|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
1-425 |
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: 805.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 1 MKILVIGNGGREHALAWKAAQSPLAETVFVAPGNAGTALEPalQNVDISPTDIPALLAFAQREAIDLTIVGPEAPLVIGV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA--ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 81 VDAFRAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 161 LEEAEAAVKDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGKNVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVT 240
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 241 DEIHQRVMDQVIWPTVRGMAAEGNVYTGFLYAGLMIDQSGqPKVIEFNCRFGDPETQPIMLRLQSDLVELCLAACDGALD 320
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 321 QKHSAWDPRPALGVVLAAGGYPGDYVNGEQIHGLPLEEVADGKVFHAGTRLDNDLVLTNGGRVLCVTALGDDVAAAQKRA 400
Cdd:COG0151 318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARERA 397
|
410 420
....*....|....*....|....*
gi 1487854209 401 YELAQPISWNGSFCRRDIGYRAINR 425
Cdd:COG0151 398 YEAVEKIRFEGMFYRRDIGWRALKR 422
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
1-423 |
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: 679.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 1 MKILVIGNGGREHALAWKAAQSPLAETVFVAPGNAGTALEPALQNVDISPTDIPALLAFAQREAIDLTIVGPEAPLVIGV 80
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 81 VDAFRAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 161 LEEAEAAVKDMLAGNaFGDAGHRIVIEEFLDGEEASFIVMVDGKNVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVT 240
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 241 DEIHQRVMDQVIWPTVRGMAAEGNVYTGFLYAGLMIDQSGqPKVIEFNCRFGDPETQPIMLRLQSDLVELCLAACDGALD 320
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 321 QKHSAWDPRPALGVVLAAGGYPGDYVNGEQIHGLPLEEVADGKVFHAGTRLDNDLVLTNGGRVLCVTALGDDVAAAQKRA 400
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 1487854209 401 YELAQPISWNGSFCRRDIGYRAI 423
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
4-426 |
0e+00 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 594.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 4 LVIGNGGREHALAWKAAQSPLAETVFVAPGNAGTALEPALQNV-DISPTDIPALLAFAQREAIDLTIVGPEAPLVIGVVD 82
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVpDLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 83 AFRAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKADGLAAGKGVIVAMTLE 162
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 163 EAEAAVKDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGKNVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVTDE 242
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 243 IHQRVMDQVIWPTVRGMAAEGNVYTGFLYAGLMID-QSGQPKVIEFNCRFGDPETQPIMLRLQSDLVELCLAACDGALDQ 321
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEkKSGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 322 KHSAWDPRPALGVVLAAGGYPGDYVNGEQIHGL-PLEEVADG-KVFHAGTRLDND-LVLTNGGRVLCVTALGDDVAAAQK 398
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLdEAEAVAPGvKVFHAGTALDSDgNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420
....*....|....*....|....*...
gi 1487854209 399 RAYELAQPISWNGSFCRRDIGYRAINRK 426
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARL 428
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
103-296 |
9.61e-111 |
|
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: 323.46 E-value: 9.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 103 GSKAFTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPI-VIKADGLAAGKGVIVAMTLEEAEAAVKDMLAGNAFGDAG 181
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 182 HRIVIEEFLDGEEASFIVMVDGKNVLPMATSQDHKRVGDGDTGPNTGGMGAYSPAPVVTDEIHQRVMDQVIWPTVRGMAA 261
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1487854209 262 EGNVYTGFLYAGLMIDQSGqPKVIEFNCRFGDPET 296
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-102 |
3.71e-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: 3.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 1 MKILVIGNGGREHALAWKAAQSPLAETVFVAPGNAGTALEPalQNVDISPTDIPALLAFAQREAIDLTIVGPEAPLVIGV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLA--ECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 1487854209 81 VDAF--RAAGLKIFGPTKNAAQLE 102
Cdd:pfam02844 79 VDALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-421 |
1.08e-39 |
|
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: 137.19 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 331 ALGVVLAAGGYPGDYVNGEQIHGLpleEVADGKVFHAGTRLDNDLVLTNGGRVLCVTALGDDVAAAQKRAYELAQPISWN 410
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGL---DEAGVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|.
