|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-426 |
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: 819.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 1 MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPalQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA--ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 81 VDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 161 LEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVT 240
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 241 DDVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLD 320
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 321 EKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVADGKVFHAGTKLADDeQVVTNGGRVLCVTALGHTVAEAQKR 400
Cdd:COG0151 318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDG-KLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....*.
gi 446789542 401 AYALMTDIHWDDCFCRKDIGWRAIER 426
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-425 |
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: 702.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 1 MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPALQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGV 80
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 81 VDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 161 LEEAEAAVHDMLAGNaFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVT 240
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 241 DDVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLD 320
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 321 EKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVADGKVFHAGTKlADDEQVVTNGGRVLCVTALGHTVAEAQKR 400
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTK-ADNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....*
gi 446789542 401 AYALMTDIHWDDCFCRKDIGWRAIE 425
Cdd:TIGR00877 398 AYEAVEYIKFEGMFYRKDIGFRALE 422
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-428 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 590.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 4 LVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPALQNVA-IGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGVVD 82
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 83 TFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLE 162
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 163 EAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDD 242
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 243 VHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQ-GNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLDE 321
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKsGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 322 KTSEWDERASLGVVMAAGGYPGDYRTGDVIHGL-PLEEVADG-KVFHAGTKLADDEQVVTNGGRVLCVTALGHTVAEAQK 399
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLdEAEAVAPGvKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420
....*....|....*....|....*....
gi 446789542 400 RAYALMTDIHWDDCFCRKDIGWRAIEREQ 428
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
103-296 |
4.70e-109 |
|
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: 319.23 E-value: 4.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 103 GSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPI-VIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAFGDAG 181
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 182 HRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDDVHQRTMERIIWPTVKGMAA 261
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 446789542 262 EGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPET 296
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-102 |
4.21e-56 |
|
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: 180.24 E-value: 4.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 1 MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPalQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLA--ECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 446789542 81 VDTF--RAAGLKIFGPTAGAAQLE 102
Cdd:pfam02844 79 VDALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-422 |
3.42e-43 |
|
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: 146.44 E-value: 3.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 331 SLGVVMAAGGYPGDYRTGDVIHGLpleEVADGKVFHAGTKLaDDEQVVTNGGRVLCVTALGHTVAEAQKRAYALMTDIHW 410
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGL---DEAGVKVFHAGTKL-KDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDF 76
|
90
....*....|..
gi 446789542 411 DDCFCRKDIGWR 422
Cdd:pfam02843 77 EGMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
86-318 |
3.33e-21 |
|
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: 92.63 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 86 AAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAE 165
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 166 AAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKrvgdkdTGPNTGGMGAYSPAPvVTDDVHQ 245
Cdd:COG0439 116 AALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELRA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446789542 246 RTMERiiwpTVKGMAAEGNTYtGFLYAGLMIDKQGNPKVIEFNCRFGDpETQPIMLRMKS--DLVELCLAACEGK 318
Cdd:COG0439 189 EIGEL----VARALRALGYRR-GAFHTEFLLTPDGEPYLIEINARLGG-EHIPPLTELATgvDLVREQIRLALGE 257
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
1-206 |
1.85e-08 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 55.93 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 1 MKVLVIGNG--GREHALAwkaAQsPL-VETVFVAPGNAGTALEPALQNVAIGVTDIPALLDFAQ--------NEKIDLTI 69
Cdd:PRK06019 3 KTIGIIGGGqlGRMLALA---AA-PLgYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEqcdvityeFENVPAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 70 VGPEAPLVKGVVdtfraaGLKIFGPTAgaaqlegSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKA--- 146
Cdd:PRK06019 79 LDALAARVPVPP------GPDALAIAQ-------DRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrg 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446789542 147 --DglaaGKGVIVAMTLEEAEAAVHDMLAGNAfgdaghriVIEEFLDGE-EASFIVM--VDGEHV 206
Cdd:PRK06019 146 gyD----GKGQWVIRSAEDLEAAWALLGSVPC--------ILEEFVPFErEVSVIVArgRDGEVV 198
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-209 |
2.10e-08 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 55.50 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 105 KAFTKDFLARHKIPTAEYQNFTEVEPALAYLREK--GAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGnafgdaGH 182
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEelGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100
....*....|....*....|....*...
