|
Name |
Accession |
Description |
Interval |
E-value |
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
64-792 |
0e+00 |
|
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130164 [Multi-domain] Cd Length: 715 Bit Score: 1253.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 64 RSELKHAKRIVVKLGSAVVTRGDECgLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALHS 143
Cdd:TIGR01092 1 RAFLKDVKRIVVKVGTAVVTRGDGR-LALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILVNSSFADLQKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 144 GqnqlkemaiPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTND 223
Cdd:TIGR01092 80 Q---------PELDGKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNEND 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 224 AVVPPAEPNSDLQGVisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQ-SVTFGTKSRVG 302
Cdd:TIGR01092 151 AVSTRAAPYSDSQGI--FWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKEKHQgEITFGTKSRLG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 303 MGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFSEVKPAGPTVEQQGE-----MARSGGRMLAT 377
Cdd:TIGR01092 229 RGGMTAKVKAAVWAAYGGTPVIIASGTAPKN----ITKVVEGKKVGTLFHEDAHLWPTVEQTGErdmavAARESSRMLQA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 378 LEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGRVLRRT 456
Cdd:TIGR01092 305 LSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAgYAASLVARLSMSPSKISSLAISLRQLAAM-EDPIGRVLKRT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 457 RIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLVNT 536
Cdd:TIGR01092 384 RIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHVGKKLIGLVTS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 537 REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACNALETL 616
Cdd:TIGR01092 464 REEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTK-IPVLGHADGICHVYVDKSASVDMAKRIVRDAKCDYPAACNAMETL 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 617 LIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDV 696
Cdd:TIGR01092 543 LVHKDLLRNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKSFRTEYSSLACTVEIVDDVYDAIDHIHKHGSAHTDC 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 697 IVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSdfSEHG 776
Cdd:TIGR01092 623 IVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLRGKGQVVS--GDHG 700
|
730
....*....|....*.
gi 1020738491 777 sLKYLHENLPIPQRNT 792
Cdd:TIGR01092 701 -LVYTHKDLPIPQRNT 715
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
64-787 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 825.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 64 RSELKHAKRIVVKLGSAVVTRGDecG-LALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQaLH 142
Cdd:PLN02418 9 RAFLRDVKRVVIKVGTAVVTRDD--GrLALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRRLVNSSFAD-LQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 143 SGQNQLKEMAipvlearaCAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTN 222
Cdd:PLN02418 86 KPQMELDGKA--------CAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 223 DAVVPPAEPNSDLQGVISvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYP-GDQQSVTFGTKSRV 301
Cdd:PLN02418 158 DAVSTRRAPYEDSSGIFW--DNDSLAALLALELKADLLILLSDVEGLYTGPPSDPSSKLIHTYIKeKHQDEITFGEKSRV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 302 GMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFseVKPAG---PTVEQQG-EMA---RSGGRM 374
Cdd:PLN02418 236 GRGGMTAKVKAAVNAASAGIPVVITSGYALDN----IRKVLRGERVGTLF--HQDAHlwaPSKEVGArEMAvaaRESSRK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 375 LATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAE-GRLAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGRVL 453
Cdd:PLN02418 310 LQALSSEERKKILLDVADALEANEELIKAENELDVAAAQeAGYEKSLVSRLTLKPGKIASLAASIRQLADM-EDPIGRVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 454 RRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQL 533
Cdd:PLN02418 389 KRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIPKTVGGKLIGL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 534 VNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACNAL 613
Cdd:PLN02418 469 VTSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTK-IPVLGHADGICHVYVDKSADMDMAKRIVVDAKTDYPAACNAM 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 614 ETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSpsEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSH 693
Cdd:PLN02418 548 ETLLVHKDLVQNGGLNDLLVALRSAGVTLYGGPRASKLLNIP--EAQSFHHEYSSLACTVEIVDDVHAAIDHIHRHGSAH 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 694 TDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSdfS 773
Cdd:PLN02418 626 TDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGNGQVVD--G 703
|
730
....*....|....
gi 1020738491 774 EHGSLkYLHENLPI 787
Cdd:PLN02418 704 DKGVV-YTHKDLPL 716
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
362-764 |
0e+00 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 596.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 362 EQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQ 440
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAgLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 441 IAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQE 520
Cdd:cd07079 81 VAALP-DPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 521 ALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTR 597
Cdd:cd07079 160 ALEEAGLpEDAVQLIPDtdREAVQELLKLDDYIDLIIPRGGAGLIRFVVENAT-IPVIKHGDGNCHVYVDESADLEMAVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 598 LVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFS-PSEVKSLRTEYGDLELCIEVV 676
Cdd:cd07079 239 IVVNAKTQRPSVCNALETLLVHRDIAEEFL-PKLAEALREAGVELRGDEETLAILPGAkPATEEDWGTEYLDLILAVKVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 677 DNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLL 756
Cdd:cd07079 318 DSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELT 397
|
....*...
gi 1020738491 757 TTKWLLRG 764
Cdd:cd07079 398 TYKYIVRG 405
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
63-352 |
0e+00 |
|
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia.
