVAEAGGFFRSDPGL---ERPDLQFHFLPLG-----------------LTPRWGKKALH 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 454 SANGFLIFPMILRAKSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQAVSLLDMPAFKAIgahllekRIPNCAK 533
Cdd:COG2303 372 DGHGFTAHVEQLRPESRGRVTLDSADPLGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPY-------RGEEILP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 534 YKWKSSAYWACYARHFTFTIYHYSGTAKMGPrsDPSAVVDARLRVHGIDKLRVVDASIMPYLISGHPNGPVYLIAEKAAD 613
Cdd:COG2303 445 GPDVQSDEELAFIRARAYTIYHPVGTCRMGT--DPDSVVDPRLRVHGVENLRVVDASVMPTITSGNTNAPTIMLAEKAAD 522
|
....*.
gi 18859995 614 MIKEDH 619
Cdd:COG2303 523 MILGDY 528
|
|
| PRK02106 |
PRK02106 |
choline dehydrogenase; Validated |
59-616 |
3.06e-141 |
|
choline dehydrogenase; Validated
Pssm-ID: 235000 [Multi-domain] Cd Length: 560 Bit Score: 422.32 E-value: 3.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 59 TTKYDFIVVGAGTAGCALAARLSENPRWRVLLLEAGGPeNYAMDIPI-----VAHLLQLGEINWKYKTEPSNSyclaMNN 133
Cdd:PRK02106 3 TMEYDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGP-DYRWDFFIqmpaaLAFPLQGKRYNWAYETEPEPH----MNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 134 NRCNWPRGKVMGGSSVLNYMMYTRGNRRDYDRWARL-GNPGWSYEEVLPYFKKYEGSVVPDADenLVGRNGPVKVSYSET 212
Cdd:PRK02106 78 RRMECPRGKVLGGSSSINGMVYIRGNAMDYDNWAELpGLEGWSYADCLPYFKKAETRDGGEDD--YRGGDGPLSVTRGKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 213 RTR-IADAFVGATQDAGLPR-GDYNGDKQIRVSYLQANIYNETRWSSNRAYLYPIKgKRRNLHVKKNALVTKILIDPqtK 290
Cdd:PRK02106 156 GTNpLFQAFVEAGVQAGYPRtDDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPAL-KRPNLTIVTHALTDRILFEG--K 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 291 SAFGIIVKMDGKMQKILARKEVILSAGAINTPQLLMLSGVGPAKHLREMGIKPLADLA-VGYNLQDHIAPAISFLCN--V 367
Cdd:PRK02106 233 RAVGVEYERGGGRETARARREVILSAGAINSPQLLQLSGIGPAEHLKELGIPVVHDLPgVGENLQDHLEVYIQYECKqpV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 368 SSLQTSEMFRSEAM-------------SDFLKGRGVLRIPGGVE--AISFYAL-----DDARNPdawadmelfVVGGGLQ 427
Cdd:PRK02106 313 SLYPALKWWNKPKIgaewlftgtglgaSNHFEAGGFIRSRAGVDwpNIQYHFLpvairYDGSNA---------VKGHGFQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 428 tnlalrlalgiqsniyetmfgelerqsangFLIFPMilRAKSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQA 507
Cdd:PRK02106 384 ------------------------------AHVGPM--RSPSRGSVKLKSADPRAHPSILFNYMSTEQDWREFRDAIRLT 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 508 VSLLDMPAFKAI-------GAHLlekripncakykwKSSAYWACYARHFTFTIYHYSGTAKMGPrsDPSAVVDARLRVHG 580
Cdd:PRK02106 432 REIMAQPALDPYrgreispGADV-------------QTDEEIDAFVREHAETAYHPSCTCKMGT--DPMAVVDPEGRVHG 496
|
570 580 590
....*....|....*....|....*....|....*.
