|
Name |
Accession |
Description |
Interval |
E-value |
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
64-794 |
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: 1253.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 64 RSELKHAKRIVVKLGSAVVTRGDECgLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALHS 143
Cdd:TIGR01092 1 RAFLKDVKRIVVKVGTAVVTRGDGR-LALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILVNSSFADLQKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 144 GqnqlkemaiPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTND 223
Cdd:TIGR01092 80 Q---------PELDGKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNEND 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 224 AVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQ-SVTFGTKSR 302
Cdd:TIGR01092 151 AVSTRAAPYSDSQGI----FWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKEKHQgEITFGTKSR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 303 VGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFSEVKPAGPTVEQQGE-----MARSGGRML 377
Cdd:TIGR01092 227 LGRGGMTAKVKAAVWAAYGGTPVIIASGTAPKN----ITKVVEGKKVGTLFHEDAHLWPTVEQTGErdmavAARESSRML 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 378 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGRVLR 456
Cdd:TIGR01092 303 QALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAgYAASLVARLSMSPSKISSLAISLRQLAAM-EDPIGRVLK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 457 RTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLV 536
Cdd:TIGR01092 382 RTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHVGKKLIGLV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 537 NTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACNALE 616
Cdd:TIGR01092 462 TSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTK-IPVLGHADGICHVYVDKSASVDMAKRIVRDAKCDYPAACNAME 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 617 TLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHT 696
Cdd:TIGR01092 541 TLLVHKDLLRNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKSFRTEYSSLACTVEIVDDVYDAIDHIHKHGSAHT 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 697 DVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSdfSE 776
Cdd:TIGR01092 621 DCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLRGKGQVVS--GD 698
|
730
....*....|....*...
gi 1020738530 777 HGsLKYLHENLPIPQRNT 794
Cdd:TIGR01092 699 HG-LVYTHKDLPIPQRNT 715
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
64-789 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 822.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 64 RSELKHAKRIVVKLGSAVVTRGDecG-LALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQaLH 142
Cdd:PLN02418 9 RAFLRDVKRVVIKVGTAVVTRDD--GrLALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRRLVNSSFAD-LQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 143 SGQNQLKEMAipvlearaCAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTN 222
Cdd:PLN02418 86 KPQMELDGKA--------CAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 223 DAVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYP-GDQQSVTFGTKS 301
Cdd:PLN02418 158 DAVSTRRAPYEDSSGI----FWDNDSLAALLALELKADLLILLSDVEGLYTGPPSDPSSKLIHTYIKeKHQDEITFGEKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 302 RVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFseVKPAG---PTVEQQG-EMA---RSGG 374
Cdd:PLN02418 234 RVGRGGMTAKVKAAVNAASAGIPVVITSGYALDN----IRKVLRGERVGTLF--HQDAHlwaPSKEVGArEMAvaaRESS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 375 RMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAE-GRLAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGR 453
Cdd:PLN02418 308 RKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQeAGYEKSLVSRLTLKPGKIASLAASIRQLADM-EDPIGR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 454 VLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAV 533
Cdd:PLN02418 387 VLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIPKTVGGKLI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 534 QLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACN 613
Cdd:PLN02418 467 GLVTSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTK-IPVLGHADGICHVYVDKSADMDMAKRIVVDAKTDYPAACN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 614 ALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSpsEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGS 693
Cdd:PLN02418 546 AMETLLVHKDLVQNGGLNDLLVALRSAGVTLYGGPRASKLLNIP--EAQSFHHEYSSLACTVEIVDDVHAAIDHIHRHGS 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 694 SHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSd 773
Cdd:PLN02418 624 AHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGNGQVVD- 702
|
730
....*....|....*.
gi 1020738530 774 fSEHGSLkYLHENLPI 789
Cdd:PLN02418 703 -GDKGVV-YTHKDLPL 716
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
364-766 |
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 1020738530 364 EQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQ 442
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAgLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 443 IAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQE 522
Cdd:cd07079 81 VAALP-DPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 523 ALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTR 599
Cdd:cd07079 160 ALEEAGLpEDAVQLIPDtdREAVQELLKLDDYIDLIIPRGGAGLIRFVVENAT-IPVIKHGDGNCHVYVDESADLEMAVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 600 LVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFS-PSEVKSLRTEYGDLELCIEVV 678
Cdd:cd07079 239 IVVNAKTQRPSVCNALETLLVHRDIAEEFL-PKLAEALREAGVELRGDEETLAILPGAkPATEEDWGTEYLDLILAVKVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 679 DNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLL 758
Cdd:cd07079 318 DSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELT 397
|
....*...