Pssm-ID: 239789 [Multi-domain] Cd Length: 284 Bit Score: 549.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 63 HRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALH 142
Cdd:cd04256 1 SRSELKHAKRIVVKLGSAVVTREDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRHEILLSSSMRQTLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 143 SgqNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTN 222
Cdd:cd04256 81 S--GQLKDMPQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 223 DAVVPPAEPNSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTKSRVG 302
Cdd:cd04256 159 DAVSPPPEPDEDLQGVISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGSDDAKLIHTFYPGDQQSITFGTKSRVG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1020738491 303 MGGMEAKVKAALWALQGGTSVVIANGTHpkvsGHVITDIVEGKKVGTFFS 352
Cdd:cd04256 239 TGGMEAKVKAALWALQGGTSVVITNGMA----GDVITKILEGKKVGTFFT 284
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
360-770 |
1.89e-174 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 507.68 E-value: 1.89e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 360 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 438
Cdd:PRK00197 5 YLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANgLSAAMLDRLLLTEARIEGIAEGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 439 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 518
Cdd:PRK00197 85 RQVAALP-DPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 519 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 595
Cdd:PRK00197 164 QEALEEAGLpADAVQLVETtdRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENAT-VPVIEHGDGICHIYVDESADLDKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 596 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTF-SPSEVKSLRTEYGDLELCIE 674
Cdd:PRK00197 243 LKIVLNAKTQRPSVCNALETLLVHEAIAEEFL-PKLAEALAEAGVELRGDEAALALLPDvVPATEEDWDTEYLDLILAVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 675 VVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEG 754
Cdd:PRK00197 322 VVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEE 401
|
410
....*....|....*.
gi 1020738491 755 LLTTKWLLRGKDHVVS 770
Cdd:PRK00197 402 LTTYKYIVLGDGQIRA 417
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
366-763 |
1.72e-172 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 502.14 E-value: 1.72e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 366 EMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAAPLLKRLSLSTSKLNSLAIGLRQIAASs 445
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 446 qdsVGRVLRRTRIAkNLELEQVTVPIGVLLVIFESRPDCL-PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSI 524
Cdd:cd07077 80 ---VGHIQDVLLPD-NGETYVRAFPIGVTMHILPSTNPLSgITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 525 HGVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRLVRDS 602
Cdd:cd07077 156 HGPKILVLYVPHPsdELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 603 KCEYPAACNALETLLIHRDLLrTPLFDQIIDMLRVEQVKIHAGPKFASYLTFsPSEVKSLRTEYGDLELCIEVVDN---V 679
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVL-DPLYEEFKLKLVVEGLKVPQETKPLSKETT-PSFDDEALESMTPLECQFRVLDVisaV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 680 QDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARG-PVGLEGLLTT 758
Cdd:cd07077 313 ENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRPL 392
|
....*
gi 1020738491 759 KWLLR 763
Cdd:cd07077 393 KRLVR 397
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
360-770 |
5.99e-172 |
|
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl phosphate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 439785 Cd Length: 414 Bit Score: 501.46 E-value: 5.99e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 360 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 438
Cdd:COG0014 2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENgLSEALLDRLKLTEERIEAMAEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 439 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 518
Cdd:COG0014 82 RQVAALP-DPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 519 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 595
Cdd:COG0014 161 QEALEEAGLpEDAVQLVPTtdREAVGELLTLDGYIDVIIPRGGAGLIRRVVENAT-VPVIEHGDGNCHVYVDASADLEMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 596 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLtfspSEVK-----SLRTEYGDLE 670
Cdd:COG0014 240 VDIVVNAKTQRPGVCNALETLLVHRDIAAEFL-PRLAAALAEAGVELRGDERTRAIL----PDVKpateeDWGTEYLDLI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 671 LCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPV 750
Cdd:COG0014 315 LAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPM 394
|
410 420
....*....|....*....|
gi 1020738491 751 GLEGLLTTKWLLRGKDHVVS 770
Cdd:COG0014 395 GLEELTTYKYVVRGDGQIRP 414
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
368-759 |
8.46e-128 |
|
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion protein delta l-pyrroline-5-carboxylate synthetase that includes a gamma-glutamyl phosphate reductase region as described by this model. Alternate name: glutamate-5-semialdehyde dehydrogenase. The prosite motif begins at residue 332 of the seed alignment although not all of the members of the family exactly obey the motif. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 161862 Cd Length: 398 Bit Score: 387.22 E-value: 8.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 368 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAaSSQ 446
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENgLADALLDRLLLTEGRLKGIADGVKDVI-ELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 447 DSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHG 526
Cdd:TIGR00407 80 DPVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 527 V-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSK 603
Cdd:TIGR00407 160 LpVGAVQLIETpsRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTST-IPVLGHGDGICHIYLDESADLIKAIKVIVNAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 604 CEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFSPSEV-----KSLRTEYGDLELCIEVVDN 678
Cdd:TIGR00407 239 TQRPSTCNAIETLLVNKAIAREFL-PVLENQLLEKGVTIHADAYALKLLELGPATEaivckTDFDKEFLSLDLSVKIVES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 679 VQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTT 758
Cdd:TIGR00407 318 LEAAIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSY 397
|
.
