|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
4-427 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 713.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKicNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 84 DDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQD 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 164 KDEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVS 243
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 244 DELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDS 323
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 324 ASVQWlQDCAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTAvKEGGGVITSGGRVLTVTAVRPTLESALQS 403
Cdd:COG0151 319 VELEW-DDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTA-LEDGKLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....
gi 28839564 404 ANEGVAAISFPDAVYRRDIGHRAI 427
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRAL 420
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
4-427 |
0e+00 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 620.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKICNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 84 DDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKASGLAAGKGVIVAQD 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 164 KDEACQAVLDIMKDKaFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 244 DELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDS 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 324 ASVQWLQDcAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTAvKEGGGVITSGGRVLTVTAVRPTLESALQS 403
Cdd:TIGR00877 320 VELRFDNR-AAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTK-ADNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....
gi 28839564 404 ANEGVAAISFPDAVYRRDIGHRAI 427
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
433-778 |
0e+00 |
|
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439920 [Multi-domain] Cd Length: 343 Bit Score: 582.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 433 TRGLTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHST 512
Cdd:COG0150 2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 513 LGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVDVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVG 592
Cdd:COG0150 82 IGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 593 AVERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPfgRPGQTIGDVLLTPTKIYSRALQPVLR 672
Cdd:COG0150 162 VVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP--ELGRTLGEALLEPTRIYVKPVLALLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 673 SGAVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKSDAQRVLR 752
Cdd:COG0150 239 AVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALA 318
|
330 340
....*....|....*....|....*..
gi 28839564 753 LLQAH-EESWIIGSLThrhPGAESVVV 778
Cdd:COG0150 319 LLKAAgETAYVIGEVV---AGEGEGVV 342
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-430 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 530.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 6 LVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGK-ICNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMVD 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDaTCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 85 DLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 165 DEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSD 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 245 ELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQG--PRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELD 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 323 SASVQWLQDcAAVTVVMASGGYPNAYRKGLEISGLSQASEM--GVQVFHAGTAVKEGGGVITSGGRVLTVTAVRPTLESA 400
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|
gi 28839564 401 LQSANEGVAAISFPDAVYRRDIGHRAITYL 430
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARL 428
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
1.51e-174 |
|
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100032 [Multi-domain] Cd Length: 297 Bit Score: 507.78 E-value: 1.51e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 469 ADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVDV 548
Cdd:cd02196 1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 549 AASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLV 628
Cdd:cd02196 81 AAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 629 RTILERSGLNISSPAPFGrpGQTIGDVLLTPTKIYSRALQPVLRSGAVKAFAHITGGGLLENIPRVLPADLTADLDACRW 708
Cdd:cd02196 160 RKILFEEGLDYDDPEPGL--GKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSW 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 709 RIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKSDAQRVLRLLQAH-EESWIIGSLT 767
Cdd:cd02196 238 EIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLgEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
436-769 |
1.37e-152 |
|
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273316 [Multi-domain] Cd Length: 332 Bit Score: 452.56 E-value: 1.37e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 436 LTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAaGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQ 515
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 516 DLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVDVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVE 595
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 596 RSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLnISSPAPFGRPGQTIGDVLLTPTKIYSRALQPVLRSGA 675
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAG-LDYEDTPEEFGKTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 676 VKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKSDAQRVLRLLQ 755
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....*
gi 28839564 756 A-HEESWIIGSLTHR 769
Cdd:TIGR00878 318 AyGEKAWVIGEVKKG 332
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
435-764 |
1.05e-126 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 387.62 E-value: 1.05e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 435 GLTYKDSGVDIAAGNRLVDIIKPLAkatsrPGcnadLGGFAGLFDlkaagFTDPILVSGTDGVGTKLKIAQECGVHSTLG 514
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 515 QDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVDVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAV 594
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 595 ERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPFGrpGQTIGDVLLTPTKIYSRALQPVLRSG 674
Cdd:PLN02557 204 KKDAVIDG-KNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGA--SVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 675 AVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKSDAQRVLRll 754
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILE-- 358
|
330
....*....|
gi 28839564 755 QAHEESWIIG 764
Cdd:PLN02557 359 EGAYPAYRIG 368
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
4.21e-120 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 363.14 E-value: 4.21e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 105 ASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPALVVKASGLAAGKGVIVAQDKDEACQAVLDIMKDKAFGSAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 185 ETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSDELLQEISRSVLQKTVDGMRE 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 28839564 265 EGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
814-912 |
2.41e-43 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 155.62 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90
....*....|....*....