gi 446789542 183 RIVIEEFLDGEEASFIVMVDGE-HVLPM 209
Cdd:COG1181 170 KVLVEEFIDGREVTVGVLGNGGpRALPP 197
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
109-206 |
7.70e-08 |
|
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: 53.92 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 109 KDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKA-----DglaaGKGVIVAMTLEEAEAAVHDMlagnafgdAGHR 183
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90 100
....*....|....*....|....*.
gi 446789542 184 IVIEEFLDGE-EASFIVM--VDGEHV 206
Cdd:COG0026 162 CILEEFVPFErELSVIVArsPDGEVA 187
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
79-288 |
1.55e-07 |
|
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: 52.64 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 79 GVVDTFRAAGLKIFGPTAgAAQLEGSKAFTKDFLARHKIPTAEyqnfTEV----EPALAYLREKGAPIVIK-ADGlAAGK 153
Cdd:COG0189 72 ALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPP----TLVtrdpDDLRAFLEELGGPVVLKpLDG-SGGR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 154 GVIVAMTLEEAEAAVHDMlagnaFGDAGHRIVIEEFLDGEEASF--IVMVDGEHVLPMA--TSQDHKRVgdkdtgpNTGG 229
Cdd:COG0189 146 GVFLVEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDirVLVVGGEPVAAIRriPAEGEFRT-------NLAR 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 230 MGAYSPAPVvtddvhqrtMERIIWPTVKGMAAegntyTGFLYAGL-MIDKQGNPKVIEFN 288
Cdd:COG0189 214 GGRAEPVEL---------TDEERELALRAAPA-----LGLDFAGVdLIEDDDGPLVLEVN 259
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-292 |
3.93e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 51.42 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 1 MKVLVIGnGGREHAL--AWKAAQSPLveTVFVA-PGNAGTALEPALQNVAI-GVTD---IPALLDFAQNEKIDLTIVG-- 71
Cdd:PRK12767 2 MNILVTS-AGRRVQLvkALKKSLLKG--RVIGAdISELAPALYFADKFYVVpKVTDpnyIDRLLDICKKEKIDLLIPLid 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 72 PEAPLVKGVVDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREK--GAPIVIKADGL 149
Cdd:PRK12767 79 PELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGelQFPLFVKPRDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 150 AAGKGVIVAMTLEEAEAAVHDMLAgnafgdaghrIVIEEFLDGEEASFIVMVD--GEHV--LPMatsqdhKRVGDKDtgp 225
Cdd:PRK12767 159 SASIGVFKVNDKEELEFLLEYVPN----------LIIQEFIEGQEYTVDVLCDlnGEVIsiVPR------KRIEVRA--- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 226 ntggmGAYSPAPVVTDDVHQRTMERIiwptVKGMAAEGNtytgflyagLMID---KQGNPKVIEFNCRFG 292
Cdd:PRK12767 220 -----GETSKGVTVKDPELFKLAERL----AEALGARGP---------LNIQcfvTDGEPYLFEINPRFG 271
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
53-292 |
2.31e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 49.54 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 53 IPALLDFAQNEKIDLtIVGPEAPLVKgVVDTFRA---AGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVE 129
Cdd:COG3919 65 VDALLELAERHGPDV-LIPTGDEYVE-LLSRHRDeleEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSAD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 130 PALAYLREKGAPIVIK-ADGLAA-------GKGVIVAMTLEEAEAAVHDMLagnafgDAGHRIVIEEFL---DGEEASFI 198
Cdd:COG3919 143 DLDALAEDLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRIA------AAGYELIVQEYIpgdDGEMRGLT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 199 VMVDGEHVLPMATSQdHKRVGDkdtgPNTGGmgayspAPVVTDDVHQRTMERIiwpTVKGMAAEGntYTGFLYAGLMID- 277
Cdd:COG3919 217 AYVDRDGEVVATFTG-RKLRHY----PPAGG------NSAARESVDDPELEEA---ARRLLEALG--YHGFANVEFKRDp 280
|
250
....*....|....*
gi 446789542 278 KQGNPKVIEFNCRFG 292
Cdd:COG3919 281 RDGEYKLIEINPRFW 295
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
86-207 |
2.19e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 46.67 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 86 AAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQN--FTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEE 163
Cdd:PRK12833 100 AAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDgvVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQ 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446789542 164 --AEAAVHDMLAGNAFGDAGhrIVIEEFLdgEEASFI---VMVDGEHVL 207
Cdd:PRK12833 180 laAELPLAQREAQAAFGDGG--VYLERFI--ARARHIevqILGDGERVV 224
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
57-290 |
9.15e-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: 44.99 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 57 LDFAQNEKIDLTIV--GPEAPLvkGVVDTFRAAGLKIFGpTAGAA--QLEGSKAFTKdFLARHKIPTAEYQNFTEVEPAL 132
Cdd:TIGR01369 622 MNIIELEKPEGVIVqfGGQTPL--NLAKALEEAGVPILG-TSPESidRAEDREKFSE-LLDELGIPQPKWKTATSVEEAV 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 133 AYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAfgdaGHRIVIEEFL-DGEEASFIVMVDGEHVLPMAT 211
Cdd:TIGR01369 698 EFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSP----EHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGI 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 212 SQDHKRvgdkdTGPNTGGMGAYSPAPVVTDDVHQRtMERIiwptVKGMAAEGNtytgflYAGLM----IDKQGNPKVIEF 287
Cdd:TIGR01369 774 MEHIEE-----AGVHSGDSTCVLPPQTLSAEIVDR-IKDI----VRKIAKELN------VKGLMniqfAVKDGEVYVIEV 837
|
...