gi 18859995 581 IDKLRVVDASIMPYLISGHPNGPVYLIAEKAADMIK 616
Cdd:PRK02106 497 VEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIR 532
|
|
| betA |
TIGR01810 |
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied ... |
63-616 |
4.51e-113 |
|
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. This enzymatic system can be found in both gram-positive and gram-negative bacteria. As in Escherichia coli, Staphylococcus xylosus, and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 273814 [Multi-domain] Cd Length: 532 Bit Score: 348.79 E-value: 4.51e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 63 DFIVVGAGTAGCALAARLSENPRWRVLLLEAGGPEnYAMDIPI-----VAHLLQLGEINWKYKTEPSNSyclaMNNNRCN 137
Cdd:TIGR01810 1 DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGSD-YPWDLLIqmpaaLAYPAGNKRYNWIYETEPEPH----MNNRRVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 138 WPRGKVMGGSSVLNYMMYTRGNRRDYDRWAR-LGNPGWSYEEVLPYFKKYEGSVVpdADENLVGRNGPVKVSYSETRTRI 216
Cdd:TIGR01810 76 HARGKVLGGSSSINGMIYQRGNPMDYEKWAKpEGMESWDYADCLPYYKRLETTFG--GEKPYRGHDGPIKVRRGPADNPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 217 ADAFVGATQDAGLPRG-DYNGDKQIRVSYLQANIYNETRWSSNRAYLYPIKgKRRNLHVKKNALVTKILIDpqTKSAFGI 295
Cdd:TIGR01810 154 FQAFIEAGVEAGYNKTpDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAM-KRPNLEVQTRAFVTKINFE--GNRATGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 296 IVKMDGKMQKILARKEVILSAGAINTPQLLMLSGVGPAKHLREMGIKPLADL-AVGYNLQDHIAPAISFLCNVS-SLQTS 373
Cdd:TIGR01810 231 EFKKGGRKEHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRIHLpGVGENLQDHLEVYVQHACKQPvSLYPS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 374 --EMFRSEAMSDFLKGRGVLRIPGGVEAISFY-ALDDARNPDawadmelfvvgggLQTNLalrLALGIQSNIYETMfgel 450
Cdd:TIGR01810 311 lnWLKQPFIGAQWLFGRKGAGASNHFEGGGFVrSNDDVDYPN-------------IQYHF---LPVAIRYDGTKAP---- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 451 erqSANGFLIFPMILRAKSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQAVSLLDMPAFKAIGAHLLEKRiPN 530
Cdd:TIGR01810 371 ---KAHGFQVHVGPMYSNSRGHVKIKSKDPFEKPEIVFNYMSHEEDWREFREAIRVTREILKQKALDPYRGGEISPG-PE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 531 CakykwKSSAYWACYARHFTFTIYHYSGTAKMGPRSDPSAVVDARLRVHGIDKLRVVDASIMPYLISGHPNGPVYLIAEK 610
Cdd:TIGR01810 447 V-----QTDEEIDEFVRRHGETALHPCGTCKMGPASDEMSVVDPETRVHGMEGLRVVDASIMPRITNGNLNAPVIMMGEK 521
|
....*.
gi 18859995 611 AADMIK 616
Cdd:TIGR01810 522 AADIIR 527
|
|
| Rv0697 |
TIGR03970 |
dehydrogenase, Rv0697 family; This model describes a set of dehydrogenases belonging to the ... |
63-615 |
3.02e-80 |
|
dehydrogenase, Rv0697 family; This model describes a set of dehydrogenases belonging to the glucose-methanol-choline oxidoreductase (GMC oxidoreductase) family. Members of the present family are restricted to Actinobacterial genome contexts containing also members of families TIGR03962 and TIGR03969 (the mycofactocin system), and are proposed to be uniform in function.