gi 28839564 894 LVCLAGFMRILTGPFVRKW 912
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAF 99
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
812-914 |
5.74e-43 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 155.19 E-value: 5.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 812 RTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFS 891
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100
....*....|....*....|...
gi 28839564 892 VELVCLAGFMRILTGPFVRKWSD 914
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPG 103
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
814-913 |
1.77e-31 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 121.24 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:pfam00551 2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAAD 81
|
90 100
....*....|....*....|
gi 28839564 894 LVCLAGFMRILTGPFVRKWS 913
Cdd:pfam00551 82 VIVLAGYMRILPPEFLQAPP 101
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
814-913 |
6.95e-30 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 117.09 E-value: 6.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:TIGR00639 2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVD 81
|
90 100
....*....|....*....|
gi 28839564 894 LVCLAGFMRILTGPFVRKWS 913
Cdd:TIGR00639 82 LVVLAGFMRILGPTFLSRFA 101
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
608-770 |
1.16e-28 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 112.44 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 608 EGDLLLGVSSSGIHSNGFSLVRTILERSGLnisspapfgrPGQTIGDVLLTPTKIYSRALQPVLrSGAVKAFAHITGGGL 687
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGL----------AAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 688 LENIPRVLPA-DLTADLDAcrwRIPPVFSWLQQqggvcEQEFCRTFNCGLGAVLVVSKsDAQRVLRLLQAH-EESWIIGS 765
Cdd:pfam02769 71 AGALAEMAPAsGVGAEIDL---DKVPIFEELML-----PLEMLLSENQGRGLVVVAPE-EAEAVLAILEKEgLEAAVIGE 141
|
....*
gi 28839564 766 LTHRH 770
Cdd:pfam02769 142 VTAGG 146
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
809-922 |
1.32e-06 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 50.88 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 809 SRRRTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLkrAALAGIQTRVVDH-KLygSRAEFDGTIDKVL 887
Cdd:PRK06027 86 SAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEARLLELI 161
|
90 100 110
....*....|....*....|....*....|....*....
gi 28839564 888 EEFSVELVCLAGFMRILTGPFVRKWSD----VEHSSLSA 922
Cdd:PRK06027 162 DEYQPDLVVLARYMQILSPDFVARFPGriinIHHSFLPA 200
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
4-427 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 713.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKicNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 84 DDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQD 163
Cdd:COG0151 80 DAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 164 KDEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVS 243
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 244 DELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDS 323
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 324 ASVQWlQDCAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTAvKEGGGVITSGGRVLTVTAVRPTLESALQS 403
Cdd:COG0151 319 VELEW-DDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTA-LEDGKLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....
gi 28839564 404 ANEGVAAISFPDAVYRRDIGHRAI 427
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRAL 420
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
4-427 |
0e+00 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 620.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKICNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 84 DDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKASGLAAGKGVIVAQD 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 164 KDEACQAVLDIMKDKaFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 244 DELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELDS 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 324 ASVQWLQDcAAVTVVMASGGYPNAYRKGLEISGLSQASEMGVQVFHAGTAvKEGGGVITSGGRVLTVTAVRPTLESALQS 403
Cdd:TIGR00877 320 VELRFDNR-AAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTK-ADNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....
gi 28839564 404 ANEGVAAISFPDAVYRRDIGHRAI 427
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PurM |
COG0150 |
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ... |
433-778 |
0e+00 |
|
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439920 [Multi-domain] Cd Length: 343 Bit Score: 582.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 433 TRGLTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHST 512
Cdd:COG0150 2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 513 LGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVDVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVG 592
Cdd:COG0150 82 IGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 593 AVERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPfgRPGQTIGDVLLTPTKIYSRALQPVLR 672
Cdd:COG0150 162 VVEKDKIIDG-SRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP--ELGRTLGEALLEPTRIYVKPVLALLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 673 SGAVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKSDAQRVLR 752
Cdd:COG0150 239 AVDVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALA 318
|
330 340
....*....|....*....|....*..
