|
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: 821.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 1 MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPTlqNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLAE--CVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 81 VDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 161 QEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVT 240
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 241 DEVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLD 320
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 321 EKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVAGGKVFHAGTKLTDDeQVVTSGGRVLCVTALGHTVAEAQKR 400
Cdd:COG0151 318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDG-KLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....*.
gi 446789600 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: 701.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 1 MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPTLQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGV 80
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 81 VDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 161 QEEAEAAVHDMLAGNaFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVT 240
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 241 DEVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLD 320
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 321 EKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVAGGKVFHAGTKLtDDEQVVTSGGRVLCVTALGHTVAEAQKR 400
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKA-DNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....*
gi 446789600 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: 589.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 4 LVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPTLQNVA-IGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGVVD 82
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 83 TFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQE 162
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 163 EAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDE 242
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 243 VHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQ-GNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLDE 321
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKsGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 322 KTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVA--GGKVFHAGTKLTDDEQVVTSGGRVLCVTALGHTVAEAQK 399
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420
....*....|....*....|....*....
gi 446789600 400 RAYALMTDIHWDDCFCRKDIGWRAIEREQ 428
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
103-296 |
3.95e-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: 319.61 E-value: 3.95e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 103 GSKAFTKDFLARHQIPTAEYQNFTEVEPALAYLREKGAPI-VIKADGLAAGKGVIVAMTQEEAEAAVHDMLAGNAFGDAG 181
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 182 HRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDEVHQRTMERIIWPTVKGMAA 261
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 446789600 262 EGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPET 296
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-102 |
6.06e-57 |
|
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: 182.56 E-value: 6.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 1 MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPTlqNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 446789600 81 VDTF--RAAGLKIFGPTAGAAQLE 102
Cdd:pfam02844 79 VDALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-422 |
4.37e-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: 146.05 E-value: 4.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 331 SLGVVMAAGGYPGDYRTGDVIHGLpleEVAGGKVFHAGTKLtDDEQVVTSGGRVLCVTALGHTVAEAQKRAYALMTDIHW 410
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGL---DEAGVKVFHAGTKL-KDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDF 76
|
90
....*....|..
gi 446789600 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 |
1.04e-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: 93.78 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 86 AAGLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEEAE 165
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 166 AAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKrvgdkdTGPNTGGMGAYSPAPvVTDEVHQ 245
Cdd:COG0439 116 AALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELRA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446789600 246 RTMERiiwpTVKGMAAEGNTYtGFLYAGLMIDKQGNPKVIEFNCRFGDpETQPIMLRMKS--DLVELCLAACEGK 318
Cdd:COG0439 189 EIGEL----VARALRALGYRR-GAFHTEFLLTPDGEPYLIEINARLGG-EHIPPLTELATgvDLVREQIRLALGE 257
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-209 |
2.23e-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: 55.11 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 105 KAFTKDFLARHQIPTAEYQNFTEVEPALAYLREK--GAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLAGnafgdaGH 182
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEelGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100
....*....|....*....|....*...
gi 446789600 183 RIVIEEFLDGEEASFIVMVDGE-HVLPM 209
Cdd:COG1181 170 KVLVEEFIDGREVTVGVLGNGGpRALPP 197
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
109-206 |
2.99e-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: 55.08 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 109 KDFLARHQIPTAEYQNFTEVEPALAYLREKGAPIVIKA-----DglaaGKGVIVAMTQEEAEAAVHDMlagnafgdAGHR 183
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90 100
....*....|....*....|....*.