gi 1020738491 759 K 759
Cdd:TIGR00407 398 K 398
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
72-351 |
9.81e-101 |
|
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.
Pssm-ID: 239775 [Multi-domain] Cd Length: 251 Bit Score: 311.30 E-value: 9.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 72 RIVVKLGSAVVTRGDEcGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRheillsqsvrqalhsgqnqLKEM 151
Cdd:cd04242 1 RIVVKVGSSLLTDEDG-GLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLG-------------------LEKR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 152 AIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAep 231
Cdd:cd04242 61 PKTLPEKQALAAVGQSLLMALYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEE-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 232 nsdlqgvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQ--QSVTFGTKSRVGMGGMEA 308
Cdd:cd04242 139 -------IRFGDNDRLSALVAGLVNADLLILLSDVDGLYDKNPRENpDAKLIPEVEEITDeiEAMAGGSGSSVGTGGMRT 211
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1020738491 309 KVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFF 351
Cdd:cd04242 212 KLKAARIATEAGIPVVIANGRKP----DVLLDILAGEAVGTLF 250
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
64-351 |
7.58e-74 |
|
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440033 [Multi-domain] Cd Length: 371 Bit Score: 244.95 E-value: 7.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 64 RSELKHAKRIVVKLGSAVVTRGDEcGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRheillsqsvrqaLHS 143
Cdd:COG0263 1 REALAKARRIVVKIGSSLLTDEGG-GLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLG------------LPK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 144 GQNQLKEmaipvleARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTND 223
Cdd:COG0263 68 RPKTLPE-------KQAAAAVGQGLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINEND 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 224 AVVpPAEpnsdlqgvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDI---FYPGDQQSVTfGTKS 299
Cdd:COG0263 141 TVA-TDE--------IRFGDNDRLAALVANLVEADLLVLLTDVDGLYDADPRKDpDAKLIPEveeITPEIEAMAG-GAGS 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1020738491 300 RVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFF 351
Cdd:COG0263 211 GLGTGGMATKLEAARIATRAGIPTVIASGREP----NVLLRILAGERVGTLF 258
|
|
| PRK12314 |
PRK12314 |
gamma-glutamyl kinase; Provisional |
63-355 |
1.30e-66 |
|
gamma-glutamyl kinase; Provisional
Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 222.04 E-value: 1.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 63 HRSELKHAKRIVVKLGSAVVTrGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLR-HEILLSQSVRQAL 141
Cdd:PRK12314 2 MRRQLENAKRIVIKVGSSTLS-YENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKlDKRPTSLAEKQAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 142 hsgqnqlkemaipvlearacAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNT 221
Cdd:PRK12314 81 --------------------AAVGQPELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 222 NDAVVppaepNSDLQGVISvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPP-GSDDAKLIDIFYPGDQQ--SVTFGTK 298
Cdd:PRK12314 141 NDAVA-----TDEIDTKFG--DNDRLSAIVAKLVKADLLIILSDIDGLYDKNPrINPDAKLRSEVTEITEEilALAGGAG 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1020738491 299 SRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFFSEVK 355
Cdd:PRK12314 214 SKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP----SDILDFLEGESIGTLFAPKK 266
|
|
| proB |
TIGR01027 |
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
71-351 |
2.59e-59 |
|
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 162163 [Multi-domain] Cd Length: 363 Bit Score: 205.62 E-value: 2.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 71 KRIVVKLGSAVVTrGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLrheillsqsvrqalhsGQNQL-K 149
Cdd:TIGR01027 1 QRIVVKVGSSSLT-GSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEAL----------------GLPERpK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 150 EMAipvlEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVpPA 229