gi 28839564 753 LLQAH-EESWIIGSLThrhPGAESVVV 778
Cdd:COG0150 319 LLKAAgETAYVIGEVV---AGEGEGVV 342
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-430 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 530.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 6 LVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGK-ICNSEVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMVD 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDaTCVPDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 85 DLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 165 DEACQAVLDIMKDKAFGSAGETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSD 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 245 ELLQEISRSVLQKTVDGMREEGAPYVGVLYAGLMLTAQG--PRVLEFNCRFGDPECQVLLPLLQSDLYEVCMQTLRCELD 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 323 SASVQWLQDcAAVTVVMASGGYPNAYRKGLEISGLSQASEM--GVQVFHAGTAVKEGGGVITSGGRVLTVTAVRPTLESA 400
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|
gi 28839564 401 LQSANEGVAAISFPDAVYRRDIGHRAITYL 430
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARL 428
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
469-767 |
1.51e-174 |
|
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.
Pssm-ID: 100032 [Multi-domain] Cd Length: 297 Bit Score: 507.78 E-value: 1.51e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 469 ADLGGFAGLFDLKAAGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVDV 548
Cdd:cd02196 1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 549 AASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLV 628
Cdd:cd02196 81 AAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDG-SKIKPGDVLIGLPSSGLHSNGYSLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 629 RTILERSGLNISSPAPFGrpGQTIGDVLLTPTKIYSRALQPVLRSGAVKAFAHITGGGLLENIPRVLPADLTADLDACRW 708
Cdd:cd02196 160 RKILFEEGLDYDDPEPGL--GKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSW 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 709 RIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKSDAQRVLRLLQAH-EESWIIGSLT 767
Cdd:cd02196 238 EIPPIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLgEKAYVIGEVV 297
|
|
| purM |
TIGR00878 |
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ... |
436-769 |
1.37e-152 |
|
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273316 [Multi-domain] Cd Length: 332 Bit Score: 452.56 E-value: 1.37e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 436 LTYKDSGVDIAAGNRLVDIIKPLAKATSRPGCNADLGGFAGLFDLKAaGFTDPILVSGTDGVGTKLKIAQECGVHSTLGQ 515
Cdd:TIGR00878 1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 516 DLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVDVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAVE 595
Cdd:TIGR00878 80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 596 RSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLnISSPAPFGRPGQTIGDVLLTPTKIYSRALQPVLRSGA 675
Cdd:TIGR00878 160 KDEIITG-EKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAG-LDYEDTPEEFGKTLGEELLEPTRIYVKPILELIKSVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 676 VKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKSDAQRVLRLLQ 755
Cdd:TIGR00878 238 VHGLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLN 317
|
330
....*....|....*
gi 28839564 756 A-HEESWIIGSLTHR 769
Cdd:TIGR00878 318 AyGEKAWVIGEVKKG 332
|
|
| PLN02557 |
PLN02557 |
phosphoribosylformylglycinamidine cyclo-ligase |
435-764 |
1.05e-126 |
|
phosphoribosylformylglycinamidine cyclo-ligase
Pssm-ID: 178172 [Multi-domain] Cd Length: 379 Bit Score: 387.62 E-value: 1.05e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 435 GLTYKDSGVDIAAGNRLVDIIKPLAkatsrPGcnadLGGFAGLFDlkaagFTDPILVSGTDGVGTKLKIAQECGVHSTLG 514
Cdd:PLN02557 58 GLTYKDAGVDIDAGSELVRRIAKMA-----PG----IGGFGGLFP-----FGDSYLVAGTDGVGTKLKLAFETGIHDTIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 515 QDLVAMCVNDVLAQGAEPLFFLDYFSCGRLDVDVAASVIGGIADACQMAGCALLGGETAEMPGVYPPGEYDLAGFCVGAV 594
Cdd:PLN02557 124 IDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 595 ERSALLPRlKDISEGDLLLGVSSSGIHSNGFSLVRTILERSGLNISSPAPFGrpGQTIGDVLLTPTKIYSRALQPVLRSG 674