gi 446789542 288 NCR 290
Cdd:TIGR01369 838 NPR 840
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
105-204 |
1.08e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 44.53 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 105 KAFTKDFLARHKIPTAEYQNFTEVEPALAYLRE-KGAPIVIKADGLAAGKGVIV---AMTLEEAEAAVhDMlagnAFGDA 180
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIfkePASLEDYEKAL-EI----AFRED 563
|
90 100
....*....|....*....|....
gi 446789542 181 GHrIVIEEFLDGEEASFIVMvDGE 204
Cdd:PRK02471 564 SS-VLVEEFIVGTEYRFFVL-DGK 585
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
103-294 |
2.87e-04 |
|
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: 41.22 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 103 GSKAFTKDFLARHKIPTAEYQNFTEvepalayLREKGAPIVIK-ADGlAAGKGVIVAMTLEEAEAAVHDMLagnafgdag 181
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTPETLQAEE-------LLREEKKYVVKpRDG-CGGEGVRKVENGREDEAFIENVL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 182 hrivIEEFLDGEEASFIVMVDGEHVLPMATSQDHkrVGdkdtgpNTGGMGAYSPAPVVTDDVHQRTMERIiwptVKGMAA 261
Cdd:pfam02655 65 ----VQEFIEGEPLSVSLLSDGEKALPLSVNRQY--ID------NGGSGFVYAGNVTPSRTELKEEIIEL----AEEVVE 128
|
170 180 190
....*....|....*....|....*....|...
gi 446789542 262 EGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDP 294
Cdd:pfam02655 129 CLPGLRGYVGVDLVLKDNE-PYVIEVNPRITTS 160
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
109-191 |
3.05e-04 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 42.77 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 109 KDFLARHKIPTAEYQNFTEVEPALAYLRE-KGAPIVIKADGLAAGK----GVIVAMTLEEAEAAVHDML----AGNAFGD 179
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQILgmtlVTHQTGP 88
|
90
....*....|....*
gi 446789542 180 AGH---RIVIEEFLD 191
Cdd:PRK00696 89 KGQpvnKVLVEEGAD 103
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
3.17e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 42.87 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 85 RAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQN--FTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLE 162
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDgpVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEA 175
|
90 100 110
....*....|....*....|....*....|..