Cdd:TIGR01027 64 TLA----EKQALAAVGQVRLMQLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTVA-TE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 230 EpnsdlqgvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGD--QQSVTFGTKSRVGMGGM 306
Cdd:TIGR01027 139 E--------IKFGDNDTLSALVAILVGADLLVLLTDVDGLYDADPRTNpDAKLIPVVEEITdlLLGVAGDSGSSVGTGGM 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1020738491 307 EAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGTFF 351
Cdd:TIGR01027 211 RTKLQAADLATRAGVPVIIASGSKPE----KIADALEGAPVGTLF 251
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
368-763 |
2.65e-59 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 205.54 E-value: 2.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 368 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEeaegrlaapllKRLSLSTSKLNSLAIGLRQIAASSQD 447
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETG-----------KPIEEALGEVARAIDTFRYAAGLADK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 448 SVGrvLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCL--PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSih 525
Cdd:cd06534 72 LGG--PELPSPDPGGEAYVRREPLGVVGVITPWNFPLLlaAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 526 gVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHMYVDSEASVDKVTRLVRD 601
Cdd:cd06534 148 -PPGVVNVVPGGgdEVGAALLSHPR-VDKISFTGSTAVGKAIMKAAAEnlKPVTLELGGKSPVIVDEDADLDAAVEGAVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 602 SKCEY-PAACNALETLLIHRDLlrtplFDQIIDMLRveQVKIHAGPKFasyltfspsevKSLRTEYGDLELCIEVVDNVQ 680
Cdd:cd06534 226 GAFFNaGQICTAASRLLVHESI-----YDEFVEKLV--TVLVDVDPDM-----------PIAQEEIFGPVLPVIRFKDEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 681 DAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYR-FGlgaevGISTSRIHAR-GPVGLEGLLTT 758
Cdd:cd06534 288 EAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEApFG-----GVKNSGIGREgGPYGLEEYTRT 362
|
....*
gi 1020738491 759 KWLLR 763
Cdd:cd06534 363 KTVVI 367
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
74-351 |
1.13e-50 |
|
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.
Pssm-ID: 239033 [Multi-domain] Cd Length: 248 Bit Score: 178.02 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 74 VVKLGSAVVTRGDecglalgRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLsqsvrqalhsgqNQLKEMAI 153
Cdd:cd02115 1 VIKFGGSSVSSEE-------RLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELL------------GYARGLRI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 154 PVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHD------EQKRRNLNGTLHELLRMNIVPIVNTNDAVVP 227
Cdd:cd02115 62 TDRETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFASpnqghvGKITKVSTDRLKSLLENGILPILSGFGGTDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 228 PAEpnsdlqGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPP-GSDDAKLIDIFYPGDQQSVTfgtksrvGMGGM 306
Cdd:cd02115 142 KET------GTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPrKVPDAKLLSELTYEEAAELA-------YAGAM 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1020738491 307 EAKVKAALWALQGGTSVVIANGTHPKVSghvitDIVEGKKVGTFF 351
Cdd:cd02115 209 VLKPKAADPAARAGIPVRIANTENPGAL-----ALFTPDGGGTLI 248
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
71-327 |
6.66e-39 |
|
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.
Pssm-ID: 395565 [Multi-domain] Cd Length: 232 Bit Score: 144.05 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 71 KRIVVKLGSAVVTRGDecglalgRLASIVEQVSVLQNQGREMMLVTSGavafGKQrLRHEILLSQSVRQALHSGQNQLKE 150
Cdd:pfam00696 1 KRVVIKLGGSSLTDKE-------RLKRLADEIAALLEEGRKLVVVHGG----GAF-ADGLLALLGLSPRFARLTDAETLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 151 maipVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVvppae 230
Cdd:pfam00696 69 ----VATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGI----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 231 pnsDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVtfgTKSRVGMGGMEAK 309
Cdd:pfam00696 140 ---DPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVpDAKLIPEISYDELLEL---LASGLATGGMKVK 213
|
250
....*....|....*....