Cdd:PLN02557 204 KKDAVIDG-KNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGA--SVTIGEALMAPTVIYVKQVLDIISKG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 675 AVKAFAHITGGGLLENIPRVLPADLTADLDACRWRIPPVFSWLQQQGGVCEQEFCRTFNCGLGAVLVVSKSDAQRVLRll 754
Cdd:PLN02557 281 GVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAADRILE-- 358
|
330
....*....|
gi 28839564 755 QAHEESWIIG 764
Cdd:PLN02557 359 EGAYPAYRIG 368
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
4.21e-120 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 363.14 E-value: 4.21e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 105 ASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPALVVKASGLAAGKGVIVAQDKDEACQAVLDIMKDKAFGSAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 185 ETVVVEELLDGQEVSCLCFSDGVTVAPMPPAQDHKRLLDGDMGPNTGGMGAYCPTPQVSDELLQEISRSVLQKTVDGMRE 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 28839564 265 EGAPYVGVLYAGLMLTAQGPRVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
4-104 |
1.11e-48 |
|
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam00289). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460723 [Multi-domain] Cd Length: 102 Bit Score: 167.53 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 4 RVLVIGSGGREHALAWKFAQSPHVQQVLVAPGNAGTANCGKICNseVSVNNHSILAQYCKDHKVGLVVVGPEVPLAAGMV 83
Cdd:pfam02844 2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAECVD--IDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 28839564 84 DDLT--AAGVLCFGPSARAAQLE 104
Cdd:pfam02844 80 DALRerAAGIPVFGPSKAAAQLE 102
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
814-912 |
2.41e-43 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 155.62 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:cd08645 1 RIAVLASGSGSNLQALIDAIKSGKLNAEIVLVISNNPDAYGLERAKKAGIPTFVINRKDFPSREEFDEALLELLKEYKVD 80
|
90
....*....|....*....
gi 28839564 894 LVCLAGFMRILTGPFVRKW 912
Cdd:cd08645 81 LIVLAGFMRILSPEFLEAF 99
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
812-914 |
5.74e-43 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 155.19 E-value: 5.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 812 RTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFS 891
Cdd:COG0299 1 MKRIAVLISGRGSNLQALIDAIEAGDLPAEIVLVISNRPDAYGLERARAAGIPTFVLDHKDFPSREAFDAALLEALDAYG 80
|
90 100
....*....|....*....|...
gi 28839564 892 VELVCLAGFMRILTGPFVRKWSD 914
Cdd:COG0299 81 PDLVVLAGFMRILTPEFVRAFPG 103
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-425 |
4.61e-38 |
|
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02787).
Pssm-ID: 460722 [Multi-domain] Cd Length: 88 Bit Score: 136.81 E-value: 4.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 334 AVTVVMASGGYPNAYRKGLEISGLSQAsemGVQVFHAGTAvKEGGGVITSGGRVLTVTAVRPTLESALQSANEGVAAISF 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA---GVKVFHAGTK-LKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDF 76
|
90
....*....|..
gi 28839564 414 PDAVYRRDIGHR 425
Cdd:pfam02843 77 EGMFYRKDIGTR 88
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
814-913 |
1.77e-31 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 121.24 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:pfam00551 2 KIAVLISGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAAD 81
|
90 100
....*....|....*....|
gi 28839564 894 LVCLAGFMRILTGPFVRKWS 913
Cdd:pfam00551 82 VIVLAGYMRILPPEFLQAPP 101
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
814-913 |
6.95e-30 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 117.09 E-value: 6.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKLYGSRAEFDGTIDKVLEEFSVE 893
Cdd:TIGR00639 2 RIVVLISGNGSNLQAIIDACKEGKIPASVVLVISNKPDAYGLERAAQAGIPTFVLSLKDFPSREAFDQAIIEELRAHEVD 81
|
90 100
....*....|....*....|
gi 28839564 894 LVCLAGFMRILTGPFVRKWS 913
Cdd:TIGR00639 82 LVVLAGFMRILGPTFLSRFA 101
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
608-770 |
1.16e-28 |
|
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.