gi 1487854209 411 GSFCRRDIGYR 421
Cdd:pfam02843 78 GMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
52-292 |
2.85e-24 |
|
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: 101.10 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 52 DIPALLAFAQREAIDLTIVGpeaplVIGVVD------AFRAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRNF 125
Cdd:COG0439 1 DIDAIIAAAAELARETGIDA-----VLSESEfavetaAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 126 TDVEVALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVKDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGKN 205
Cdd:COG0439 76 DSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 206 VLPMATSQDHKrvgdgdTGPNTGGMGAYSPAPvVTDEIHQRVMDQViwptVRGMAAEGnVYTGFLYAGLMIDQSGQPKVI 285
Cdd:COG0439 156 VVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELRAEIGELV----ARALRALG-YRRGAFHTEFLLTPDGEPYLI 223
|
....*..
gi 1487854209 286 EFNCRFG 292
Cdd:COG0439 224 EINARLG 230
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
109-199 |
1.15e-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: 56.24 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 109 KDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKA-----DglaaGKGVIVAMTLEEAEAAVKDMlagnafgdAGHR 183
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90
....*....|....*..
gi 1487854209 184 IVIEEFLDGE-EASFIV 199
Cdd:COG0026 162 CILEEFVPFErELSVIV 178
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-194 |
2.25e-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: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 105 KAFTKDFLARHHIPTAEYRNFTDVEVALAYLREK--GAPIVIKADGLAAGKGVIVAMTLEEAEAAVKDMLAGnafgdaGH 182
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEelGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90
....*....|..
gi 1487854209 183 RIVIEEFLDGEE 194
Cdd:COG1181 170 KVLVEEFIDGRE 181
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
1-199 |
4.79e-08 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 54.77 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 1 MKILVIGNG--GREHALAwkAAQSPLaETVFVAPGNAGTALEPALQNVDISPTDIPALLAFAQR--------EAIDLTIV 70
Cdd:PRK06019 3 KTIGIIGGGqlGRMLALA--AAPLGY-KVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEQcdvityefENVPAEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 71 GPEAPLVigvvdaFRAAGLKIFGPTKNaaqlegsKAFTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKA---- 146
Cdd:PRK06019 80 DALAARV------PVPPGPDALAIAQD-------RLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrrgg 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1487854209 147 -DglaaGKGVIVAMTLEEAEAAVKDMLAGNAfgdaghriVIEEFLDGE-EASFIV 199
Cdd:PRK06019 147 yD----GKGQWVIRSAEDLEAAWALLGSVPC--------ILEEFVPFErEVSVIV 189
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
79-288 |
5.16e-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: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 79 GVVDAFRAAGLKIFGPTkNAAQLEGSKAFTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIK-ADGlAAGKGVIV 157
Cdd:COG0189 72 ALLRQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKpLDG-SGGRGVFL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 158 AMTLEEAEAAVKDMlagnaFGDAGHRIVIEEFLDGEEASF--IVMVDGKNVLPMA--TSQDHKRVgdgdtgpNTGGMGAY 233
Cdd:COG0189 150 VEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDirVLVVGGEPVAAIRriPAEGEFRT-------NLARGGRA 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1487854209 234 SPAPvVTDEIHQrvmdqviwpTVRGMAAEgnvyTGFLYAGL-MIDQSGQPKVIEFN 288
Cdd:COG0189 218 EPVE-LTDEERE---------LALRAAPA----LGLDFAGVdLIEDDDGPLVLEVN 259
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
57-252 |
3.33e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 52.66 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 57 LAFAQREAIDLTIVGPEAPLVIGVVDAFRAAGLKIFGPTKNAA-QLEGSKAFTKdFLARHHIPTAEYRNFTDVEVALAYL 135
Cdd:PRK12815 623 LNVAEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIdRLEDRDRFYQ-LLDELGLPHVPGLTATDEEEAFAFA 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 136 REKGAPIVIKADGLAAGKGVIVAMTleeaEAAVKDMLAGNAfgDAGHRIVIEEFLDGEEASFIVMVDGKNVLpMATSQDH 215
Cdd:PRK12815 702 KRIGYPVLIRPSYVIGGQGMAVVYD----EPALEAYLAENA--SQLYPILIDQFIDGKEYEVDAISDGEDVT-IPGIIEH 774
|
170 180 190
....*....|....*....|....*....|....*..