gi 1020738491 310 VKAALWALQ-GGTSVVIAN 327
Cdd:pfam00696 214 LPAALEAARrGGIPVVIVN 232
|
|
| PTZ00489 |
PTZ00489 |
glutamate 5-kinase; Provisional |
67-330 |
9.04e-23 |
|
glutamate 5-kinase; Provisional
Pssm-ID: 240438 [Multi-domain] Cd Length: 264 Bit Score: 98.55 E-value: 9.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 67 LKHAKRIVVKLGSAVVTRGDEcgLALGRLASIVEQVSVLQNQgREMMLVTSGAVAFGKQrlrheillsqsvrqalhsgQN 146
Cdd:PTZ00489 5 LKSVKRIVVKVGSSILVDNQE--IAAHRIEALCRFIADLQTK-YEVILVTSGAVAAGYT-------------------KK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 147 QLKEMAIPvlEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVV 226
Cdd:PTZ00489 63 EMDKSYVP--NKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 227 ppaepnsdLQGVIsVKDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSPPGSDDAKLIDIFYPGDQQSVTFGT--KSRVGM 303
Cdd:PTZ00489 141 --------LHELV-FGDNDRLSALVAHHFKADLLVILSDIDGYYtENPRTSTDAKIRSVVHELSPDDLVAEAtpNNRFAT 211
|
250 260
....*....|....*....|....*..
gi 1020738491 304 GGMEAKVKAALWALQGGTSVVIANGTH 330
Cdd:PTZ00489 212 GGIVTKLQAAQFLLERGGKMYLSSGFH 238
|
|
| AAK_FomA-like |
cd04241 |
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
72-349 |
1.20e-11 |
|
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239774 [Multi-domain] Cd Length: 252 Bit Score: 65.75 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 72 RIVVKLGSAVVTRGDECGLA-LGRLASIVEQVSvlQNQGREMMLVtSGAVAFG----KQRLRHEILLSQS------VRQA 140
Cdd:cd04241 1 MIILKLGGSVITDKDRPETIrEENLERIARELA--EAIDEKLVLV-HGGGSFGhpkaKEYGLPDGDGSFSaegvaeTHEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 141 LHSgqnqlkemaipvLEARACAAAGQSGLMAlyeamftqYSICAAQILVTNldfhdeqKRRNLNG---TLHELLRMNIVP 217
Cdd:cd04241 78 MLE------------LNSIVVDALLEAGVPA--------VSVPPSSFFVTE-------NGRIVSFdleVIKELLDRGFVP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 218 IVNtNDAVVppaepnsDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGsdDAKLIDIFYPGDQQSVTFGT 297
Cdd:cd04241 131 VLH-GDVVL-------DEGGGITILSGDDIVVELAKALKPERVIFLTDVDGVYDKPPP--DAKLIPEIDVGSLEDILAAL 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1020738491 298 KSRVG--MGGMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGT 349
Cdd:cd04241 201 GSAGTdvTGGMAGKIEELLELARRGIEVYIFNGDKPE----NLYRALLGNFIGT 250
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
207-328 |
4.11e-09 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 58.37 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 207 LHELLRMNIVPIVNtndavvPPAEpnsDLQGV-ISVkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLIDIF 285
Cdd:PRK14058 142 LKLLLKAGYLPVVA------PPAL---SEEGEpLNV-DGDRAAAAIAGALKAEALVLLSDVPGLLRDPP--DEGSLIERI 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1020738491 286 YPGDqqsvtFGTKSRVGMGGMEAKVKAALWALQGG-TSVVIANG 328
Cdd:PRK14058 210 TPEE-----AEELSKAAGGGMKKKVLMAAEAVEGGvGRVIIADA 248
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
207-349 |
1.64e-08 |
|
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239771 [Multi-domain] Cd Length: 256 Bit Score: 56.36 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 207 LHELLRMNIVPIVNtndavvPPAepnSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLIDIFY 286
Cdd:cd04238 131 LETLLEAGYIPVIA------PIA---VDEDGETYNVNADTAAGAIAAALKAEKLILLTDVPGVLD-----DPGSLISELT 196
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738491 287 PGD-QQSVTFGTKSrvgmGGMEAKVKAALWALQGG-TSVVIANGTHPkvsgHVITDIVEGKK-VGT 349
Cdd:cd04238 197 PKEaEELIEDGVIS----GGMIPKVEAALEALEGGvRKVHIIDGRVP----HSLLLELFTDEgIGT 254
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
230-357 |
1.15e-07 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 54.45 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 230 EPNSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSppGSDDAKLIDIFYPGDQQSVTFGTksrvgmGGMEA 308
Cdd:PRK12354 191 DADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYlDW--GKPTQRAIAQATPDELRELGFAA------GSMGP 262
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1020738491 309 KVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGKKvGTFFSEVKPA 357
Cdd:PRK12354 263 KVEAACeFVRATGKIAGIG-------SLEDIQAILAGEA-GTRISPETAG 304
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
367-642 |
1.20e-07 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 54.91 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 367 MARSGGRMLAtlePEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRlslstsklns 433