Pssm-ID: 460684 [Multi-domain] Cd Length: 152 Bit Score: 112.44 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 608 EGDLLLGVSSSGIHSNGFSLVRTILERSGLnisspapfgrPGQTIGDVLLTPTKIYSRALQPVLrSGAVKAFAHITGGGL 687
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGL----------AAVQLGDPLLEPTLIYVKLLLAAL-GGLVKAMHDITGGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 688 LENIPRVLPA-DLTADLDAcrwRIPPVFSWLQQqggvcEQEFCRTFNCGLGAVLVVSKsDAQRVLRLLQAH-EESWIIGS 765
Cdd:pfam02769 71 AGALAEMAPAsGVGAEIDL---DKVPIFEELML-----PLEMLLSENQGRGLVVVAPE-EAEAVLAILEKEgLEAAVIGE 141
|
....*
gi 28839564 766 LTHRH 770
Cdd:pfam02769 142 VTAGG 146
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
490-765 |
3.64e-27 |
|
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 100027 [Multi-domain] Cd Length: 222 Bit Score: 110.56 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 490 LVSGTDGVGTKLKIAqecgvHSTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGR-LDVDVAASVIGGIADACQMAGCALL 568
Cdd:cd00396 2 LAMSTDGINPPLAIN-----PWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 569 GGETAEMPGVYPPgEYDLAGFCVGAVERSAllprlkdisegdlllGVSSSGIhsngfslvrtilersglnisspapfgRP 648
Cdd:cd00396 77 GGHTSVSPGTMGH-KLSLAVFAIGVVEKDR---------------VIDSSGA--------------------------RP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 649 GQTIgdvLLTPTkiysRALQPVLRSGAVKAFAHITGGGLLENIPRVLPA-DLTADLDACRWRIPPVFSWLQQQGGvceqE 727
Cdd:cd00396 115 GDVL---ILTGV----DAVLELVAAGDVHAMHDITDGGLLGTLPELAQAsGVGAEIDLEAIPLDEVVRWLCVEHI----E 183
|
250 260 270
....*....|....*....|....*....|....*....
gi 28839564 728 FCRTFNCGLGAVLVVSKSDAQRVLRLLQAH-EESWIIGS 765
Cdd:cd00396 184 EALLFNSSGGLLIAVPAEEADAVLLLLNGNgIDAAVIGR 222
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
487-594 |
7.26e-23 |
|
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.
Pssm-ID: 459859 [Multi-domain] Cd Length: 104 Bit Score: 94.05 E-value: 7.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 487 DPILVSGTDGVGTKLKIAqecGVHsTLGQDLVAMCVNDVLAQGAEPLFFLDYFSCGR--LDVDVAASVIGGIADACQMAG 564
Cdd:pfam00586 2 DAAVAVTTDGHGTPSLVD---PYH-FPGAKAVAGNLSDIAAMGARPLAFLDSLALPGgpEVEWVLEEIVEGIAEACREAG 77
|
90 100 110
....*....|....*....|....*....|
gi 28839564 565 CALLGGETAEMPGVYPPgeyDLAGFCVGAV 594
Cdd:pfam00586 78 VPLVGGDTSFDPEGGKP---TISVTAVGIV 104
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
95-294 |
3.21e-17 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 82.61 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 95 GPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDKDEACQAVLDI 174
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYP-VVVKPADGAGSRGVRVVRDEEELEAALAEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 175 MKDKAFGSAGETVVVEELLDGQEVSCLCFS-DGVTVapmpPAQDHKRLLDGDMGPNTGGMgayCPTPqVSDELLQEIsRS 253
Cdd:COG0439 122 RAEAKAGSPNGEVLVEEFLEGREYSVEGLVrDGEVV----VCSITRKHQKPPYFVELGHE---APSP-LPEELRAEI-GE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 28839564 254 VLQKTVD--GMREegapyvGVLYAGLMLTAQG-PRVLEFNCRFG 294
Cdd:COG0439 193 LVARALRalGYRR------GAFHTEFLLTPDGePYLIEINARLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
86-290 |
4.25e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 61.88 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 86 LTAAGVLCFgPSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDKD 165
