|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
3-304 |
4.58e-97 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 287.58 E-value: 4.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 3 VVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPTEaidaVRSEPVVLVSNTYPDS-GIVSTLLLLEAiadvrr 81
Cdd:PRK00934 2 IIGGSASQLLASEVARLLNTELALVETKRFPDGELYVRILGE----IDGEDVVIISTTYPQDeNLVELLLLIDA------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 82 gdlsnLKGEEPQSMDdvgggvfLAIPYYGYSRQDKRFSKGEAVSARVIAEILARGCDGIAILDLHEPAVLEGMDVPIEFV 161
Cdd:PRK00934 72 -----LRDEGAKSIT-------LVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIHEPSILEFFPIPFINL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 162 SSMPEIAELLQSEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDAHTIEHTPKDLDVGGKVVAIVDDMISTGGT 241
Cdd:PRK00934 140 DAAPLIAEYIGDKLDDPLVLAPDKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDVKGKDVLIVDDIISTGGT 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663515100 242 ICRASDALRRQGATEVHAACTHGLFTGGAILRL-ANHVDGVHSTDSLPNPRAVVSAAPALARGL 304
Cdd:PRK00934 220 MATAIKILKEQGAKKVYVACVHPVLVGDAILKLyNAGVDEIIVTDTLESEVSKISVAPLIADLL 283
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
1-306 |
6.52e-82 |
|
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273523 [Multi-domain] Cd Length: 308 Bit Score: 249.89 E-value: 6.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 1 MPVVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPtEAIDAvrSEPVVLVSNTYP--DSGIVSTLLLLEAiad 78
Cdd:TIGR01251 1 MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRIN-ESVRG--KDVFIIQQSTSApvNDNLMELLIMIDA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 79 VRRGDLSNLKgeepqsmddvgggvfLAIPYYGYSRQDKRFSKGEAVSARVIAEIL-ARGCDGIAILDLHEPAVLEGMDVP 157
Cdd:TIGR01251 75 LKRASAKSIT---------------AVIPYYGYARQDKKFKSREPISAKLVANLLeTAGADRVLTVDLHSPQIQGFFDVP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 158 IEFVSSMPEIAE-LLQSEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDAH-TIEHTPKDLDVGGKVVAIVDDM 235
Cdd:TIGR01251 140 VDNLYASPVLAEyLKKKILDNPVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATnEVEVMNLVGDVEGKDVVIVDDI 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663515100 236 ISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLAN-HVDGVHSTDSLPNPRA-----VVSAAPALARGLQR 306
Cdd:TIGR01251 220 IDTGGTIAKAAEILKSAGAKRVIAAATHGVFSGPAIERIANaGVEEVIVTNTIPHEKHkpkvsVISVAPLIAEAIRR 296
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
3-309 |
8.32e-81 |
|
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis
Pssm-ID: 440230 [Multi-domain] Cd Length: 311 Bit Score: 247.28 E-value: 8.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 3 VVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVRSEPVVLVSNTYP--DSGIVSTLLLLEAI--AD 78
Cdd:COG0462 6 IFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIE----ESVRGRDVFVIQSTSPpvNDNLMELLIMIDALkrAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 79 VRRgdlsnlkgeepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEIL-ARGCDGIAILDLHEPAVLEGMDVP 157
Cdd:COG0462 82 ARR--------------------ITAVIPYYGYARQDRKFRPREPITAKLVADLLeAAGADRVLTVDLHAPQIQGFFDIP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 158 IEFVSSMPEIAELLQSEVSPDFVL-SPDKGAISRATEVAGLIGCDFSYLEKTRIDAHTIEHTPKDLDVGGKVVAIVDDMI 236
Cdd:COG0462 142 VDHLYAAPLLADYIKSKDLEDLVVvSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVEGKTCIIVDDMI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 237 STGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLANH-VDGVHSTDSLPNPRA-------VVSAAPALARGLQRLM 308
Cdd:COG0462 222 DTGGTLVEAAEALKEAGAKSVYAAATHGVLSGPAVERLENSpIDELVVTDTIPLPEEkrcdkikVLSVAPLLAEAIRRIH 301
|
.