Cdd:cd07078 9 AAFKAWAALP---PAERAAILRKLADLLEERREELaaLETleTGKPIEEALGevaraadtfRYYAGLARR---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 434 laIGLRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPDCLP--QVAAlAIASGNGLLLKGGKEA 507
Cdd:cd07078 76 --LHGEVIPSPDPGELAIVRRE--------------PLGVVGAItpwnF---PLLLAawKLAP-ALAAGNTVVLKPSELT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 508 AHSNRILHLLTQEALSIHGVkeaVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHM 584
Cdd:cd07078 136 PLTALLLAELLAEAGLPPGV---LNVVTgDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEnlKRVTLELGGKSPL 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1020738491 585 YVDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 642
Cdd:cd07078 213 IVFDDADLDAAVKGAVFGAFGNAGqVCTAASRLLVHES-----IYDEFVERLveRVKALKV 268
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
226-349 |
5.62e-07 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 52.31 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 226 VPPAEPNSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSpPGSDDAKLIDIFYPgdQQSVTFGTKSRVGMGG 305
Cdd:PRK12454 196 IPVIEEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYLN-YGKPDQKPLDKVTV--EEAKKYYEEGHFKAGS 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1020738491 306 MEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGkKVGT 349
Cdd:PRK12454 273 MGPKILAAIrFVENGGKRAIIA-------SLEKAVEALEG-KTGT 309
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
361-642 |
1.11e-06 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 52.05 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 361 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 427
Cdd:cd07094 23 AEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEfakiIACEGGKPIKDARVevdraidtlRLAAEEAERIRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 428 TSKLNSLAIGLRQIAASSQDSVGRVLRRTriAKNLELEQVTVPIGvllvifesrPdclpqvaalAIASGNGLLLKGGKEA 507
Cdd:cd07094 103 EIPLDATQGSDNRLAWTIREPVGVVLAIT--PFNFPLNLVAHKLA---------P---------AIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 508 AHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMY 585
Cdd:cd07094 163 PLSALELAKILVEA----GVpEGVLQVVTgEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 586 VDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 642
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGqVCISVQRIYVHEE-----LYDEFIEAFvaAVKKLKV 293
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
376-760 |
2.57e-06 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 50.61 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 376 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSlstsklnslaiGlrQIA 442
Cdd:pfam00171 46 RKTPAAERAAILRKAADLLEERKDELaeLETleNGKPLAEARGevdraidvlRYYAGLARRLD-----------G--ETL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 443 ASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI--FESrPDCLP--QVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 518
Cdd:pfam00171 113 PSDPGRLAYTRRE--------------PLGVVGAItpWNF-PLLLPawKIAP-ALAAGNTVVLKPSELTPLTALLLAELF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 519 QEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHSegicHMYVDSE 589
Cdd:pfam00171 177 EEA----GLpAGVLNVVTGsgAEVGEALVE-HPDVRKVSFTGSTAVGRHIAEAAaqNLKRVTlelgGKN----PLIVLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 590 ASVDKVTRLVRDSKCEYP-AACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI--------HAGP--------KFAS 650
Cdd:pfam00171 248 ADLDAAVEAAVFGAFGNAgQVCTATSRLLVHES-----IYDEFVEKLveAAKKLKVgdpldpdtDMGPliskaqleRVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 651 Y-----------------------------LTFSPSEVKSLRTE-YGDLeLCIEVVDNVQDAIDHIH--KYGssHTDVIV 698
Cdd:pfam00171 323 YvedakeegaklltggeagldngyfveptvLANVTPDMRIAQEEiFGPV-LSVIRFKDEEEAIEIANdtEYG--LAAGVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738491 699 TEDENTAEFFLQHVDSACVFWNASTRFS-DGYRFGlgaevGISTSRI-HARGPVGLEGLLTTKW 760
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDaDGLPFG-----GFKQSGFgREGGPYGLEEYTEVKT 458
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
243-332 |
3.71e-06 |
|
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239784 [Multi-domain] Cd Length: 257 Bit Score: 49.29 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 243 DNDSLAARLAVEMKTDLLIVLSDVEGLFdsppgsDDAKLIDIFYPGDQQSVtfgtKSRVGmGGMEAKVKAALWALQGGTS 322
Cdd:cd04251 165 DGDRAAAAIAAALKAERLILLTDVEGLY------LDGRVIERITVSDAESL----LEKAG-GGMKRKLLAAAEAVEGGVR 233
|
90
....*....|.