Cdd:COG0189 77 LEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGP-VVLKPLDGSGGRGVFLVEDED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 166 EAcQAVLDIMkdkaFGSAGETVVVEELL---DGQEVSCLCFsDGVTVAPM---PPAQDHKRlldgdmgpNT--GGMGAYC 237
Cdd:COG0189 155 AL-ESILEAL----TELGSEPVLVQEFIpeeDGRDIRVLVV-GGEPVAAIrriPAEGEFRT--------NLarGGRAEPV 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28839564 238 PtpqVSDELLqEISRSVlqktvdgmreegAPYVGVLYAG--LMLTAQGPRVLEFN 290
Cdd:COG0189 221 E---LTDEER-ELALRA------------APALGLDFAGvdLIEDDDGPLVLEVN 259
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
62-294 |
5.02e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 58.74 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 62 CKDHKVGLVVVG--PEVPLAAGMVDDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARwsSFTDPQQACAYIRD 139
Cdd:PRK12767 65 CKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPK--SYLPESLEDFKAAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 140 A----DFPaLVVKASGLAAGKGVIVAQDKDE---ACQAVLDIMkdkafgsagetvvVEELLDGQE--VSCLCFSDGVTVA 210
Cdd:PRK12767 143 AkgelQFP-LFVKPRDGSASIGVFKVNDKEElefLLEYVPNLI-------------IQEFIEGQEytVDVLCDLNGEVIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 211 PMPpaqdHKRLldgdmgpntgGM--GAYCPTPQVSDELLQEISRSVLQKTvdgmreegaPYVGVLYAGLMLTAQGPRVLE 288
Cdd:PRK12767 209 IVP----RKRI----------EVraGETSKGVTVKDPELFKLAERLAEAL---------GARGPLNIQCFVTDGEPYLFE 265
|
....*.
gi 28839564 289 FNCRFG 294
Cdd:PRK12767 266 INPRFG 271
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
86-290 |
9.17e-07 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 51.58 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 86 LTAAGVLCFGPSAraAQLEAS-KSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDK 164
Cdd:TIGR00768 69 LESLGVPVINSSD--AILNAGdKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFP-VVLKPVFGSWGRGVSLARDR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 165 DEAcQAVLDIMkdKAFGSAGETVVVEELLD---GQEVSCLCFSDGVtVAPMppaqdhKRLLDGDMGPNT--GGMGAYCP- 238
Cdd:TIGR00768 146 QAA-ESLLEHF--EQLNGPQNLFLVQEYIKkpgGRDIRVFVVGDEV-VAAI------YRITSGHWRSNLarGGKAEPCSl 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 28839564 239 TPQVsDELLQEISRSVlqktvdgmreeGAPYVGVlyaGLMLTAQGPRVLEFN 290
Cdd:TIGR00768 216 TEEI-EELAIKAAKAL-----------GLDVAGV---DLLESEDGLLVNEVN 252
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
65-292 |
1.22e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 51.95 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 65 HKVGLVVV--GPE--VPLAagmvDDLTAAGVLCFG-----PSARAAQLEASKSFSKAfmdrhNIPTARWSSFTDPQQACA 135
Cdd:PRK07206 67 RKLGPEAIiaGAEsgVELA----DRLAEILTPQYSndpalSSARRNKAEMINALAEA-----GLPAARQINTADWEEAEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 136 YIRDADFPA--LVVKASGLAAGKGVIVAQDKDEACQAVLDIM-KDKAFGSAGETVVVEELLDGQEVSCLCFS-DG-VTVA 210
Cdd:PRK07206 138 WLRENGLIDrpVVIKPLESAGSDGVFICPAKGDWKHAFNAILgKANKLGLVNETVLVQEYLIGTEYVVNFVSlDGnHLVT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 211 PMppAQDHKRlldgdmgPNTGGMGAYcptpqVSDELL-------QEISRSVlQKTVD--GMREegapyvGVLYAGLMLTA 281
Cdd:PRK07206 218 EI--VRYHKT-------SLNSGSTVY-----DYDEFLdysepeyQELVDYT-KQALDalGIKN------GPAHAEVMLTA 276
|
250
....*....|.