gi 1487854209 216 KRvgdgDTGPNTGGMGAYSPAPVVTDEIHQRVMDQVI 252
Cdd:PRK12815 775 IE----QAGVHSGDSIAVLPPQSLSEEQQEKIRDYAI 807
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
53-367 |
4.17e-07 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 51.85 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 53 IPALLAFAQREAIDLTI-VGPEAPLVIGVVDAFRAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRNFTDVEVA 131
Cdd:COG3919 65 VDALLELAERHGPDVLIpTGDEYVELLSRHRDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 132 LAYLREKGAPIVIK-ADGLAA-------GKGVIVAMTLEEAEAAVKDMLagnafgDAGHRIVIEEFL---DGEEASFIVM 200
Cdd:COG3919 145 DALAEDLGFPVVVKpADSVGYdelsfpgKKKVFYVDDREELLALLRRIA------AAGYELIVQEYIpgdDGEMRGLTAY 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 201 VD--GKnvlPMATSQDHKRVGDgdtgPNTGGMGAYspapVVTDEiHQRVMDQVIwptvRGMAAEGnvYTGFLYAGLMID- 277
Cdd:COG3919 219 VDrdGE---VVATFTGRKLRHY----PPAGGNSAA----RESVD-DPELEEAAR----RLLEALG--YHGFANVEFKRDp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 278 QSGQPKVIEFNCRFGdpetqpimlrLQSDL-----VELCLAACDGALDQKH-SAWDPRPALGVVLAAGGYPGDYVNGEQI 351
Cdd:COG3919 281 RDGEYKLIEINPRFW----------RSLYLataagVNFPYLLYDDAVGRPLePVPAYREGVLWRVLPGDLLLRYLRDGEL 350
|
330
....*....|....*.
gi 1487854209 352 HGLPLEEVADGKVFHA 367
Cdd:COG3919 351 RKRLRELLRRGKVVDA 366
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-194 |
1.68e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 49.50 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 1 MKILVIGNGGReHALAwKAAQSPLAE-TVFVAPGNAgtaLEPALQNVD---ISP--TD---IPALLAFAQREAIDLTIVG 71
Cdd:PRK12767 2 MNILVTSAGRR-VQLV-KALKKSLLKgRVIGADISE---LAPALYFADkfyVVPkvTDpnyIDRLLDICKKEKIDLLIPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 72 --PEAPLVIGVVDAFRAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRNFTDVEVALAYLREK--GAPIVIKAD 147
Cdd:PRK12767 77 idPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGelQFPLFVKPR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1487854209 148 GLAAGKGVIVAMTLEEAEAAVKDMLAgnafgdaghrIVIEEFLDGEE 194
Cdd:PRK12767 157 DGSASIGVFKVNDKEELEFLLEYVPN----------LIIQEFIEGQE 193
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
105-204 |
2.84e-06 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 49.54 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 105 KAFTKDFLARHHIPTAEYRNFTDVEVALAYLRE-KGAPIVIKADGLAAGKGVIV---AMTLEEAEAAVKdmlagNAFGDA 180
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISIfkePASLEDYEKALE-----IAFRED 563
|
90 100
....*....|....*....|....
gi 1487854209 181 GHrIVIEEFLDGEEASFIVMvDGK 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 |
1.69e-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: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 103 GSKAFTKDFLARHHIPTAEYRNFTDvevalayLREKGAPIVIK-ADGlAAGKGVIVAMTLEEAEAAVKDMLagnafgdag 181
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTPETLQAEE-------LLREEKKYVVKpRDG-CGGEGVRKVENGREDEAFIENVL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 182 hrivIEEFLDGEEASFIVMVDGKNVLPMATSQDHKRVGdGDTGPNTGGMgaySPAPVVTDEIHQRVMDQVI--WPTVRGM 259
Cdd:pfam02655 65 ----VQEFIEGEPLSVSLLSDGEKALPLSVNRQYIDNG-GSGFVYAGNV---TPSRTELKEEIIELAEEVVecLPGLRGY 136
|
170 180 190
....*....|....*....|....*....|....*
gi 1487854209 260 AAEGNVYTGflyaglmidqsGQPKVIEFNCRFGDP 294
Cdd:pfam02655 137 VGVDLVLKD-----------NEPYVIEVNPRITTS 160
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
109-191 |
1.94e-05 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 46.62 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 109 KDFLARHHIPTAEYRNFTDVEVALAYLRE-KGAPIVIKADGLAAGK----GVIVAMTLEEAEAAVKDML----AGNAFGD 179
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQILgmtlVTHQTGP 88
|
90
....*....|....*
gi 1487854209 180 AGH---RIVIEEFLD 191
Cdd:PRK00696 89 KGQpvnKVLVEEGAD 103
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
109-290 |
4.55e-05 |
|
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: 44.22 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 109 KDFLARHHIPTAE--YRNFTDVEVALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVKDML--AGNAFGDagHRI 184
Cdd:pfam02786 6 KAAMKEAGVPTVPgtAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALaeAPAAFGN--PQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 185 VIEEFLDG-EEASFIVMVDGK-NVLPMATSQ--DHKRVGDGDTgpntggmgaYSPAPVVTDEIHQRVMDQVIwPTVR--G 258
Cdd:pfam02786 84 LVEKSLKGpKHIEYQVLRDAHgNCITVCNREcsDQRRTQKSIE---------VAPSQTLTDEERQMLREAAV-KIARhlG 153
|
170 180 190
....*....|....*....|....*....|..
