|
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: 806.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 1 MKVLVIGNGGREHALAWKAAQSPLVDTVFVAPGNAGTALEPalQNVAIGVTDIPALLSFAQNEKIDLTIVGPEAPLVIGV 80
Cdd:COG0151 1 MKVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAQLA--ECVDIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 81 VDAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEIEPALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 161 QEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGNGDTGPNTGGMGAYSPAPVVT 240
Cdd:COG0151 159 LEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 241 DEVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPETQPIMLRMKSDLVDLCLAACDGKLN 320
Cdd:COG0151 239 EELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADG-PKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 321 EKTSEWDERASLGVVIAAGGYPGNYSTGDEIHGLPLEEAADGKVFHAGTKLaDDDRVLTSGGRVLCATALGRTVAEAQKH 400
Cdd:COG0151 318 EVELEWDDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTAL-EDGKLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....*.
gi 1730625705 401 AYALMSDISWDGSFSRNDIGWRAIER 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: 689.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 1 MKVLVIGNGGREHALAWKAAQSPLVDTVFVAPGNAGTALEPALQNVAIGVTDIPALLSFAQNEKIDLTIVGPEAPLVIGV 80
Cdd:TIGR00877 1 MKVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 81 VDAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEIEPALAYLREKGAPIVIKADGLAAGKGVIVAMT 160
Cdd:TIGR00877 81 VDALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPIVVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 161 QEEAEAAVHDMLAGNaFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGNGDTGPNTGGMGAYSPAPVVT 240
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 241 DEVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPETQPIMLRMKSDLVDLCLAACDGKLN 320
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEG-PKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 321 EKTSEWDERASLGVVIAAGGYPGNYSTGDEIHGLPLEEAADGKVFHAGTKlADDDRVLTSGGRVLCATALGRTVAEAQKH 400
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTK-ADNGKLVTNGGRVLAVTALGKTLEEARER 397
|
410 420
....*....|....*....|....*
gi 1730625705 401 AYALMSDISWDGSFSRNDIGWRAIE 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: 580.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 4 LVIGNGGREHALAWKAAQSPLVDTVFVAPGNAGTALEPALQNVA-IGVTDIPALLSFAQNEKIDLTIVGPEAPLVIGVVD 82
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 83 AFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEIEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQE 162
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 163 EAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGNGDTGPNTGGMGAYSPAPVVTDE 242
Cdd:PLN02257 161 EAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 243 VHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQ-GNPKVIEFNCRFGDPETQPIMLRMKSDLVDLCLAACDGKLNE 321
Cdd:PLN02257 241 LESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKsGLPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 322 KTSEWDERASLGVVIAAGGYPGNYSTGDEIHGL-PLEEAADG-KVFHAGTKLADDDRVLTSGGRVLCATALGRTVAEAQK 399
Cdd:PLN02257 321 VSLTWSPDSAMVVVMASNGYPGSYKKGTVIKNLdEAEAVAPGvKVFHAGTALDSDGNVVAAGGRVLGVTAKGKDIAEARA 400
|
410 420
....*....|....*....|....*....
gi 1730625705 400 HAYALMSDISWDGSFSRNDIGWRAIEREQ 428
Cdd:PLN02257 401 RAYDAVDQIDWPGGFFRRDIGWRAVARLQ 429
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
103-296 |
2.99e-110 |
|
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: 322.31 E-value: 2.99e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 103 GSKAFTKDFLARHKIPTAEYQNFTEIEPALAYLREKGAPI-VIKADGLAAGKGVIVAMTQEEAEAAVHDMLAGNAFGDAG 181
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAiVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 182 HRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGNGDTGPNTGGMGAYSPAPVVTDEVHQRTMERIIWPTVKGMAA 261
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1730625705 262 EGNTYTGFLYAGLMIDKQGnPKVIEFNCRFGDPET 296
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDG-PKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
1-102 |
3.03e-55 |
|
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: 178.32 E-value: 3.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 1 MKVLVIGNGGREHALAWKAAQSPLVDTVFVAPGNAGTALEPalQNVAIGVTDIPALLSFAQNEKIDLTIVGPEAPLVIGV 80
Cdd:pfam02844 1 MKVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLA--ECVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGI 78
|
90 100
....*....|....*....|....
gi 1730625705 81 VDAF--RAAGLKIFGPTEGAAQLE 102
Cdd:pfam02844 79 VDALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
331-422 |
2.33e-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: 136.04 E-value: 2.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 331 SLGVVIAAGGYPGNYSTGDEIHGLpleEAADGKVFHAGTKLaDDDRVLTSGGRVLCATALGRTVAEAQKHAYALMSDISW 410
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGL---DEAGVKVFHAGTKL-KDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDF 76
|
90
....*....|..