gi 1020738530 759 TTKWLLRG 766
Cdd:cd07079 398 TYKYIVRG 405
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
63-354 |
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: 543.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 63 HRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALH 142
Cdd:cd04256 1 SRSELKHAKRIVVKLGSAVVTREDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRHEILLSSSMRQTLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 143 SgqNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTN 222
Cdd:cd04256 81 S--GQLKDMPQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 223 DAVVPPAEPNSDLQGVnvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTKSR 302
Cdd:cd04256 159 DAVSPPPEPDEDLQGV--ISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGSDDAKLIHTFYPGDQQSITFGTKSR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1020738530 303 VGMGGMEAKVKAALWALQGGTSVVIANGTHpkvsGHVITDIVEGKKVGTFFS 354
Cdd:cd04256 237 VGTGGMEAKVKAALWALQGGTSVVITNGMA----GDVITKILEGKKVGTFFT 284
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
362-772 |
2.06e-174 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 507.68 E-value: 2.06e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 362 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 440
Cdd:PRK00197 5 YLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANgLSAAMLDRLLLTEARIEGIAEGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 441 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:PRK00197 85 RQVAALP-DPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 521 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 597
Cdd:PRK00197 164 QEALEEAGLpADAVQLVETtdRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENAT-VPVIEHGDGICHIYVDESADLDKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 598 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTF-SPSEVKSLRTEYGDLELCIE 676
Cdd:PRK00197 243 LKIVLNAKTQRPSVCNALETLLVHEAIAEEFL-PKLAEALAEAGVELRGDEAALALLPDvVPATEEDWDTEYLDLILAVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 677 VVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEG 756
Cdd:PRK00197 322 VVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEE 401
|
410
....*....|....*.
gi 1020738530 757 LLTTKWLLRGKDHVVS 772
Cdd:PRK00197 402 LTTYKYIVLGDGQIRA 417
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
368-765 |
1.95e-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: 1.95e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 368 EMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAAPLLKRLSLSTSKLNSLAIGLRQIAASs 447
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 448 qdsVGRVLRRTRIAkNLELEQVTVPIGVLLVIFESRPDCL-PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSI 526
Cdd:cd07077 80 ---VGHIQDVLLPD-NGETYVRAFPIGVTMHILPSTNPLSgITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 527 HGVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRLVRDS 604
Cdd:cd07077 156 HGPKILVLYVPHPsdELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 605 KCEYPAACNALETLLIHRDLLrTPLFDQIIDMLRVEQVKIHAGPKFASYLTFsPSEVKSLRTEYGDLELCIEVVDN---V 681
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVL-DPLYEEFKLKLVVEGLKVPQETKPLSKETT-PSFDDEALESMTPLECQFRVLDVisaV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 682 QDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARG-PVGLEGLLTT 760
Cdd:cd07077 313 ENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRPL 392
|
....*
gi 1020738530 761 KWLLR 765
Cdd:cd07077 393 KRLVR 397
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
362-772 |
6.37e-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: 6.37e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 362 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 440
Cdd:COG0014 2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENgLSEALLDRLKLTEERIEAMAEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 441 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:COG0014 82 RQVAALP-DPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 521 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 597
Cdd:COG0014 161 QEALEEAGLpEDAVQLVPTtdREAVGELLTLDGYIDVIIPRGGAGLIRRVVENAT-VPVIEHGDGNCHVYVDASADLEMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 598 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLtfspSEVK-----SLRTEYGDLE 672
Cdd:COG0014 240 VDIVVNAKTQRPGVCNALETLLVHRDIAAEFL-PRLAAALAEAGVELRGDERTRAIL----PDVKpateeDWGTEYLDLI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 673 LCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPV 752
Cdd:COG0014 315 LAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPM 394
|
410 420
....*....|....*....|
gi 1020738530 753 GLEGLLTTKWLLRGKDHVVS 772
Cdd:COG0014 395 GLEELTTYKYVVRGDGQIRP 414
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
370-761 |
9.03e-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: 9.03e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 370 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAaSSQ 448
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENgLADALLDRLLLTEGRLKGIADGVKDVI-ELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 449 DSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHG 528
Cdd:TIGR00407 80 DPVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 529 V-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSK 605
Cdd:TIGR00407 160 LpVGAVQLIETpsRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTST-IPVLGHGDGICHIYLDESADLIKAIKVIVNAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 606 CEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFSPSEV-----KSLRTEYGDLELCIEVVDN 680
Cdd:TIGR00407 239 TQRPSTCNAIETLLVNKAIAREFL-PVLENQLLEKGVTIHADAYALKLLELGPATEaivckTDFDKEFLSLDLSVKIVES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 681 VQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTT 760
Cdd:TIGR00407 318 LEAAIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSY 397
|
.