gi 446789600 184 IVIEEFLDGE-EASFIVM--VDGEHV 206
Cdd:COG0026 162 CILEEFVPFErELSVIVArsPDGEVA 187
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
1-206 |
4.68e-08 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 54.77 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 1 MKVLVIGNG--GREHALAwkaAQsPL-VETVFVAPGNAGTALEPTLQNVAIGVTDIPALLDFAQ--------NEKIDLTI 69
Cdd:PRK06019 3 KTIGIIGGGqlGRMLALA---AA-PLgYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEqcdvityeFENVPAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 70 VGPEAPLVKGVVdtfraaGLKIFGPTAgaaqlegSKAFTKDFLARHQIPTAEYQNFTEVEPALAYLREKGAPIVIKA--- 146
Cdd:PRK06019 79 LDALAARVPVPP------GPDALAIAQ-------DRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrg 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446789600 147 --DglaaGKGVIVAMTQEEAEAAVHDMLAGNAfgdaghriVIEEFLDGE-EASFIVM--VDGEHV 206
Cdd:PRK06019 146 gyD----GKGQWVIRSAEDLEAAWALLGSVPC--------ILEEFVPFErEVSVIVArgRDGEVV 198
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
79-288 |
4.95e-08 |
|
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: 54.18 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 79 GVVDTFRAAGLKIFGPTAgAAQLEGSKAFTKDFLARHQIPTAEyqnfTEV----EPALAYLREKGAPIVIK-ADGlAAGK 153
Cdd:COG0189 72 ALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPP----TLVtrdpDDLRAFLEELGGPVVLKpLDG-SGGR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 154 GVIVAMTQEEAEAAVHDMlagnaFGDAGHRIVIEEFLDGEEASF--IVMVDGEHVLPMA--TSQDHKRVgdkdtgpNTGG 229
Cdd:COG0189 146 GVFLVEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDirVLVVGGEPVAAIRriPAEGEFRT-------NLAR 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 230 MGAYSPAPvVTDEVHQrtmeriiwptvkgMAAEGNTYTGFLYAGL-MIDKQGNPKVIEFN 288
Cdd:COG0189 214 GGRAEPVE-LTDEERE-------------LALRAAPALGLDFAGVdLIEDDDGPLVLEVN 259
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
50-292 |
3.50e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 51.81 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 50 VTD---IPALLDFAQNEKIDLTIVG--PEAPLVKGVVDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQN 124
Cdd:PRK12767 52 VTDpnyIDRLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 125 FTEVEPALAYLREK--GAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLAgnafgdaghrIVIEEFLDGEEASFIVMVD 202
Cdd:PRK12767 132 PESLEDFKAALAKGelQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPN----------LIIQEFIEGQEYTVDVLCD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 203 --GEHV--LPMatsqdhKRVGDKDtgpntggmGAYSPAPVVTDEVHQRTMERIiwptVKGMAAEGNtytgflyagLMID- 277
Cdd:PRK12767 202 lnGEVIsiVPR------KRIEVRA--------GETSKGVTVKDPELFKLAERL----AEALGARGP---------LNIQc 254
|
250
....*....|....*..
gi 446789600 278 --KQGNPKVIEFNCRFG 292
Cdd:PRK12767 255 fvTDGEPYLFEINPRFG 271
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
53-292 |
5.56e-07 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 51.47 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 53 IPALLDFAQNEKIDLtIVGPEAPLVKgVVDTFRA---AGLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQNFTEVE 129
Cdd:COG3919 65 VDALLELAERHGPDV-LIPTGDEYVE-LLSRHRDeleEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSAD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 130 PALAYLREKGAPIVIK-ADGLAA-------GKGVIVAMTQEEAEAAVHDMLagnafgDAGHRIVIEEFL---DGEEASFI 198
Cdd:COG3919 143 DLDALAEDLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRIA------AAGYELIVQEYIpgdDGEMRGLT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 199 VMVDGEHVLPMATSQdHKRVGDkdtgPNTGGmgayspAPVVTDEVHQRTMERIiwpTVKGMAAEGntYTGFLYAGLMID- 277
Cdd:COG3919 217 AYVDRDGEVVATFTG-RKLRHY----PPAGG------NSAARESVDDPELEEA---ARRLLEALG--YHGFANVEFKRDp 280
|
250
....*....|....*
gi 446789600 278 KQGNPKVIEFNCRFG 292
Cdd:COG3919 281 RDGEYKLIEINPRFW 295
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
86-207 |
1.30e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 47.06 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 86 AAGLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQN--FTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEE 163
Cdd:PRK12833 100 AAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDgvVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQ 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446789600 164 --AEAAVHDMLAGNAFGDAGhrIVIEEFLdgEEASFI---VMVDGEHVL 207
Cdd:PRK12833 180 laAELPLAQREAQAAFGDGG--VYLERFI--ARARHIevqILGDGERVV 224
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
103-294 |
2.06e-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: 44.68 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 103 GSKAFTKDFLARHQIPTAEYQNFTEvepalayLREKGAPIVIK-ADGlAAGKGVIVAMTQEEAEAAVHDMLagnafgdag 181
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTPETLQAEE-------LLREEKKYVVKpRDG-CGGEGVRKVENGREDEAFIENVL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 182 hrivIEEFLDGEEASFIVMVDGEHVLPMATSqdhKRVGDKDTGPN--TGGMgaySPAPVVTDEVHQRTMERII--WPTVK 257
Cdd:pfam02655 65 ----VQEFIEGEPLSVSLLSDGEKALPLSVN---RQYIDNGGSGFvyAGNV---TPSRTELKEEIIELAEEVVecLPGLR 134
|
170 180 190
....*....|....*....|....*....|....*..