gi 1730625705 411 DGSFSRNDIGWR 422
Cdd:pfam02843 77 EGMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
52-292 |
2.11e-22 |
|
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: 95.71 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 52 DIPALLSFAQNEKIDLTIVGpeaplVIGVVD------AFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHKIPTAEYQNF 125
Cdd:COG0439 1 DIDAIIAAAAELARETGIDA-----VLSESEfavetaAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 126 TEIEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEH 205
Cdd:COG0439 76 DSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 206 VLPMATSQDHKrvgngdTGPNTGGMGAYSPAPvVTDEVHQRTMERiiwpTVKGMAAEGNTYtGFLYAGLMIDKQGNPKVI 285
Cdd:COG0439 156 VVVCSITRKHQ------KPPYFVELGHEAPSP-LPEELRAEIGEL----VARALRALGYRR-GAFHTEFLLTPDGEPYLI 223
|
....*..
gi 1730625705 286 EFNCRFG 292
Cdd:COG0439 224 EINARLG 230
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
79-288 |
2.77e-09 |
|
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: 58.03 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 79 GVVDAFRAAGLKIFGPTEgAAQLEGSKAFTKDFLARHKIPTAEyqnfTEI----EPALAYLREKGAPIVIK-ADGlAAGK 153
Cdd:COG0189 72 ALLRQLEAAGVPVVNDPE-AIRRARDKLFTLQLLARAGIPVPP----TLVtrdpDDLRAFLEELGGPVVLKpLDG-SGGR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 154 GVIVAMTQEEAEAAVHDMlagnaFGDAGHRIVIEEFLDGEEASF--IVMVDGEHVLPMA-TSQDHKRVGNGDTGpntggm 230
Cdd:COG0189 146 GVFLVEDEDALESILEAL-----TELGSEPVLVQEFIPEEDGRDirVLVVGGEPVAAIRrIPAEGEFRTNLARG------ 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730625705 231 GAYSPAPvVTDEVHQrtmeriiwptvkgMAAEGNTYTGFLYAGL-MIDKQGNPKVIEFN 288
Cdd:COG0189 215 GRAEPVE-LTDEERE-------------LALRAAPALGLDFAGVdLIEDDDGPLVLEVN 259
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-209 |
1.60e-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: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 105 KAFTKDFLARHKIPTAEYQNFT--EIEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLAGnafgdaGH 182
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100
....*....|....*....|....*...
gi 1730625705 183 RIVIEEFLDGEEASFIVMVDGE-HVLPM 209
Cdd:COG1181 170 KVLVEEFIDGREVTVGVLGNGGpRALPP 197
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
109-206 |
6.02e-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: 54.31 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 109 KDFLARHKIPTAEYQNFTEIEPALAYLREKGAPIVIKA-----DglaaGKGVIVAMTQEEAEAAVHDMlagnafgdAGHR 183
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTrrggyD----GKGQVVIKSAADLEAAWAAL--------GGGP 161
|
90 100
....*....|....*....|....*.