gi 1020738530 761 K 761
Cdd:TIGR00407 398 K 398
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
72-353 |
9.22e-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: 311.68 E-value: 9.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 72 RIVVKLGSAVVTRGDEcGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRheillsqsvrqalhsgqnqLKEM 151
Cdd:cd04242 1 RIVVKVGSSLLTDEDG-GLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLG-------------------LEKR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 152 AIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVppaep 231
Cdd:cd04242 61 PKTLPEKQALAAVGQSLLMALYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVA----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 232 nsdlqgVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQ--QSVTFGTKSRVGMGGM 308
Cdd:cd04242 136 ------TEEIRFGDNDRLSALVAGLVNADLLILLSDVDGLYDKNPRENpDAKLIPEVEEITDeiEAMAGGSGSSVGTGGM 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1020738530 309 EAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFF 353
Cdd:cd04242 210 RTKLKAARIATEAGIPVVIANGRKP----DVLLDILAGEAVGTLF 250
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
64-353 |
2.43e-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: 246.49 E-value: 2.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 64 RSELKHAKRIVVKLGSAVVTRGDEcGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRheillsqsvrqaLHS 143
Cdd:COG0263 1 REALAKARRIVVKIGSSLLTDEGG-GLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLG------------LPK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 144 GQNQLKEmaipvleARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTND 223
Cdd:COG0263 68 RPKTLPE-------KQAAAAVGQGLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINEND 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 224 AVVppaepnsdlqgVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDI---FYPGDQQSVTfGT 299
Cdd:COG0263 141 TVA-----------TDEIRFGDNDRLAALVANLVEADLLVLLTDVDGLYDADPRKDpDAKLIPEveeITPEIEAMAG-GA 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1020738530 300 KSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFF 353
Cdd:COG0263 209 GSGLGTGGMATKLEAARIATRAGIPTVIASGREP----NVLLRILAGERVGTLF 258
|
|
| PRK12314 |
PRK12314 |
gamma-glutamyl kinase; Provisional |
63-357 |
3.28e-66 |
|
gamma-glutamyl kinase; Provisional
Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 220.88 E-value: 3.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 63 HRSELKHAKRIVVKLGSAVVTrGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLR-HEILLSQSVRQAL 141
Cdd:PRK12314 2 MRRQLENAKRIVIKVGSSTLS-YENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKlDKRPTSLAEKQAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 142 hsgqnqlkemaipvlearacAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNT 221
Cdd:PRK12314 81 --------------------AAVGQPELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 222 NDAVVppaepnsdlqgVNVISVK--DNDSLAARLAVEMKTDLLIVLSDVEGLFDSPP-GSDDAKLIDIFYPGDQQ--SVT 296
Cdd:PRK12314 141 NDAVA-----------TDEIDTKfgDNDRLSAIVAKLVKADLLIILSDIDGLYDKNPrINPDAKLRSEVTEITEEilALA 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1020738530 297 FGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFFSEVK 357
Cdd:PRK12314 210 GGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP----SDILDFLEGESIGTLFAPKK 266
|
|
| proB |
TIGR01027 |
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
71-353 |
3.06e-60 |
|
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: 207.93 E-value: 3.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 71 KRIVVKLGSAVVTrGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLrheillsqsvrqalhsGQNQL-K 149
Cdd:TIGR01027 1 QRIVVKVGSSSLT-GSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEAL----------------GLPERpK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 150 EMAipvlEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVvppa 229
Cdd:TIGR01027 64 TLA----EKQALAAVGQVRLMQLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTV---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 230 epnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGD--QQSVTFGTKSRVGMG 306
Cdd:TIGR01027 136 -------ATEEIKFGDNDTLSALVAILVGADLLVLLTDVDGLYDADPRTNpDAKLIPVVEEITdlLLGVAGDSGSSVGTG 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1020738530 307 GMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGTFF 353
Cdd:TIGR01027 209 GMRTKLQAADLATRAGVPVIIASGSKPE----KIADALEGAPVGTLF 251