Pssm-ID: 274888 [Multi-domain] Cd Length: 487 Bit Score: 261.67 E-value: 3.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 63 DFIVVGAGTAGCALAARLSENPRWRVLLLEAGGPENYAMDIP-IVAHLLQL-----GEINWKYKTE----PSNSYCLAmn 132
Cdd:TIGR03970 2 DVLIVGAGSAGSVLAARLSEDPSCTVTVLEAGPGYRDPSRLPaQLTDGLRLpigpaSPVVWRYGVEltdgPRRASQIV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 133 nnrcnwpRGKVMGGSSVLNYMMYTRGNRRDYDRWARlgnPGWSYEEVLPYFKKYEGSVvpDADENLVGRNGPVKVSYSET 212
Cdd:TIGR03970 80 -------RGRVLGGSGAVNGGYFCRALPADFDAWPI---PGWSWDDVLPHFRAIETDL--DFDGPLHGTAGPIPVRRTAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 213 RTRIADAFVGATQDAGLP-RGDYNGDKQIRVSYLQA---NIYNETRWSSNRAYLYPiKGKRRNLHVKKNALVTKILIDPQ 288
Cdd:TIGR03970 148 LDGISAAFVAAALGAGFGwIADLNGSGPGLPGGVGAvplNVDGGRRVSTAVAYLLP-ALKRPNLTVEADTRVVRILFSGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 289 TksAFGIIVKMDGKMQKILARKeVILSAGAINTPQLLMLSGVGPAKHLREMGIKPLADLAVGYNLQDHiaPAISFLCNVS 368
Cdd:TIGR03970 227 R--AVGVEVLGDGGPRTLRADR-VVLCAGAVESAHLLLLSGIGPAEQLRAAGIAVVLDLPVGSDFVDH--PEWVLPYRWR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 369 SlqtsemfrseamsdflkgrgVLRIPGGVEAISfYALDDarnpdawADMEL------FV--VGGGLQTNLALRLALgiqs 440
Cdd:TIGR03970 302 P--------------------THDRPPTSPVLE-TVLNT-------ADIEIrpytagFTalVPGSPRDDPHLGVAL---- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 441 niyetmfgelerqsangflifpmiLRAKSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQAVSLLdmpafkaiG 520
Cdd:TIGR03970 350 ------------------------MRPHSRGRIRLASADPADPPRIEHRYDSSAADRAALRAGAALAHELL--------G 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 521 AHLLEKRIPNCAKykwKSSAYWacyARHFTFTIYHYSGTAKMGPRSDPSAVVDARLRVHGIDKLRVVDASIMPYLISGHP 600
Cdd:TIGR03970 398 SPELGPLLEPAVR---EGEASW---VLARLATSQHLCGSCRMGGRDDPGAVVDARCRVRGVEGLWVVDGSILPVIPSRGP 471
|
570
....*....|....*
gi 18859995 601 NGPVYLIAEKAADMI 615
Cdd:TIGR03970 472 HATAVMVAERAAEFL 486
|
|
| GMC_oxred_N |
pfam00732 |
GMC oxidoreductase; This family of proteins bind FAD as a cofactor. |
132-356 |
2.19e-46 |
|
GMC oxidoreductase; This family of proteins bind FAD as a cofactor.
Pssm-ID: 366272 [Multi-domain] Cd Length: 218 Bit Score: 162.84 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 132 NNNRCNWPRGKVMGGSSVLNYMMYTRGNRRDYDRWARL-GNPGWSYEEVLPYFKKYEG--SVVPDADENLvGRNgpvkvs 208
Cdd:pfam00732 15 NGRRMILPAGSTVGGGSSVNWSACIRTPAAVLDEWASEfGLEGWGYDDYLPYMDKVEGplGVTTKGIEES-PLN------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 209 ysetrtriaDAFVGATQDAGLP----RGDYNGDKQIRVSYLQANiyNETRWSSNRAYLYPikGKRRNLHVKKNALVTKIL 284
Cdd:pfam00732 88 ---------QALLKAAEELGYPveavPRNSNGCHYCGFCGLGCP--TGAKQSTARTWLRP--ALERNLRILTGAKAEKII 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859995 285 IDPQTKSAFGI-IVKMDGK-MQKILARKEVILSAGAINTPQLLMLSGVGPAKHlremgikpladlAVGYNLQDH 356
Cdd:pfam00732 155 ILGRGGRAVGVeARDGGGGiKRLITAAKEVVVAAGALNTPPLLLRSGLGKNPH------------PVGKNLQLH 216
|
|
| GMC_oxred_C |
pfam05199 |
GMC oxidoreductase; This domain found associated with pfam00732. |
468-611 |
3.72e-42 |
|
GMC oxidoreductase; This domain found associated with pfam00732.