gi 1730625705 184 IVIEEFLDGE-EASFIVM--VDGEHV 206
Cdd:COG0026 162 CILEEFVPFErELSVIVArsPDGEVA 187
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
1-206 |
9.75e-08 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 53.62 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 1 MKVLVIGNG--GREHALAwkaAQsPL-VDTVFVAPGNAGTALEPALQNVAIGVTDIPALLSFAQ--------NEKID--- 66
Cdd:PRK06019 3 KTIGIIGGGqlGRMLALA---AA-PLgYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELAEqcdvityeFENVPaea 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 67 LTIVGPEAPLVIGVvDAFRAAGLKIfgpTEgaaqlegskaftKDFLARHKIPTAEYQNFTEIEPALAYLREKGAPIVIKA 146
Cdd:PRK06019 79 LDALAARVPVPPGP-DALAIAQDRL---TE------------KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKT 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730625705 147 -----DglaaGKGVIVAMTQEEAEAAVHDMLAGNAfgdaghriVIEEFLDGE-EASFIVM--VDGEHV 206
Cdd:PRK06019 143 rrggyD----GKGQWVIRSAEDLEAAWALLGSVPC--------ILEEFVPFErEVSVIVArgRDGEVV 198
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
1-292 |
5.39e-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: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 1 MKVLVIGNGGREHALAwkaaqSPLVDTVFVAPGnagtalePALQNVAIgvtdIPALLSFAQNEKIDLTI-VGPEAPLVIG 79
Cdd:COG3919 29 VRVIVVDRDPLGPAAR-----SRYVDEVVVVPD-------PGDDPEAF----VDALLELAERHGPDVLIpTGDEYVELLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 80 VVDAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEIEPALAYLREKGAPIVIK-ADGLAA------- 151
Cdd:COG3919 93 RHRDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKpADSVGYdelsfpg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 152 GKGVIVAMTQEEAEAAVHDMLagnafgDAGHRIVIEEFL---DGEEASFIVMVDGEHVLPMATSQdHKRVGNgdtgPNTG 228
Cdd:COG3919 173 KKKVFYVDDREELLALLRRIA------AAGYELIVQEYIpgdDGEMRGLTAYVDRDGEVVATFTG-RKLRHY----PPAG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730625705 229 GmgayspAPVVTDEVHQRTMERIiwpTVKGMAAEGntYTGFLYAGLMID-KQGNPKVIEFNCRFG 292
Cdd:COG3919 242 G------NSAARESVDDPELEEA---ARRLLEALG--YHGFANVEFKRDpRDGEYKLIEINPRFW 295
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-194 |
3.72e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 48.73 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 1 MKVLVIGNGGReHAL--AWKAAQSPlvDTVFVA-PGNAGTALEPALQNVAI-GVTD---IPALLSFAQNEKIDLTIVG-- 71
Cdd:PRK12767 2 MNILVTSAGRR-VQLvkALKKSLLK--GRVIGAdISELAPALYFADKFYVVpKVTDpnyIDRLLDICKKEKIDLLIPLid 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 72 PEAPLVIGVVDAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEIEPALAYLREK--GAPIVIKADGL 149
Cdd:PRK12767 79 PELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGelQFPLFVKPRDG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1730625705 150 AAGKGVIVAMTQEEAEAAVHDMLAgnafgdaghrIVIEEFLDGEE 194
Cdd:PRK12767 159 SASIGVFKVNDKEELEFLLEYVPN----------LIIQEFIEGQE 193
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
61-290 |
3.85e-06 |
|
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: 49.23 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 61 QNEKIDLTIVGPEAPLVIGVVDAFRAAGLKIFG-PTEGAAQLEGSKAFTKdFLARHKIPTAEYQNFTEIEPALAYLREKG 139
Cdd:TIGR01369 626 ELEKPEGVIVQFGGQTPLNLAKALEEAGVPILGtSPESIDRAEDREKFSE-LLDELGIPQPKWKTATSVEEAVEFASEIG 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 140 APIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLAGNafgdAGHRIVIEEFL-DGEEASFIVMVDGEHVLPMATSQDHKRv 218
Cdd:TIGR01369 705 YPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVS----PEHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGIMEHIEE- 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730625705 219 gngdTGPNTGGMGAYSPAPVVTDEVHQRtMERIiwptVKGMAAEGNtytgflYAGLM----IDKQGNPKVIEFNCR 290
Cdd:TIGR01369 780 ----AGVHSGDSTCVLPPQTLSAEIVDR-IKDI----VRKIAKELN------VKGLMniqfAVKDGEVYVIEVNPR 840
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
103-294 |
9.83e-06 |
|
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: 45.45 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 103 GSKAFTKDFLARHKIPTAEYQNFTEIEPAlaylrekGAPIVIK-ADGlAAGKGVIVAMTQEEAEAAVHDMLagnafgdag 181
Cdd:pfam02655 2 SDKLKTYKALKNAGVPTPETLQAEELLRE-------EKKYVVKpRDG-CGGEGVRKVENGREDEAFIENVL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 182 hrivIEEFLDGEEASFIVMVDGEHVLPMATSQDHkrVGN-GDTGPNTGGMgaySPAPVVTDEVHQRTMERII--WPTVKG 258
Cdd:pfam02655 65 ----VQEFIEGEPLSVSLLSDGEKALPLSVNRQY--IDNgGSGFVYAGNV---TPSRTELKEEIIELAEEVVecLPGLRG 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 1730625705 259 MAAEgntytgflyaGLMIDKQGnPKVIEFNCRFGDP 294
Cdd:pfam02655 136 YVGV----------DLVLKDNE-PYVIEVNPRITTS 160
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
82-207 |
4.50e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 45.52 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 82 DAFRAAGLKIFGPTEGAAQLEGSKAFTKDFLARHKIPTAEYQN--FTEIEPALAYLREKGAPIVIKADGLAAGKGVIVAM 159
Cdd:PRK12833 96 EAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDgvVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAH 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1730625705 160 TQEE--AEAAVHDMLAGNAFGDAGhrIVIEEFLdgEEASFI---VMVDGEHVL 207
Cdd:PRK12833 176 DAAQlaAELPLAQREAQAAFGDGG--VYLERFI--ARARHIevqILGDGERVV 224
|
|
| PRK02471 |
PRK02471 |
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB; |
105-204 |
1.09e-04 |
|
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
Pssm-ID: 179427 [Multi-domain] Cd Length: 752 Bit Score: 44.53 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 105 KAFTKDFLARHKIPTAEYQNFTEIEPALAYLRE-KGAPIVIKADGLAAGKGVIVamTQEEAEAAVHDMLAGNAFGDAGHr 183
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLfADKAIVVKPKSTNFGLGISI--FKEPASLEDYEKALEIAFREDSS- 565
|
90 100
....*....|....*....|.