gi 446789600 258 GMAAEgntytgflyaGLMIDKQGnPKVIEFNCRFGDP 294
Cdd:pfam02655 135 GYVGV----------DLVLKDNE-PYVIEVNPRITTS 160
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
57-290 |
3.96e-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: 46.15 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 57 LDFAQNEKIDLTIV--GPEAPLvkGVVDTFRAAGLKIFGpTAGAA--QLEGSKAFTKdFLARHQIPTAEYQNFTEVEPAL 132
Cdd:TIGR01369 622 MNIIELEKPEGVIVqfGGQTPL--NLAKALEEAGVPILG-TSPESidRAEDREKFSE-LLDELGIPQPKWKTATSVEEAV 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 133 AYLREKGAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLAGNafgdAGHRIVIEEFL-DGEEASFIVMVDGEHVLPMAT 211
Cdd:TIGR01369 698 EFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVS----PEHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGI 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 212 SQDHKRvgdkdTGPNTGGMGAYSPAPVVTDEVHQRtMERIiwptVKGMAAEGNtytgflYAGLM----IDKQGNPKVIEF 287
Cdd:TIGR01369 774 MEHIEE-----AGVHSGDSTCVLPPQTLSAEIVDR-IKDI----VRKIAKELN------VKGLMniqfAVKDGEVYVIEV 837
|
...
gi 446789600 288 NCR 290
Cdd:TIGR01369 838 NPR 840
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
105-204 |
1.07e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 44.53 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 105 KAFTKDFLARHQIPTAEYQNFTEVEPALAYLRE-KGAPIVIKADGLAAGKGVIVamTQEEAEAAVHDMLAGNAFGDAGHr 183
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISI--FKEPASLEDYEKALEIAFREDSS- 565
|
90 100
....*....|....*....|.
gi 446789600 184 IVIEEFLDGEEASFIVMvDGE 204
Cdd:PRK02471 566 VLVEEFIVGTEYRFFVL-DGK 585
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
40-207 |
1.55e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 44.19 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 40 EP-TLQNVaigvtdipalLDFAQNEKIDLTIV--GPEAPLvkGVVDTFRAAGLKIFGPTAGAA-QLEGSKAFTKdFLARH 115
Cdd:PRK12815 615 EPlTLEDV----------LNVAEAENIKGVIVqfGGQTAI--NLAKGLEEAGLTILGTSPDTIdRLEDRDRFYQ-LLDEL 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 116 QIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEEAEAavhdMLAGNAfgDAGHRIVIEEFLDGEEA 195
Cdd:PRK12815 682 GLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEA----YLAENA--SQLYPILIDQFIDGKEY 755
|
170
....*....|..
gi 446789600 196 SFIVMVDGEHVL 207
Cdd:PRK12815 756 EVDAISDGEDVT 767
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
1-290 |
1.67e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 43.48 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 1 MKVLVIGNG---GREHALAWKAAQSPLVETVFVA--PGNAGTALEPTLQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAp 75
Cdd:PRK07206 2 MKKVVIVDPfssGKFLAPAFKKRGIEPIAVTSSCllDPYYYASFDTSDFIEVIINGDIDDLVEFLRKLGPEAIIAGAES- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 76 lvkGV--VDTFRAA-GLKIF-GPTAGAAQLEgsKAFTKDFLARHQIPTAEYQNFTEVEPALAYLRE---KGAPIVIKADG 148
Cdd:PRK07206 81 ---GVelADRLAEIlTPQYSnDPALSSARRN--KAEMINALAEAGLPAARQINTADWEEAEAWLREnglIDRPVVIKPLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 149 LAAGKGVIVAMTQEEAEAAVHDMLAG-NAFGDAGHRIVIEEFLDGEE-ASFIVMVDGEHVLPMATSQDHKRVGDkdtgpn 226
Cdd:PRK07206 156 SAGSDGVFICPAKGDWKHAFNAILGKaNKLGLVNETVLVQEYLIGTEyVVNFVSLDGNHLVTEIVRYHKTSLNS------ 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446789600 227 tgGMGAYSP---APVVTDEVHQrtmeriIWPTVKG-MAAEGNTYtGFLYAGLMIDKQGnPKVIEFNCR 290
Cdd:PRK07206 230 --GSTVYDYdefLDYSEPEYQE------LVDYTKQaLDALGIKN-GPAHAEVMLTADG-PRLIEIGAR 287
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
2.93e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 42.87 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 85 RAAGLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQN--FTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQE 162
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDgpVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEA 175
|
90 100 110
....*....|....*....|....*....|..