Pssm-ID: 398739 [Multi-domain] Cd Length: 143 Bit Score: 148.70 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 468 KSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQAVSLLDMPAFkAIGAHLLEKRIPNCAKYKWKSSAYWACYAR 547
Cdd:pfam05199 2 RSRGRVTLSSSDPTGLPVIDPNYLSDPADLAALRAALRLARRILAAAGL-VLGVELTPGPVPEVSDAAVTSDDELLAYIR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859995 548 HFTFTIYHYSGTAKMGPRSDPSaVVDARLRVHGIDKLRVVDASIMPYLISGHPNGPVYLIAEKA 611
Cdd:pfam05199 81 AAASTSYHPMGTCRMGADPDDA-VVDPDLRVHGVDNLRVVDASVFPSSPSGNPTLTIYALAERA 143
|
|
| PLN02785 |
PLN02785 |
Protein HOTHEAD |
62-591 |
1.33e-29 |
|
Protein HOTHEAD
Pssm-ID: 215420 [Multi-domain] Cd Length: 587 Bit Score: 123.76 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 62 YDFIVVGAGTAGCALAARLSENprWRVLLLEAGGPENYAMDIPivahLLQLGEINWKYKTEPSNSYCLAMNNNRCNwPRG 141
Cdd:PLN02785 56 YDYIVVGGGTAGCPLAATLSQN--FSVLLLERGGVPFGNANVS----FLENFHIGLADTSPTSASQAFISTDGVIN-ARA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 142 KVMGGSSVLNYMMYTRGNRRDYDRwarlgnPGWsyeevlpyfkkyegsvvpdaDENLVGRngpvkvSYSETRTRIAD--- 218
Cdd:PLN02785 129 RVLGGGTCINAGFYSRASTRFIQK------AGW--------------------DAKLVNE------SYPWVERQIVHwpk 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 219 ------AFVGATQDAGL-PRGDYNGDkQIRVSYLQANIYNETRWSSNRAYLYPiKGKRRNLHVKKNALVTKILIDPQTKS 291
Cdd:PLN02785 177 vapwqaALRDSLLEVGVsPFNGFTYD-HVYGTKVGGTIFDEFGRRHTAAELLA-AGNPNKLRVLLHATVQKIVFDTSGKR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 292 --AFGIIVKMD--GKMQKILARK---EVILSAGAINTPQLLMLSGVGPAKHLREMGIK-PLADLAVGYNLQDHIAPAIsF 363
Cdd:PLN02785 255 prATGVIFKDEngNQHQAFLSNNkgsEIILSAGAIGSPQMLLLSGIGPKKELKKHKIPvVLHNEHVGKGMADNPMNSI-F 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 364 L-----CNVSSLQTSEMFRS----EAMSDFLKGRGVLRIPGGVEAISFYALD----DARNPDAwadmelfvvggglqtnl 430
Cdd:PLN02785 334 VpskapVEQSLIQTVGITKMgvyiEASSGFGQSPDSIHCHHGIMSAEIGQLStippKQRTPEA----------------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 431 alrlalgIQSNIYETMFgeLERQSANGFLIFPMILRAKSRGRIKLKSRNPEEHPRIYANYFANPYDMNITVRGIEQAVSL 510
Cdd:PLN02785 397 -------IQAYIHRKKN--LPHEAFNGGFILEKIAGPISTGHLSLINTNVDDNPSVTFNYFKHPQDLQRCVYGIRTIEKI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859995 511 LDMPAFKAI---GAHLLEKRIP-------NCAKYKWKSSAYWACYARHFTFTIYHYSGTAKMGprsdpsAVVDARLRVHG 580
Cdd:PLN02785 468 VKTNHFTNFtqcDKQTMEKVLNmsvkaniNLIPKHTNDTKSLEQFCKDTVITIWHYHGGCHVG------KVVDQNYKVLG 541
|
570
....*....|.