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
370-765 |
2.79e-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: 2.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 370 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEeaegrlaapllKRLSLSTSKLNSLAIGLRQIAASSQD 449
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETG-----------KPIEEALGEVARAIDTFRYAAGLADK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 450 SVGrvLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCL--PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSih 527
Cdd:cd06534 72 LGG--PELPSPDPGGEAYVRREPLGVVGVITPWNFPLLlaAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 528 gVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHMYVDSEASVDKVTRLVRD 603
Cdd:cd06534 148 -PPGVVNVVPGGgdEVGAALLSHPR-VDKISFTGSTAVGKAIMKAAAEnlKPVTLELGGKSPVIVDEDADLDAAVEGAVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 604 SKCEY-PAACNALETLLIHRDLlrtplFDQIIDMLRveQVKIHAGPKFasyltfspsevKSLRTEYGDLELCIEVVDNVQ 682
Cdd:cd06534 226 GAFFNaGQICTAASRLLVHESI-----YDEFVEKLV--TVLVDVDPDM-----------PIAQEEIFGPVLPVIRFKDEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 683 DAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYR-FGlgaevGISTSRIHAR-GPVGLEGLLTT 760
Cdd:cd06534 288 EAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEApFG-----GVKNSGIGREgGPYGLEEYTRT 362
|
....*
gi 1020738530 761 KWLLR 765
Cdd:cd06534 363 KTVVI 367
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
74-353 |
2.11e-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: 177.25 E-value: 2.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 74 VVKLGSAVVTRGDecglalgRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLsqsvrqalhsgqNQLKEMAI 153
Cdd:cd02115 1 VIKFGGSSVSSEE-------RLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELL------------GYARGLRI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 154 PVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHD------EQKRRNLNGTLHELLRMNIVPIVNTNDAVVP 227
Cdd:cd02115 62 TDRETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFASpnqghvGKITKVSTDRLKSLLENGILPILSGFGGTDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 228 PaepnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPP-GSDDAKLIDIFYPGDQQSVTfgtksrvGMG 306
Cdd:cd02115 142 K--------ETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPrKVPDAKLLSELTYEEAAELA-------YAG 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1020738530 307 GMEAKVKAALWALQGGTSVVIANGTHPKVSghvitDIVEGKKVGTFF 353
Cdd:cd02115 207 AMVLKPKAADPAARAGIPVRIANTENPGAL-----ALFTPDGGGTLI 248
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
71-329 |
8.73e-38 |
|
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: 140.96 E-value: 8.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 71 KRIVVKLGSAVVTRGDecglalgRLASIVEQVSVLQNQGREMMLVTSGavafGKQrLRHEILLSQSVRQALHSGQNQLKE 150
Cdd:pfam00696 1 KRVVIKLGGSSLTDKE-------RLKRLADEIAALLEEGRKLVVVHGG----GAF-ADGLLALLGLSPRFARLTDAETLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 151 maipVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAE 230
Cdd:pfam00696 69 ----VATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 231 pnsdlqgvnvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVtfgTKSRVGMGGME 309
Cdd:pfam00696 145 ----------LGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVpDAKLIPEISYDELLEL---LASGLATGGMK 211
|
250 260
....*....|....*....|.
gi 1020738530 310 AKVKAALWALQ-GGTSVVIAN 329
Cdd:pfam00696 212 VKLPAALEAARrGGIPVVIVN 232
|
|
| PTZ00489 |
PTZ00489 |
glutamate 5-kinase; Provisional |
67-332 |
4.49e-23 |
|
glutamate 5-kinase; Provisional
Pssm-ID: 240438 [Multi-domain] Cd Length: 264 Bit Score: 99.70 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 67 LKHAKRIVVKLGSAVVTRGDEcgLALGRLASIVEQVSVLQNQgREMMLVTSGAVAFGKQrlrheillsqsvrqalhsgQN 146
Cdd:PTZ00489 5 LKSVKRIVVKVGSSILVDNQE--IAAHRIEALCRFIADLQTK-YEVILVTSGAVAAGYT-------------------KK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 147 QLKEMAIPvlEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVv 226
Cdd:PTZ00489 63 EMDKSYVP--NKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDAT- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 227 ppaepnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSPPGSDDAKLIDIFYPGDQQSVTFGT--KSRV 303
Cdd:PTZ00489 140 ----------ALHELVFGDNDRLSALVAHHFKADLLVILSDIDGYYtENPRTSTDAKIRSVVHELSPDDLVAEAtpNNRF 209
|
250 260
....*....|....*....|....*....