gi 1487854209 259 MAAEGNVYtgFLYAglmiDQSGQPKVIEFNCR 290
Cdd:pfam02786 154 YVGAGTVE--FALD----PFSGEYYFIEMNTR 179
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
87-190 |
5.98e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 45.36 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 87 AGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRN--FTDVEVALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEA 164
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEegIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEEL 177
|
90 100
....*....|....*....|....*...
gi 1487854209 165 EAAVKDM--LAGNAFGDAghRIVIEEFL 190
Cdd:PRK08654 178 EDAIESTqsIAQSAFGDS--TVFIEKYL 203
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
109-213 |
1.12e-04 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 43.02 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 109 KDFLARHHIPTAEYRNFTDVEVALAYLREKGAP-IVIKADGLAAGKG----VIVAMTLEEAEAAVKDMLAGN----AFGD 179
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRGkaggVKLAKSPEEAKEVAKEMLGKNlvtkQTGP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1487854209 180 AGH---RIVIEEFLD-GEEASFIVMVD--GKNVLPMATSQ 213
Cdd:pfam08442 88 DGQpvnKVLVEEALDiKKEYYLSIVLDraSKGPVIIASTE 127
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
82-207 |
1.35e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 43.98 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 82 DAFRAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRN--FTDVEVALAYLREKGAPIVIKADGLAAGKGVIVAM 159
Cdd:PRK12833 96 EAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDgvVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAH 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1487854209 160 TLEE--AEAAVKDMLAGNAFGDAGhrIVIEEFLdgEEASFI---VMVDGKNVL 207
Cdd:PRK12833 176 DAAQlaAELPLAQREAQAAFGDGG--VYLERFI--ARARHIevqILGDGERVV 224
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
109-191 |
2.94e-04 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 42.73 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 109 KDFLARHHIPTAEYRNFTDVEVALAYLRE-KGAPIVIKADGLAAGK----GVIVAMTLEEAEAAVKDML----AGNAFGD 179
Cdd:COG0045 9 KELLAKYGVPVPRGIVATTPEEAVAAAEElGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEILgmtlVTHQTGP 88
|
90
....*....|....*
gi 1487854209 180 AGH---RIVIEEFLD 191
Cdd:COG0045 89 KGKpvnKVLVEEGVD 103
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
4.04e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 42.48 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 85 RAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPTAEYRN--FTDVEVALAYLREKGAPIVIKADGLAAGKGVIVAMTLE 162
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDgpVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEA 175
|
90 100 110
....*....|....*....|....*....|..
gi 1487854209 163 EAEAAVKdML---AGNAFGDAGhrIVIEEFLD 191
Cdd:PRK08591 176 ELEKAFS-MAraeAKAAFGNPG--VYMEKYLE 204
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-194 |
4.35e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 42.02 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 105 KAFTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKadglAAGKGVIVAMTLEEAEAAVKDMLAGNA-FGDaghR 183
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVK----PAREGSSVGVSKVKEEDELQAALELAFkYDD---E 171
|
90
....*....|.