gi 18859995 581 IDKLRVVDASI 591
Cdd:PLN02785 542 VSRLRVIDGST 552
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
59-93 |
1.65e-05 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 47.45 E-value: 1.65e-05
10 20 30
....*....|....*....|....*....|....*
gi 18859995 59 TTKYDFIVVGAGTAGCALAARLSENPRWRVLLLEA 93
Cdd:COG0579 2 MEMYDVVIIGAGIVGLALARELSRYEDLKVLVLEK 36
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
60-96 |
1.18e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 44.90 E-value: 1.18e-04
10 20 30
....*....|....*....|....*....|....*..
gi 18859995 60 TKYDFIVVGAGTAGCALAARLSENpRWRVLLLEAGGP 96
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARR-GLDVTVLERGRP 36
|
|
| Lycopene_cycl |
pfam05834 |
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. ... |
63-99 |
1.42e-04 |
|
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. Carotenoids with cyclic end groups are essential components of the photosynthetic membranes in all plants, algae, and cyanobacteria. These lipid-soluble compounds protect against photo-oxidation, harvest light for photosynthesis, and dissipate excess light energy absorbed by the antenna pigments. The cyclization of lycopene (psi, psi-carotene) is a key branch point in the pathway of carotenoid biosynthesis. Two types of cyclic end groups are found in higher plant carotenoids: the beta and epsilon rings. Carotenoids with two beta rings are ubiquitous, and those with one beta and one epsilon ring are common; however, carotenoids with two epsilon rings are rare.
Pssm-ID: 310433 [Multi-domain] Cd Length: 380 Bit Score: 44.33 E-value: 1.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 18859995 63 DFIVVGAGTAGCALAARLSEN-PRWRVLLLEAG----GPENY 99
Cdd:pfam05834 1 DVVIIGAGPAGLSLAARLAAAkPGLSVVLIEPGpsllRPNNY 42
|
|
| PTZ00367 |
PTZ00367 |
squalene epoxidase; Provisional |
62-116 |
2.56e-04 |
|
squalene epoxidase; Provisional
Pssm-ID: 240384 [Multi-domain] Cd Length: 567 Bit Score: 44.07 E-value: 2.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 18859995 62 YDFIVVGAGTAGCALAARLSENPRwRVLLLE---AGGPENyamdipIVAHLLQLGEIN 116
Cdd:PTZ00367 34 YDVIIVGGSIAGPVLAKALSKQGR-KVLMLErdlFSKPDR------IVGELLQPGGVN 84
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
62-92 |
3.70e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 42.69 E-value: 3.70e-04
10 20 30
....*....|....*....|....*....|.
gi 18859995 62 YDFIVVGAGTAGCALAARLSENPRwRVLLLE 92
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGL-RVLLLE 30
|
|
| carotene-cycl |
TIGR01790 |
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ... |
63-99 |
5.88e-04 |
|
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.
Pssm-ID: 130850 [Multi-domain] Cd Length: 388 Bit Score: 42.42 E-value: 5.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 18859995 63 DFIVVGAGTAGCALAARLSEnPRWRVLLLEA----GGPENY 99
Cdd:TIGR01790 1 DLAVIGGGPAGLAIALELAR-PGLRVQLIEPhppiPGNHTY 40
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
59-92 |
3.33e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 40.19 E-value: 3.33e-03
10 20 30
....*....|....*....|....*....|....
gi 18859995 59 TTKYDFIVVGAGTAGCALAARLSENPrWRVLLLE 92
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLG-MKVALIE 35
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
63-94 |
4.77e-03 |
|
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: 39.69 E-value: 4.77e-03
10 20 30
....*....|....*....|....*....|..
gi 18859995 63 DFIVVGAGTAGCALAARLSENPrWRVLLLEAG 94
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRG-LSVTLLERG 31
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
63-93 |
7.27e-03 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 39.44 E-value: 7.27e-03
10 20 30
....*....|....*....|....*....|..
gi 18859995 63 DFIVVGAGTAGCALAARLSEnpR-WRVLLLEA 93
Cdd:PRK01747 262 DAAIIGGGIAGAALALALAR--RgWQVTLYEA 291
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
66-94 |
8.91e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 35.20 E-value: 8.91e-03
10 20
....*....|....*....|....*....
gi 18859995 66 VVGAGTAGCALAARLSENPRwRVLLLEAG 94
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGF-RVLVLEKR 28
|
|
|