gi 1020738530 304 GMGGMEAKVKAALWALQGGTSVVIANGTH 332
Cdd:PTZ00489 210 ATGGIVTKLQAAQFLLERGGKMYLSSGFH 238
|
|
| AAK_FomA-like |
cd04241 |
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
72-351 |
3.72e-12 |
|
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: 67.29 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 72 RIVVKLGSAVVTRGDECGLA-LGRLASIVEQVSvlQNQGREMMLVtSGAVAFG----KQRLRHEILLSQS------VRQA 140
Cdd:cd04241 1 MIILKLGGSVITDKDRPETIrEENLERIARELA--EAIDEKLVLV-HGGGSFGhpkaKEYGLPDGDGSFSaegvaeTHEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 141 LHSgqnqlkemaipvLEARACAAAGQSGLMAlyeamftqYSICAAQILVTNldfhdeqKRRNLNG---TLHELLRMNIVP 217
Cdd:cd04241 78 MLE------------LNSIVVDALLEAGVPA--------VSVPPSSFFVTE-------NGRIVSFdleVIKELLDRGFVP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 218 IVNtNDAVVppaepnSDLQGVNVISvkdNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGsdDAKLIDIFYPGDQQSVTF 297
Cdd:cd04241 131 VLH-GDVVL------DEGGGITILS---GDDIVVELAKALKPERVIFLTDVDGVYDKPPP--DAKLIPEIDVGSLEDILA 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738530 298 GTKSRVG--MGGMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGT 351
Cdd:cd04241 199 ALGSAGTdvTGGMAGKIEELLELARRGIEVYIFNGDKPE----NLYRALLGNFIGT 250
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
207-351 |
3.41e-10 |
|
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: 61.37 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 207 LHELLRMNIVPivntndaVVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLIDI 286
Cdd:cd04238 131 LETLLEAGYIP-------VIAPIAVDEDGETYNV----NADTAAGAIAAALKAEKLILLTDVPGVLD-----DPGSLISE 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1020738530 287 FYPGD-QQSVTFGTKSrvgmGGMEAKVKAALWALQGG-TSVVIANGTHPkvsgHVITDIVEGKK-VGT 351
Cdd:cd04238 195 LTPKEaEELIEDGVIS----GGMIPKVEAALEALEGGvRKVHIIDGRVP----HSLLLELFTDEgIGT 254
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
207-330 |
2.03e-09 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 59.14 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 207 LHELLRMNIVPIVNtndavvPPAEpnsDLQG--VNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLI 284
Cdd:PRK14058 142 LKLLLKAGYLPVVA------PPAL---SEEGepLNV----DGDRAAAAIAGALKAEALVLLSDVPGLLRDPP--DEGSLI 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1020738530 285 DIFYPGDqqsvtFGTKSRVGMGGMEAKVKAALWALQGG-TSVVIANG 330
Cdd:PRK14058 207 ERITPEE-----AEELSKAAGGGMKKKVLMAAEAVEGGvGRVIIADA 248
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
207-330 |
9.47e-08 |
|
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: 54.43 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 207 LHELLRMNIVPivntndaVVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLIDI 286
Cdd:cd04250 151 LETLLEAGYIP-------VIAPVGVGEDGETYNI----NADTAAGAIAAALKAEKLILLTDVAGVLDDPN--DPGSLISE 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1020738530 287 FYPGD-QQSVTFGTKSrvgmGGMEAKVKAALWALQGGT-SVVIANG 330
Cdd:cd04250 218 ISLKEaEELIADGIIS----GGMIPKVEACIEALEGGVkAAHIIDG 259
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
369-644 |
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 1020738530 369 MARSGGRMLAtlePEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRlslstsklns 435