gi 28839564 282 QGPRVLEFNCR 292
Cdd:PRK07206 277 DGPRLIEIGAR 287
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
809-922 |
1.32e-06 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 50.88 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 809 SRRRTRVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLkrAALAGIQTRVVDH-KLygSRAEFDGTIDKVL 887
Cdd:PRK06027 86 SAERKRVVILVSKEDHCLGDLLWRWRSGELPVEIAAVISNHDDLRSL--VERFGIPFHHVPVtKE--TKAEAEARLLELI 161
|
90 100 110
....*....|....*....|....*....|....*....
gi 28839564 888 EEFSVELVCLAGFMRILTGPFVRKWSD----VEHSSLSA 922
Cdd:PRK06027 162 DEYQPDLVVLARYMQILSPDFVARFPGriinIHHSFLPA 200
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
814-910 |
7.77e-06 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 47.77 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 814 RVAVLISGSGTNLQALMDQARKPSSSAEIVLVISNRPGVMGLKRAALAGIQTRVVDHKlygsRAEFDG-TIDKVLE---E 889
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVNGDVVVVVTNKPGCGGAEYARENGIPVLVYPKT----KGEPDGlSPDELVDalrG 76
|
90 100
....*....|....*....|.
gi 28839564 890 FSVELVCLAGFMRILTGPFVR 910
Cdd:PLN02331 77 AGVDFVLLAGYLKLIPVELVR 97
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
508-612 |
8.72e-06 |
|
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).
Pssm-ID: 100030 [Multi-domain] Cd Length: 291 Bit Score: 48.70 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 508 GVH-------STLGQDLVAMCVNDVLAQGAEPLFFLdyFSCG---RLDVDVAASVIGGIADACQMAGCALLGGETAEMPG 577
Cdd:cd02194 47 GVHfppdttpEDIGWKALAVNLSDLAAMGARPLGFL--LSLGlppDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSE 124
|
90 100 110
....*....|....*....|....*....|....*
gi 28839564 578 VYppgeydLAGFCVGAVERSALLPRlKDISEGDLL 612
Cdd:cd02194 125 LV------ISVTALGEVEKGKPLRR-SGAKPGDLL 152
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
105-296 |
1.39e-05 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 46.22 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 105 ASKSFSKAFMDRHNIPTarwssftdPQQACAYIRDADFPALVVKASGLAAGKGVIVAQDKDEACqavldimkdkafgSAG 184
Cdd:pfam02655 2 SDKLKTYKALKNAGVPT--------PETLQAEELLREEKKYVVKPRDGCGGEGVRKVENGREDE-------------AFI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 185 ETVVVEELLDGQEVSCLCFSDGVTVAPMPPaqdHKRLLDgdmgpNTGGMGAYC----PTPQVSDELLQEISRSVLQKtVD 260
Cdd:pfam02655 61 ENVLVQEFIEGEPLSVSLLSDGEKALPLSV---NRQYID-----NGGSGFVYAgnvtPSRTELKEEIIELAEEVVEC-LP 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 28839564 261 GMReeGapYVGVlyaGLMLTAQGPRVLEFNCRFGDP 296
Cdd:pfam02655 132 GLR--G--YVGV---DLVLKDNEPYVIEVNPRITTS 160
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
115-286 |
1.96e-05 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 46.09 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 115 DRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKASGLA-AGKGVIVAQDKDEACQAVldimkdKAFGsaGETVVVEELL 193
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPC-VVKARRGGyDGKGQYVVRSEADLPQAW------EELG--DGPVIVEEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 194 D-GQEVSCLC--FSDGVTVAPmPPAQDHKRllDGDMgpntggmgAYCPTPQVSDELLQEISRSVLQKTVDGMreegaPYV 270
Cdd:pfam02222 72 PfDRELSVLVvrSVDGETAFY-PVVETIQE--DGIC--------RLSVAPARVPQAIQAEAQDIAKRLVDEL-----GGV 135
|
170 180
....*....|....*....|....
gi 28839564 271 GVLYAGLMLTAQG--------PRV 286
Cdd:pfam02222 136 GVFGVELFVTEDGdllinelaPRP 159
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
111-199 |
2.91e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 47.38 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 111 KAFMDRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKasglAA-----GKGVIVAQDKDEAcqavldimkDKAFGSAGE 185
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPA-VLK----TRrggydGKGQVVIKSAADL---------EAAWAALGG 159
|
90
....*....|....*.