gi 1730625705 184 IVIEEFLDGEEASFIVMvDGE 204
Cdd:PRK02471 566 VLVEEFIVGTEYRFFVL-DGK 585
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
57-207 |
1.58e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 44.19 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 57 LSFAQNEKIDLTIVGPEAPLVIGVVDAFRAAGLKIFGPT-EGAAQLEGSKAFTKdFLARHKIPTAEYQNFTEIEPALAYL 135
Cdd:PRK12815 623 LNVAEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSpDTIDRLEDRDRFYQ-LLDELGLPHVPGLTATDEEEAFAFA 701
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730625705 136 REKGAPIVIKADGLAAGKGVIVAMTQEEAEAavhdMLAGNAfgDAGHRIVIEEFLDGEEASFIVMVDGEHVL 207
Cdd:PRK12815 702 KRIGYPVLIRPSYVIGGQGMAVVYDEPALEA----YLAENA--SQLYPILIDQFIDGKEYEVDAISDGEDVT 767
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
112-290 |
3.69e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 42.71 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 112 LARHKIPTAEYQNFTEIEPALAYLRE---KGAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLAG-NAFGDAGHRIVIE 187
Cdd:PRK07206 116 LAEAGLPAARQINTADWEEAEAWLREnglIDRPVVIKPLESAGSDGVFICPAKGDWKHAFNAILGKaNKLGLVNETVLVQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 188 EFLDGEE-ASFIVMVDGEHVLPMATSQDHKRVGNgdtgpntgGMGAYSP---APVVTDEVHQrtmeriIWPTVKG-MAAE 262
Cdd:PRK07206 196 EYLIGTEyVVNFVSLDGNHLVTEIVRYHKTSLNS--------GSTVYDYdefLDYSEPEYQE------LVDYTKQaLDAL 261
|
170 180
....*....|....*....|....*...
gi 1730625705 263 GNTYtGFLYAGLMIDKQGnPKVIEFNCR 290
Cdd:PRK07206 262 GIKN-GPAHAEVMLTADG-PRLIEIGAR 287
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
139-293 |
7.88e-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: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 139 GAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDMLA--------GNAFGDAGHRIVIEEFLDGEEASFIVMVD--GEHVLp 208
Cdd:pfam13535 2 PYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREeieqwkemYPEAVVDGGSFLVEEYIEGEEFAVDAYFDenGEPVI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 209 maTSQDHKRvgngdtgpntggmgaYSPAPVVTDEVHQrTMERIIWPTVKGMA---AEGNTYTGF----LYAGLMIDKQGN 281
Cdd:pfam13535 81 --LNILKHD---------------FASSEDVSDRIYV-TSASIIRETQAAFTeflKRINALLGLknfpVHIELRVDEDGQ 142
|
170
....*....|...
gi 1730625705 282 PKVIEFN-CRFGD 293
Cdd:pfam13535 143 IIPIEVNpLRFAG 155
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
113-204 |
1.05e-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: 39.54 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 113 ARHKIPTAEYQNFTEIEPALAYLREKGAPIVIKADGLA-AGKGVIVAMTQEEAEAAVHDMLAGnafgdaghRIVIEEFLD 191
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAWEELGDG--------PVIVEEFVP 72
|
90
....*....|....*.
gi 1730625705 192 GE-EASFIVM--VDGE 204
Cdd:pfam02222 73 FDrELSVLVVrsVDGE 88
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-208 |
1.24e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 40.48 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 105 KAFTKDFLARHKIPTAEYQNFTEIEPALAYLREKGAPIVIKAdgLAAGK--GVIVAMTQEEAEAAVHDMLagnAFGDagh 182
Cdd:PRK01372 99 KLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAF---KYDD--- 170
|
90 100
....*....|....*....|....*.