Cdd:cd07078 9 AAFKAWAALP---PAERAAILRKLADLLEERREELaaLETleTGKPIEEALGevaraadtfRYYAGLARR---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 436 laIGLRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPDCLP--QVAAlAIASGNGLLLKGGKEA 509
Cdd:cd07078 76 --LHGEVIPSPDPGELAIVRRE--------------PLGVVGAItpwnF---PLLLAawKLAP-ALAAGNTVVLKPSELT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 510 AHSNRILHLLTQEALSIHGVkeaVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHM 586
Cdd:cd07078 136 PLTALLLAELLAEAGLPPGV---LNVVTgDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEnlKRVTLELGGKSPL 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1020738530 587 YVDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 644
Cdd:cd07078 213 IVFDDADLDAAVKGAVFGAFGNAGqVCTAASRLLVHES-----IYDEFVERLveRVKALKV 268
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
207-351 |
2.07e-07 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 53.19 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 207 LHELLRMNIVPivntndaVVPPAEPNSDLQGVNVisvkdN-DSLAARLAVEMKTDLLIVLSDVEGLFDSpPGS------- 278
Cdd:PRK00942 155 LEALLEAGYIP-------VISPIGVGEDGETYNI-----NaDTAAGAIAAALGAEKLILLTDVPGVLDD-KGQliselta 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738530 279 DDA-KLIdifypgDQQSVTfgtksrvgmGGMEAKVKAALWALQGG-TSVVIANGTHPkvsgH-VITDIVEGKKVGT 351
Cdd:PRK00942 222 SEAeELI------EDGVIT---------GGMIPKVEAALDAARGGvRSVHIIDGRVP----HaLLLELFTDEGIGT 278
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
363-644 |
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 1020738530 363 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 429
Cdd:cd07094 23 AEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEfakiIACEGGKPIKDARVevdraidtlRLAAEEAERIRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 430 TSKLNSLAIGLRQIAASSQDSVGRVLRRTriAKNLELEQVTVPIGvllvifesrPdclpqvaalAIASGNGLLLKGGKEA 509
Cdd:cd07094 103 EIPLDATQGSDNRLAWTIREPVGVVLAIT--PFNFPLNLVAHKLA---------P---------AIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 510 AHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMY 587
Cdd:cd07094 163 PLSALELAKILVEA----GVpEGVLQVVTgEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 588 VDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 644
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGqVCISVQRIYVHEE-----LYDEFIEAFvaAVKKLKV 293
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
230-359 |
1.33e-06 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 50.99 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 230 EPNSDLQGVN-VIsvkDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSppGSDDAKLIDIFYPGDQQSVTFGTksrvgmGG 307
Cdd:PRK12354 191 DADGKLHGVEaVI---DKDLAAALLAEQLDADLLLILTDVDAVYlDW--GKPTQRAIAQATPDELRELGFAA------GS 259
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1020738530 308 MEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGKKvGTFFSEVKPA 359
Cdd:PRK12354 260 MGPKVEAACeFVRATGKIAGIG-------SLEDIQAILAGEA-GTRISPETAG 304
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
225-334 |
2.41e-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: 49.67 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 225 VVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFdsppgsDDAKLIDIFYPGDQQSVtfgtKSRVG 304
Cdd:cd04251 149 VVSPVAYSEEGEPLNV----DGDRAAAAIAAALKAERLILLTDVEGLY------LDGRVIERITVSDAESL----LEKAG 214
|
90 100 110
....*....|....*....|....*....|.