gi 1487854209 184 IVIEEFLDGEE 194
Cdd:PRK01372 172 VLVEKYIKGRE 182
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
107-290 |
4.65e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 42.65 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 107 FTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVKDMLAGNAFgdagHRIVI 186
Cdd:PRK12815 131 RFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPI----HQCLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 187 EEFLDG-EEASFIVMVDGK----------NVLPMatsqdhkrvgdgdtGPNTGGMGAYSPAPVVTDEIHQRVMDqviwpT 255
Cdd:PRK12815 207 EESIAGwKEIEYEVMRDRNgncitvcnmeNIDPV--------------GIHTGDSIVVAPSQTLTDDEYQMLRS-----A 267
|
170 180 190
....*....|....*....|....*....|....*.
gi 1487854209 256 VRGMAAEGNVyTGFLYAGLMIDQ-SGQPKVIEFNCR 290
Cdd:PRK12815 268 SLKIISALGV-VGGCNIQFALDPkSKQYYLIEVNPR 302
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
105-206 |
7.79e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 41.68 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 105 KAFTKDFLARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKA-DGlAAGKGVIV-AMTLEEAEAAVKdmlAGNAFGDAgh 182
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPlDG-NHGRGVTVnITTREEIEAAYA---VASKESSD-- 288
|
90 100
....*....|....*....|....
gi 1487854209 183 rIVIEEFLDGEEASFIVmVDGKNV 206
Cdd:PRK14016 289 -VIVERYIPGKDHRLLV-VGGKLV 310
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
113-204 |
8.34e-04 |
|
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: 39.93 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 113 ARHHIPTAEYRNFTDVEVALAYLREKGAPIVIKADGLA-AGKGVIVAMTLEEAEAAVKDMLAGnafgdaghRIVIEEFLD 191
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72
|
90
....*....|....*.
gi 1487854209 192 GE-EASFIVM--VDGK 204
Cdd:pfam02222 73 FDrELSVLVVrsVDGE 88
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
139-293 |
1.45e-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: 39.19 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 139 GAPIVIKADGLAAGKGVIVAMTLEEAEAAVKDMLA--------GNAFGDAGHRIVIEEFLDGEEASfivmVDG---KNVL 207
Cdd:pfam13535 2 PYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREeieqwkemYPEAVVDGGSFLVEEYIEGEEFA----VDAyfdENGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 208 PMATSQDHKRvgdgdtgpntggmgaYSPAPVVTDEIH---QRVMDQVIWP---TVRGMAAEGNVYTGFLYAGLMIDQSGQ 281
Cdd:pfam13535 78 PVILNILKHD---------------FASSEDVSDRIYvtsASIIRETQAAfteFLKRINALLGLKNFPVHIELRVDEDGQ 142
|
170
....*....|...
gi 1487854209 282 PKVIEFN-CRFGD 293
Cdd:pfam13535 143 IIPIEVNpLRFAG 155
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
2.73e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 40.01 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 85 RAAGLKIFGPTKNAAQLEGSKAFTKDFLARHHIPT--AEYRNFTDVEVALAYLREKGAPIVIKAdglAAGKGVIvAMTLE 162
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpGITTNLEDAEEAIAIARQIGYPVMLKA---SAGGGGI-GMQLV 171
|
90 100 110
....*....|....*....|....*....|....*
gi 1487854209 163 EAEAAVKDMLAGN------AFGDAghRIVIEEFLD 191
Cdd:PRK06111 172 ETEQELTKAFESNkkraanFFGNG--EMYIEKYIE 204
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
112-290 |
8.73e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 38.09 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 112 LARHHIPTAEYRNFTDVEVALAYLRE---KGAPIVIKADGLAAGKGVIVAMTLEEAEAAVKDMLA-GNAFGDAGHRIVIE 187
Cdd:PRK07206 116 LAEAGLPAARQINTADWEEAEAWLREnglIDRPVVIKPLESAGSDGVFICPAKGDWKHAFNAILGkANKLGLVNETVLVQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487854209 188 EFLDGEE-ASFIVMVDGKNVLPMATSQDHKRVGDgdtgpntgGMGAYS-------PAPVVtdeihqrvmdQVIWPTVRGM 259
Cdd:PRK07206 196 EYLIGTEyVVNFVSLDGNHLVTEIVRYHKTSLNS--------GSTVYDydefldySEPEY----------QELVDYTKQA 257
|
170 180 190
....*....|....*....|....*....|.
gi 1487854209 260 AAEGNVYTGFLYAGLMIDQSGqPKVIEFNCR 290
Cdd:PRK07206 258 LDALGIKNGPAHAEVMLTADG-PRLIEIGAR 287
|
|
| |