gi 1020738491 323 -VVIANGTHPK 332
Cdd:cd04251 234 eVVIGDARADS 244
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
245-349 |
3.90e-06 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 49.34 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 245 DSLAARLAVEMKTDLLIVLSDVEGLFDSpPGS-------DDA-KLIdifypgDQQSVTfgtksrvgmGGMEAKVKAALWA 316
Cdd:PRK00942 184 DTAAGAIAAALGAEKLILLTDVPGVLDD-KGQliseltaSEAeELI------EDGVIT---------GGMIPKVEAALDA 247
|
90 100 110
....*....|....*....|....*....|....*
gi 1020738491 317 LQGG-TSVVIANGTHPkvsgH-VITDIVEGKKVGT 349
Cdd:PRK00942 248 ARGGvRSVHIIDGRVP----HaLLLELFTDEGIGT 278
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
245-328 |
5.26e-06 |
|
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239783 [Multi-domain] Cd Length: 279 Bit Score: 49.04 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 245 DSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLIDIFYPGD-QQSVTFGTKSrvgmGGMEAKVKAALWALQGGT-S 322
Cdd:cd04250 180 DTAAGAIAAALKAEKLILLTDVAGVLDDPN--DPGSLISEISLKEaEELIADGIIS----GGMIPKVEACIEALEGGVkA 253
|
....*.
gi 1020738491 323 VVIANG 328
Cdd:cd04250 254 AHIIDG 259
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
368-642 |
5.81e-06 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 49.74 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 368 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLA----NKKDLEEAEG---------RLAAPLLKRLSlstsklnsl 434
Cdd:COG1012 52 ARAAFPAWAATPPAERAAILLRAADLLEERREELAALltleTGKPLAEARGevdraadflRYYAGEARRLY--------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 435 aiGlRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPdcLPQVA---ALAIASGNGLLLKGGKEA 507
Cdd:COG1012 123 --G-ETIPSDAPGTRAYVRRE--------------PLGVVGAItpwnF---P--LALAAwklAPALAAGNTVVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 508 AHSNRILHLLTQEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHS 578
Cdd:COG1012 181 PLSALLLAELLEEA----GLpAGVLNVVTGdgSEVGAALVA-HPDVDKISFTGSTAVGRRIAAAAaeNLKRVTlelgGKN 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1020738491 579 egicHMYVDSEASVDKVTRLVRDSKCEYpA--ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 642
Cdd:COG1012 256 ----PAIVLDDADLDAAVEAAVRGAFGN-AgqRCTAASRLLVHES-----IYDEFVERLvaAAKALKV 313
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
245-331 |
3.67e-05 |
|
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440314 [Multi-domain] Cd Length: 283 Bit Score: 46.18 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 245 DSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLIDIFYPGDQQSVTfgtKSRVGMGGMEAKVKAALWALQGGT-SV 323
Cdd:COG0548 186 DTVAGAIAAALKAEKLILLTDVPGVLD-----DPGSLISELTAAEAEELI---ADGVISGGMIPKLEAALDAVRGGVkRV 257
|
....*...
gi 1020738491 324 VIANGTHP 331
Cdd:COG0548 258 HIIDGRVP 265
|
|
| AAK_NAGK-NC |
cd04249 |
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ... |
207-349 |
4.93e-05 |
|
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239782 [Multi-domain] Cd Length: 252 Bit Score: 45.87 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 207 LHELLRMNIVPIVNTNDAvvppaepnsDLQGVISVKDNDSLAARLAVEMKTDLlIVLSDVEGLFDSppgsdDAKLIDIFy 286
Cdd:cd04249 129 LNDLLKAGFLPIISSIGA---------DDQGQLMNVNADQAATAIAQLLNADL-VLLSDVSGVLDA-----DKQLISEL- 192
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738491 287 pgDQQSVTFGTKSRVGMGGMEAKVKAALWALQG-GTSVVIANGTHPKvsghVITDIVEGKKVGT 349
Cdd:cd04249 193 --NAKQAAELIEQGVITDGMIVKVNAALDAAQSlRRGIDIASWQYPE----QLTALLAGEPVGT 250
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|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
376-576 |
5.04e-04 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 43.33 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 376 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSLSTSKLNslaiglrqIA 442
Cdd:cd07082 56 PTMPLEERIDCLHKFADLLKENKEEVanLLMweIGKTLKDALKevdrtidyiRDTIEELKRLDGDSLPGD--------WF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 443 ASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI-------FESrpdclpqVAALAIA--SGNGLLLKGGKEAAhsnrI 513
Cdd:cd07082 128 PGTKGKIAQVRR--------------EPLGVVLAIgpfnyplNLT-------VSKLIPAliMGNTVVFKPATQGV----L 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738491 514 LHLLTQEALSIHGV-KEAVQLVNTR-EEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP-VMG 576
Cdd:cd07082 183 LGIPLAEAFHDAGFpKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRlVLE 248
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| AAK_UMPK-PyrH-Pf |
cd04253 |
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
245-350 |
5.75e-04 |
|
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239786 [Multi-domain] Cd Length: 221 Bit Score: 42.24 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 245 DSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVTFGTKSRVGmggmeAKVKAALWALQ----G 319
Cdd:cd04253 118 DAVAALLAERLGADLLINATNVDGVYSKDPRKDpDAKKFDRLSADELIDIVGKSSWKAG-----SNEPFDPLAAKiierS 192
|
90 100 110
....*....|....*....|....*....|.