gi 1020738530 305 mGGMEAKVKAALWALQGGTS-VVIANGTHPK 334
Cdd:cd04251 215 -GGMKRKLLAAAEAVEGGVReVVIGDARADS 244
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
378-762 |
2.62e-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: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 378 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSlstsklnslaiGlrQIA 444
Cdd:pfam00171 46 RKTPAAERAAILRKAADLLEERKDELaeLETleNGKPLAEARGevdraidvlRYYAGLARRLD-----------G--ETL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 445 ASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI--FESrPDCLP--QVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:pfam00171 113 PSDPGRLAYTRRE--------------PLGVVGAItpWNF-PLLLPawKIAP-ALAAGNTVVLKPSELTPLTALLLAELF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 521 QEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHSegicHMYVDSE 591
Cdd:pfam00171 177 EEA----GLpAGVLNVVTGsgAEVGEALVE-HPDVRKVSFTGSTAVGRHIAEAAaqNLKRVTlelgGKN----PLIVLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 592 ASVDKVTRLVRDSKCEYP-AACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI--------HAGP--------KFAS 652
Cdd:pfam00171 248 ADLDAAVEAAVFGAFGNAgQVCTATSRLLVHES-----IYDEFVEKLveAAKKLKVgdpldpdtDMGPliskaqleRVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 653 Y-----------------------------LTFSPSEVKSLRTE-YGDLeLCIEVVDNVQDAIDHIH--KYGssHTDVIV 700
Cdd:pfam00171 323 YvedakeegaklltggeagldngyfveptvLANVTPDMRIAQEEiFGPV-LSVIRFKDEEEAIEIANdtEYG--LAAGVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738530 701 TEDENTAEFFLQHVDSACVFWNASTRFS-DGYRFGlgaevGISTSRI-HARGPVGLEGLLTTKW 762
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDaDGLPFG-----GFKQSGFgREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
370-644 |
5.77e-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: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 370 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLA----NKKDLEEAEG---------RLAAPLLKRLSlstsklnsl 436
Cdd:COG1012 52 ARAAFPAWAATPPAERAAILLRAADLLEERREELAALltleTGKPLAEARGevdraadflRYYAGEARRLY--------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 437 aiGlRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPdcLPQVA---ALAIASGNGLLLKGGKEA 509
Cdd:COG1012 123 --G-ETIPSDAPGTRAYVRRE--------------PLGVVGAItpwnF---P--LALAAwklAPALAAGNTVVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 510 AHSNRILHLLTQEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHS 580
Cdd:COG1012 181 PLSALLLAELLEEA----GLpAGVLNVVTGdgSEVGAALVA-HPDVDKISFTGSTAVGRRIAAAAaeNLKRVTlelgGKN 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1020738530 581 egicHMYVDSEASVDKVTRLVRDSKCEYpA--ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 644
Cdd:COG1012 256 ----PAIVLDDADLDAAVEAAVRGAFGN-AgqRCTAASRLLVHES-----IYDEFVERLvaAAKALKV 313
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
226-351 |
9.29e-06 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 48.46 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 226 VPPAEPNSDLQGVNviSVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSpPGSDDAKLIDIFYPgdQQSVTFGTKSRVGM 305
Cdd:PRK12454 196 IPVIEEDGELKGVE--AVIDKDLASELLAEELNADIFIILTDVEKVYLN-YGKPDQKPLDKVTV--EEAKKYYEEGHFKA 270
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1020738530 306 GGMEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGkKVGT 351
Cdd:PRK12454 271 GSMGPKILAAIrFVENGGKRAIIA-------SLEKAVEALEG-KTGT 309
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
207-333 |
1.39e-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: 47.72 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 207 LHELLRMNIVPivntndaVVPPAEPNSDLQGVNVisvkdN-DSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLID 285
Cdd:COG0548 157 IRALLDAGYIP-------VISPIGYSPTGEVYNI-----NaDTVAGAIAAALKAEKLILLTDVPGVLD-----DPGSLIS 219
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1020738530 286 IFYPGDQQSVTfgtKSRVGMGGMEAKVKAALWALQGGT-SVVIANGTHP 333
Cdd:COG0548 220 ELTAAEAEELI---ADGVISGGMIPKLEAALDAVRGGVkRVHIIDGRVP 265
|
|
| AAK_NAGK-NC |
cd04249 |
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ... |
207-351 |
5.13e-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: 45.48 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 207 LHELLRMNIVPIVNTNDAvvppaepnsDLQG--VNVisvkDNDSLAARLAVEMKTDLlIVLSDVEGLFDSppgsdDAKLI 284
Cdd:cd04249 129 LNDLLKAGFLPIISSIGA---------DDQGqlMNV----NADQAATAIAQLLNADL-VLLSDVSGVLDA-----DKQLI 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1020738530 285 DIFypgDQQSVTFGTKSRVGMGGMEAKVKAALWALQG-GTSVVIANGTHPKvsghVITDIVEGKKVGT 351
Cdd:cd04249 190 SEL---NAKQAAELIEQGVITDGMIVKVNAALDAAQSlRRGIDIASWQYPE----QLTALLAGEPVGT 250
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| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
378-578 |
5.18e-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: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 378 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSLSTSKLNslaiglrqIA 444
Cdd:cd07082 56 PTMPLEERIDCLHKFADLLKENKEEVanLLMweIGKTLKDALKevdrtidyiRDTIEELKRLDGDSLPGD--------WF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 445 ASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI-------FESrpdclpqVAALAIA--SGNGLLLKGGKEAAhsnrI 515
Cdd:cd07082 128 PGTKGKIAQVRR--------------EPLGVVLAIgpfnyplNLT-------VSKLIPAliMGNTVVFKPATQGV----L 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738530 516 LHLLTQEALSIHGV-KEAVQLVNTR-EEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP-VMG 578
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 ... |
247-352 |
5.93e-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: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 247 DSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVTFGTKSRVGmggmeAKVKAALWALQ----G 321
Cdd:cd04253 118 DAVAALLAERLGADLLINATNVDGVYSKDPRKDpDAKKFDRLSADELIDIVGKSSWKAG-----SNEPFDPLAAKiierS 192
|
90 100 110
....*....|....*....|....*....|.