gi 446789600 163 EAEAAVHdML---AGNAFGDAGhrIVIEEFLD 191
Cdd:PRK08591 176 ELEKAFS-MAraeAKAAFGNPG--VYMEKYLE 204
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
109-191 |
4.49e-04 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 42.38 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 109 KDFLARHQIPTAEYQNFTEVEPALAYLRE-KGAPIVIKADGLAAGK----GVIVAMTQEEAEAAVHDML----AGNAFGD 179
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQILgmtlVTHQTGP 88
|
90
....*....|....*
gi 446789600 180 AGH---RIVIEEFLD 191
Cdd:PRK00696 89 KGQpvnKVLVEEGAD 103
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
109-252 |
5.93e-04 |
|
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: 40.75 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 109 KDFLARHQIPTAEYQ--NFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDML--AGNAFGDagHRI 184
Cdd:pfam02786 6 KAAMKEAGVPTVPGTagPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALaeAPAAFGN--PQV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446789600 185 VIEEFLDG-EEASFIVMVDGE----HVLPMATSqDHKRVGDKDTgpntggmgaYSPAPVVTDEVHQRTMERII 252
Cdd:pfam02786 84 LVEKSLKGpKHIEYQVLRDAHgnciTVCNRECS-DQRRTQKSIE---------VAPSQTLTDEERQMLREAAV 146
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
139-293 |
7.36e-04 |
|
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: 39.96 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 139 GAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLA--------GNAFGDAGHRIVIEEFLDGEEASFIVMVD--GEHVLp 208
Cdd:pfam13535 2 PYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREeieqwkemYPEAVVDGGSFLVEEYIEGEEFAVDAYFDenGEPVI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 209 maTSQDHKRvgdkdtgpntggmgaYSPAPVVTDEVHQrTMERIIWPTVKGMA---AEGNTYTGF----LYAGLMIDKQGN 281
Cdd:pfam13535 81 --LNILKHD---------------FASSEDVSDRIYV-TSASIIRETQAAFTeflKRINALLGLknfpVHIELRVDEDGQ 142
|
170
....*....|...
gi 446789600 282 PKVIEFN-CRFGD 293
Cdd:pfam13535 143 IIPIEVNpLRFAG 155
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
105-194 |
1.82e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.52 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 105 KAFTKDFLARHQIPTAEYQNFTEVEPALAYLREKGAPIVIK-ADGlAAGKGVIV-AMTQEEAEAAVHdmlAGNAFGDAgh 182
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKpLDG-NHGRGVTVnITTREEIEAAYA---VASKESSD-- 288
|
90
....*....|..
gi 446789600 183 rIVIEEFLDGEE 194
Cdd:PRK14016 289 -VIVERYIPGKD 299
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
113-204 |
2.03e-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: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 113 ARHQIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLA-AGKGVIVAMTQEEAEAAVHDMLAGnafgdaghRIVIEEFLD 191
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72
|
90
....*....|....*.
gi 446789600 192 GE-EASFIVM--VDGE 204
Cdd:pfam02222 73 FDrELSVLVVrsVDGE 88
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
109-191 |
2.11e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 39.17 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 109 KDFLARHQIPTAEYQNFTEVEPALAYLREKGAP-IVIKADGLAAGKG----VIVAMTQEEAEAAVHDMLAGN----AFGD 179
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRGkaggVKLAKSPEEAKEVAKEMLGKNlvtkQTGP 87
|
90
....*....|....*
gi 446789600 180 AGH---RIVIEEFLD 191
Cdd:pfam08442 88 DGQpvnKVLVEEALD 102
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-208 |
2.51e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 39.71 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 105 KAFTKDFLARHQIPTAEYQNFTEVEPALAYLREKGAPIVIKAdgLAAGK--GVIVAMTQEEAEAAVHDMLagnAFGDagh 182
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAF---KYDD--- 170
|
90 100
....*....|....*....|....*.
gi 446789600 183 RIVIEEFLDGEEasFIVMVDGEHVLP 208
Cdd:PRK01372 171 EVLVEKYIKGRE--LTVAVLGGKALP 194
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
88-318 |
4.97e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 38.96 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 88 GLKIFGPTAGAAQLEGSKAFTKDFLARHQIPTAEYQN--FTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEEAE 165
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDgaLKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 166 ----AAVHDMLAgnAFGDAghRIVIEEFLD----------GEEASFIVMVdGEHVLPMatSQDHKRVGDKdtgpntggmg 231
Cdd:PRK08462 181 nlylAAESEALS--AFGDG--TMYMEKFINnprhievqilGDKHGNVIHV-GERDCSL--QRRHQKLIEE---------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446789600 232 aySPAPVVTDEVHQRTMEriiwptvkgMAAEGNTYTGFLYAG---LMIDKQGNPKVIEFNCRFgdpETQPIMLRMKS--D 306
Cdd:PRK08462 244 --SPAVVLDEKTRERLHE---------TAIKAAKAIGYEGAGtfeFLLDSNLDFYFMEMNTRL---QVEHTVSEMVSglD 309
|
250
....*....|..
gi 446789600 307 LVELCLAACEGK 318
Cdd:PRK08462 310 LIEWMIKIAEGE 321
|
|
| |