gi 1020738491 320 GTSVVIANGTHPKvsghVITDIVEGKKVGTF 350
Cdd:cd04253 193 GIKTIVVDGRDPE----NLERALKGEFVGTI 219
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| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
361-569 |
9.40e-04 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 42.58 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 361 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 427
Cdd:cd07149 23 VEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEfartIALEAGKPIKDARKevdraietlRLSAEEAKRLAGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 428 TSKLNSlaiglrqiAASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI--FEsrpDCLPQVA---ALAIASGNGLLLK 502
Cdd:cd07149 103 TIPFDA--------SPGGEGRIGFTIR--------------EPIGVVAAItpFN---FPLNLVAhkvGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 503 GGKEAAHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVED-LCRlDKMIDLIIPRGSSQLVRDIQKAA 569
Cdd:cd07149 158 PASQTPLSALKLAELLLEA----GLpKGALNVVTgSGETVGDaLVT-DPRVRMISFTGSPAVGEAIARKA 222
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| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
348-641 |
1.26e-03 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 42.23 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 348 GTFFSEVKPAGP-TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEGRLAapllk 422
Cdd:cd07147 9 GEVVARVALAGPdDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEElaetIVLEAGKPIKDARGEVA----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 423 RlslstsklnslAIGLRQIAA-SSQDSVGRVLRRTRIAKNLELEQVT--VPIGVLLVIfesRPDCLP--QVA---ALAIA 494
Cdd:cd07147 84 R-----------AIDTFRIAAeEATRIYGEVLPLDISARGEGRQGLVrrFPIGPVSAI---TPFNFPlnLVAhkvAPAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 495 SGNGLLLKggkeAAHSNRILHLLTQEALSIHGV-KEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP 573
Cdd:cd07147 150 AGCPFVLK----PASRTPLSALILGEVLAETGLpKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1020738491 574 VMGHSEGICHMYVDSEASVDK-VTRLVRDSKCEYPAACNALETLLIHRDllrtpLFDQIIDMLrVEQVK 641
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFaAQRIIFGAFYQAGQSCISVQRVLVHRS-----VYDEFKSRL-VARVK 288
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
226-349 |
1.72e-03 |
|
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239768 Cd Length: 308 Bit Score: 41.34 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 226 VPPAEPNSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGL---FDSPpgsDDAKLIDIFYpgdQQSVTFGTKSRVG 302
Cdd:cd04235 192 IPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVyinFGKP---NQKALEQVTV---EELEKYIEEGQFA 265
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1020738491 303 MGGMEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGKKvGT 349
Cdd:cd04235 266 PGSMGPKVEAAIrFVESGGKKAIIT-------SLENAEAALEGKA-GT 305
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|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
376-648 |
1.76e-03 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 41.55 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 376 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLeeaegrlaapllkRLSLSTSKLNSLAIGLRQIAASSQDsvgrvlrr 455
Cdd:PTZ00381 24 KTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDL-------------GRHPFETKMTEVLLTVAEIEHLLKH-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 456 trIAKNLELEQVTV--------------PIGVLLVIFE-SRP--DCLPQVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 518
Cdd:PTZ00381 83 --LDEYLKPEKVDTvgvfgpgksyiipePLGVVLVIGAwNYPlnLTLIPLAG-AIAAGNTVVLKPSELSPHTSKLMAKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738491 519 QEALSihgvKEAVQLVNT-REEVEDLCRLDkmIDLIIPRGSSQLVRDIQKAA--KGIPVMGHSEGICHMYVDSEASVDKV 595
Cdd:PTZ00381 160 TKYLD----PSYVRVIEGgVEVTTELLKEP--FDHIFFTGSPRVGKLVMQAAaeNLTPCTLELGGKSPVIVDKSCNLKVA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1020738491 596 TRLVRDSKC-EYPAACNALETLLIHRDLLrtplfDQIIDMLRvEQVKIHAGPKF 648
Cdd:PTZ00381 234 ARRIAWGKFlNAGQTCVAPDYVLVHRSIK-----DKFIEALK-EAIKEFFGEDP 281
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