gi 1730625705 183 RIVIEEFLDGEEasFIVMVDGEHVLP 208
Cdd:PRK01372 171 EVLVEKYIKGRE--LTVAVLGGKALP 194
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
105-194 |
1.26e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 41.30 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 105 KAFTKDFLARHKIPTAEYQNFTEIEPALAYLREKGAPIVIK-ADGlAAGKGVIV-AMTQEEAEAAVHdmlAGNAFGDAgh 182
Cdd:PRK14016 215 KELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKpLDG-NHGRGVTVnITTREEIEAAYA---VASKESSD-- 288
|
90
....*....|..
gi 1730625705 183 rIVIEEFLDGEE 194
Cdd:PRK14016 289 -VIVERYIPGKD 299
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-252 |
1.28e-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: 39.98 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 128 IEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEEAEAAVHDML--AGNAFGDagHRIVIEEFLDG-EEASFIVMVDGE 204
Cdd:pfam02786 27 EEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALaeAPAAFGN--PQVLVEKSLKGpKHIEYQVLRDAH 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1730625705 205 ----HVLPMATSqDHKRvgngdtgpnTGGMGAYSPAPVVTDEVHQRTMERII 252
Cdd:pfam02786 105 gnciTVCNRECS-DQRR---------TQKSIEVAPSQTLTDEERQMLREAAV 146
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
85-191 |
1.31e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 40.94 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 85 RAAGLKIFGPTEGAAQLEGSKAFTKDFLARHKIPTAEYQN--FTEIEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQE 162
Cdd:PRK08591 96 EDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDgpVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEA 175
|
90 100 110
....*....|....*....|....*....|..
gi 1730625705 163 EAEAAVHdML---AGNAFGDAGhrIVIEEFLD 191
Cdd:PRK08591 176 ELEKAFS-MAraeAKAAFGNPG--VYMEKYLE 204
|
|
| ATPgrasp_ST |
pfam14397 |
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ... |
103-292 |
1.87e-03 |
|
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the biosynthesis of cell surface polysaccharides.
Pssm-ID: 405145 [Multi-domain] Cd Length: 278 Bit Score: 40.02 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 103 GSKAFTKDFLARHKIPTAE----YQNFTEIEPALAYLREKGAPIVIKADGLAAGKGVIVAMTQEEAE-------AAVHDM 171
Cdd:pfam14397 20 DDKLKFKQLALRAGLPVPKlygvISIGHDISRLDAFVRSLPPGFVIKPAKGSGGKGILVITRRGDQDyfkssgcRILLDE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 172 LAGN--AFGDAGHRIVIEEFL--DGEEASF----------IVMVDGE--HVLP--MATSQDHKRVGNGDTG-------PN 226
Cdd:pfam14397 100 LKRHvsSLGGKPDVALVEERIvqDPVFAKLspesvntirvITFLLDNgvPVMPamLRLGTGASLVDNLHQGgvgvgidLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 227 TGGMGAYSPAPVVTDEVH-------QRTMERII--WPTVKGMAAEgnTYTGFLYAGLM-----IDKQGNPKVIEFNCRFG 292
Cdd:pfam14397 180 TGVLFKPALQAVQYGEPIehhpdtgVKFRGFQIpnWDQILELAAE--CAQTLPGLGYVgwdivIDENGGPLLLELNARPG 257
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
109-191 |
3.84e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 39.30 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 109 KDFLARHKIPTAEYQNFTEIEPALAYLRE-KGAPIVIKADGLAAGK----GVIVAMTQEEAEAAVHDML----AGNAFGD 179
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEElGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQILgmtlVTHQTGP 88
|
90
....*....|....*
gi 1730625705 180 AGH---RIVIEEFLD 191
Cdd:PRK00696 89 KGQpvnKVLVEEGAD 103
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
109-191 |
4.63e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 38.01 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730625705 109 KDFLARHKIPTAEYQNFTEIEPALAYLREKGAP-IVIKADGLAAGKG----VIVAMTQEEAEAAVHDMLAGN----AFGD 179
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKvYVVKAQVLAGGRGkaggVKLAKSPEEAKEVAKEMLGKNlvtkQTGP 87
|
90
....*....|....*
gi 1730625705 180 AGH---RIVIEEFLD 191
Cdd:pfam08442 88 DGQpvnKVLVEEALD 102
|
|
| |