gi 28839564 186 T-VVVEELLD-GQEVS 199
Cdd:COG0026 160 GpCILEEFVPfERELS 175
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
68-292 |
5.77e-05 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 46.92 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 68 GLVV-VGPEVPLaaGMVDDLTAAGVLCFGPSARAA-QLEASKSFSKaFMDRHNIPTARWSSFTDPQQACAYIRDADFPAL 145
Cdd:TIGR01369 632 GVIVqFGGQTPL--NLAKALEEAGVPILGTSPESIdRAEDREKFSE-LLDELGIPQPKWKTATSVEEAVEFASEIGYPVL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 146 vVKASGLAAGKGVIVAQDKDEacqaVLDIMKDKAFGSAGETVVVEELL-DGQEVSCLCFSDGVTVApMPPAQDHKRlldg 224
Cdd:TIGR01369 709 -VRPSYVLGGRAMEIVYNEEE----LRRYLEEAVAVSPEHPVLIDKYLeDAVEVDVDAVSDGEEVL-IPGIMEHIE---- 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28839564 225 DMGPNTGGMGAYCPTPQVSDELLQEISRSVlQKTVDGMReegapYVGVLYAGLMLTAQGPRVLEFNCR 292
Cdd:TIGR01369 779 EAGVHSGDSTCVLPPQTLSAEIVDRIKDIV-RKIAKELN-----VKGLMNIQFAVKDGEVYVIEVNPR 840
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
89-193 |
2.09e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 44.97 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 89 AGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWS--SFTDPQQACAYIRDADFPaLVVKASGLAAGKGVIVAQDKDE 166
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTeeGIEDIEEAKEIAEEIGYP-VIIKASAGGGGIGMRVVYSEEE 176
|
90 100
....*....|....*....|....*....
gi 28839564 167 ACQAVLDIMK--DKAFGSAgeTVVVEELL 193
Cdd:PRK08654 177 LEDAIESTQSiaQSAFGDS--TVFIEKYL 203
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
96-199 |
3.30e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.99 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 96 PSARAAQLEASKSFSKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPAlVVKasglAA-----GKGVIVAQDKDEAcqa 170
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPA-VLK----TRrggydGKGQWVIRSAEDL--- 161
|
90 100 110
....*....|....*....|....*....|.
gi 28839564 171 vldimkDKAFGSAGET-VVVEELLD-GQEVS 199
Cdd:PRK06019 162 ------EAAWALLGSVpCILEEFVPfEREVS 186
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-194 |
4.06e-04 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 42.63 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 110 SKAFMDRHNIPTARWSSFTDPQQACAYIRDADFPALVVKASGLAAGK----GVIVAQDKDEACQAVLDI----MKDKAFG 181
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMlgknLVTKQTG 86
|
90
....*....|....*.
gi 28839564 182 SAGETV---VVEELLD 194
Cdd:pfam08442 87 PDGQPVnkvLVEEALD 102
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
80-209 |
1.98e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 41.55 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28839564 80 AGMVDDLTAAGVLCFGPSARAAQLEASKSFSKAFMDRHNIPTARWSSFT--DPQQACAYIRDADFPaLVVKASGLAAGKG 157
Cdd:PRK06111 89 ASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNleDAEEAIAIARQIGYP-VMLKASAGGGGIG 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 28839564 158 VIVAQDKDEACQAvLDIMKDKA---FGSAgeTVVVEELLDGQ---EVSCLCFSDGVTV 209
Cdd:PRK06111 168 MQLVETEQELTKA-FESNKKRAanfFGNG--EMYIEKYIEDPrhiEIQLLADTHGNTV 222
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
524-574 |
9.41e-03 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 39.29 E-value: 9.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 28839564 524 DVLAQGAEPLFFLDY--FSCGRLDVDVAASVIGGIADACQMAGCALLGGETAE 574
Cdd:COG0709 89 DVYAMGGRPLTALAIvgFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSID 141
|
|
| |