gi 446789542 163 EAEAAVHdML---AGNAFGDAGhrIVIEEFLD 191
Cdd:PRK08591 176 ELEKAFS-MAraeAKAAFGNPG--VYMEKYLE 204
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-208 |
5.21e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 41.64 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 105 KAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKadglAAGKGVIVAMTLEEAEAAVHDMLAGNA-FGDaghR 183
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKVKEEDELQAALELAFkYDD---E 171
|
90 100
....*....|....*....|....*
gi 446789542 184 IVIEEFLDGEEasFIVMVDGEHVLP 208
Cdd:PRK01372 172 VLVEKYIKGRE--LTVAVLGGKALP 194
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
57-207 |
9.46e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 41.49 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 57 LDFAQNEKIDLTIV--GPEAPLvkGVVDTFRAAGLKIFGPTAGAA-QLEGSKAFTKdFLARHKIPTAEYQNFTEVEPALA 133
Cdd:PRK12815 623 LNVAEAENIKGVIVqfGGQTAI--NLAKGLEEAGLTILGTSPDTIdRLEDRDRFYQ-LLDELGLPHVPGLTATDEEEAFA 699
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446789542 134 YLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAavhdMLAGNAfgDAGHRIVIEEFLDGEEASFIVMVDGEHVL 207
Cdd:PRK12815 700 FAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEA----YLAENA--SQLYPILIDQFIDGKEYEVDAISDGEDVT 767
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-252 |
1.53e-03 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 39.60 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 128 VEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDML--AGNAFGDagHRIVIEEFLDG-EEASFIVMVDGE 204
Cdd:pfam02786 27 EEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALaeAPAAFGN--PQVLVEKSLKGpKHIEYQVLRDAH 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446789542 205 ----HVLPMATSqDHKRVGDKDTgpntggmgaYSPAPVVTDDVHQRTMERII 252
Cdd:pfam02786 105 gnciTVCNRECS-DQRRTQKSIE---------VAPSQTLTDEERQMLREAAV 146
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
109-191 |
1.71e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 39.55 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 109 KDFLARHKIPTAEYQNFTEVEPALAYLREKGAP-IVIKADGLAAGKG----VIVAMTLEEAEAAVHDMLAGN----AFGD 179
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRGkaggVKLAKSPEEAKEVAKEMLGKNlvtkQTGP 87
|
90
....*....|....*
gi 446789542 180 AGH---RIVIEEFLD 191
Cdd:pfam08442 88 DGQpvnKVLVEEALD 102
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
1.82e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 40.40 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 85 RAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPT--AEYQNFTEVEPALAYLREKGAPIVIKAdglAAGKGVIvAMTLE 162
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKA---SAGGGGI-GMQLV 171
|
90 100 110
....*....|....*....|....*....|....*
gi 446789542 163 EAEAAVHDMLAGN------AFGDAghRIVIEEFLD 191
Cdd:PRK06111 172 ETEQELTKAFESNkkraanFFGNG--EMYIEKYIE 204
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
113-204 |
2.02e-03 |
|
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: 38.77 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 113 ARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLA-AGKGVIVAMTLEEAEAAVHDMLAGnafgdaghRIVIEEFLD 191
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72
|
90
....*....|....*.
gi 446789542 192 GE-EASFIVM--VDGE 204
Cdd:pfam02222 73 FDrELSVLVVrsVDGE 88
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
1-290 |
3.28e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 39.63 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 1 MKVLVIGNG---GREHALAWKAAQSPLVETVFVA--PGNAGTALEPALQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAp 75
Cdd:PRK07206 2 MKKVVIVDPfssGKFLAPAFKKRGIEPIAVTSSCllDPYYYASFDTSDFIEVIINGDIDDLVEFLRKLGPEAIIAGAES- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 76 lvkGV--VDTFRAA-GLKIF-GPTAGAAQLEgsKAFTKDFLARHKIPTAEYQNFTEVEPALAYLRE---KGAPIVIKADG 148
Cdd:PRK07206 81 ---GVelADRLAEIlTPQYSnDPALSSARRN--KAEMINALAEAGLPAARQINTADWEEAEAWLREnglIDRPVVIKPLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 149 LAAGKGVIVAMTLEEAEAAVHDMLAG-NAFGDAGHRIVIEEFLDGEE-ASFIVMVDGEHVLPMATSQDHKRVGDkdtgpn 226
Cdd:PRK07206 156 SAGSDGVFICPAKGDWKHAFNAILGKaNKLGLVNETVLVQEYLIGTEyVVNFVSLDGNHLVTEIVRYHKTSLNS------ 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446789542 227 tgGMGAYSPAPVV--TDDVHQRtmeriIWPTVKG-MAAEGNTYtGFLYAGLMIDKQGnPKVIEFNCR 290
Cdd:PRK07206 230 --GSTVYDYDEFLdySEPEYQE-----LVDYTKQaLDALGIKN-GPAHAEVMLTADG-PRLIEIGAR 287
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
139-203 |
4.14e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 37.65 E-value: 4.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446789542 139 GAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLA--------GNAFGDAGHRIVIEEFLDGEEASfivmVDG 203
Cdd:pfam13535 2 PYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREeieqwkemYPEAVVDGGSFLVEEYIEGEEFA----VDA 70
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
105-194 |
4.56e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 39.37 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789542 105 KAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIK-ADGlAAGKGVIV-AMTLEEAEAAVHdmlAGNAFGDAgh 182
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKpLDG-NHGRGVTVnITTREEIEAAYA---VASKESSD-- 288
|
90
....*....|..
gi 446789542 183 rIVIEEFLDGEE 194
Cdd:PRK14016 289 -VIVERYIPGKD 299
|
|
| |