gi 1020738530 322 GTSVVIANGTHPKvsghVITDIVEGKKVGTF 352
Cdd:cd04253 193 GIKTIVVDGRDPE----NLERALKGEFVGTI 219
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| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
363-571 |
9.43e-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: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 363 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 429
Cdd:cd07149 23 VEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEfartIALEAGKPIKDARKevdraietlRLSAEEAKRLAGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 430 TSKLNSlaiglrqiAASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI--FEsrpDCLPQVA---ALAIASGNGLLLK 504
Cdd:cd07149 103 TIPFDA--------SPGGEGRIGFTIR--------------EPIGVVAAItpFN---FPLNLVAhkvGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 505 GGKEAAHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVED-LCRlDKMIDLIIPRGSSQLVRDIQKAA 571
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) ... |
350-643 |
1.22e-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: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 350 GTFFSEVKPAGP-TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEGRLAapllk 424
Cdd:cd07147 9 GEVVARVALAGPdDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEElaetIVLEAGKPIKDARGEVA----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 425 RlslstsklnslAIGLRQIAA-SSQDSVGRVLRRTRIAKNLELEQVT--VPIGVLLVIfesRPDCLP--QVA---ALAIA 496
Cdd:cd07147 84 R-----------AIDTFRIAAeEATRIYGEVLPLDISARGEGRQGLVrrFPIGPVSAI---TPFNFPlnLVAhkvAPAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 497 SGNGLLLKggkeAAHSNRILHLLTQEALSIHGV-KEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP 575
Cdd:cd07147 150 AGCPFVLK----PASRTPLSALILGEVLAETGLpKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1020738530 576 VMGHSEGICHMYVDSEASVDK-VTRLVRDSKCEYPAACNALETLLIHRDllrtpLFDQIIDMLrVEQVK 643
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFaAQRIIFGAFYQAGQSCISVQRVLVHRS-----VYDEFKSRL-VARVK 288
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
378-650 |
1.77e-03 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 41.55 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 378 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLeeaegrlaapllkRLSLSTSKLNSLAIGLRQIAASSQDsvgrvlrr 457
Cdd:PTZ00381 24 KTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDL-------------GRHPFETKMTEVLLTVAEIEHLLKH-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 458 trIAKNLELEQVTV--------------PIGVLLVIFE-SRP--DCLPQVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:PTZ00381 83 --LDEYLKPEKVDTvgvfgpgksyiipePLGVVLVIGAwNYPlnLTLIPLAG-AIAAGNTVVLKPSELSPHTSKLMAKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738530 521 QEALSihgvKEAVQLVNT-REEVEDLCRLDkmIDLIIPRGSSQLVRDIQKAA--KGIPVMGHSEGICHMYVDSEASVDKV 597
Cdd:PTZ00381 160 TKYLD----PSYVRVIEGgVEVTTELLKEP--FDHIFFTGSPRVGKLVMQAAaeNLTPCTLELGGKSPVIVDKSCNLKVA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1020738530 598 TRLVRDSKC-EYPAACNALETLLIHRDLLrtplfDQIIDMLRvEQVKIHAGPKF 650
Cdd:PTZ00381 234 ARRIAWGKFlNAGQTCVAPDYVLVHRSIK-----DKFIEALK-EAIKEFFGEDP 281
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