gi 663515100 309 E 309
Cdd:COG0462 302 E 302
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
167-286 |
3.71e-21 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 87.07 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 167 IAELLQSEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDA------HTIEHTPKDLDVGGKVVAIVDDMISTGG 240
Cdd:cd06223 6 AEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPgrtpsePYGLELPLGGDVKGKRVLLVDDVIATGG 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 663515100 241 TICRASDALRRQGATEVHAACTHGLFTGGAILrLANHVDGVHSTDS 286
Cdd:cd06223 86 TLLAAIELLKEAGAKVVGVAVLLDKPEGGARE-LASPGDPVYSLFT 130
|
|
| Pribosyltran_N |
pfam13793 |
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ... |
1-133 |
8.41e-14 |
|
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.
Pssm-ID: 433483 [Multi-domain] Cd Length: 117 Bit Score: 66.67 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 1 MPVVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVRSEPVVLVSNTYPD--SGIVSTLLLLEAI-- 76
Cdd:pfam13793 1 LKIFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIE----ESVRGKDVFIIQSTCPPvnDNLMELLIMIDALkr 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 663515100 77 ADVRRgdlsnlkgeepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEIL 133
Cdd:pfam13793 77 ASAKR--------------------ITAVIPYFGYARQDRKDKPREPITAKLVADLL 113
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00934 |
PRK00934 |
ribose-phosphate pyrophosphokinase; Provisional |
3-304 |
4.58e-97 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 234868 [Multi-domain] Cd Length: 285 Bit Score: 287.58 E-value: 4.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 3 VVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPTEaidaVRSEPVVLVSNTYPDS-GIVSTLLLLEAiadvrr 81
Cdd:PRK00934 2 IIGGSASQLLASEVARLLNTELALVETKRFPDGELYVRILGE----IDGEDVVIISTTYPQDeNLVELLLLIDA------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 82 gdlsnLKGEEPQSMDdvgggvfLAIPYYGYSRQDKRFSKGEAVSARVIAEILARGCDGIAILDLHEPAVLEGMDVPIEFV 161
Cdd:PRK00934 72 -----LRDEGAKSIT-------LVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIHEPSILEFFPIPFINL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 162 SSMPEIAELLQSEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDAHTIEHTPKDLDVGGKVVAIVDDMISTGGT 241
Cdd:PRK00934 140 DAAPLIAEYIGDKLDDPLVLAPDKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDVKGKDVLIVDDIISTGGT 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663515100 242 ICRASDALRRQGATEVHAACTHGLFTGGAILRL-ANHVDGVHSTDSLPNPRAVVSAAPALARGL 304
Cdd:PRK00934 220 MATAIKILKEQGAKKVYVACVHPVLVGDAILKLyNAGVDEIIVTDTLESEVSKISVAPLIADLL 283
|
|
| ribP_PPkin |
TIGR01251 |
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ... |
1-306 |
6.52e-82 |
|
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273523 [Multi-domain] Cd Length: 308 Bit Score: 249.89 E-value: 6.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 1 MPVVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPtEAIDAvrSEPVVLVSNTYP--DSGIVSTLLLLEAiad 78
Cdd:TIGR01251 1 MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRIN-ESVRG--KDVFIIQQSTSApvNDNLMELLIMIDA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 79 VRRGDLSNLKgeepqsmddvgggvfLAIPYYGYSRQDKRFSKGEAVSARVIAEIL-ARGCDGIAILDLHEPAVLEGMDVP 157
Cdd:TIGR01251 75 LKRASAKSIT---------------AVIPYYGYARQDKKFKSREPISAKLVANLLeTAGADRVLTVDLHSPQIQGFFDVP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 158 IEFVSSMPEIAE-LLQSEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDAH-TIEHTPKDLDVGGKVVAIVDDM 235
Cdd:TIGR01251 140 VDNLYASPVLAEyLKKKILDNPVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATnEVEVMNLVGDVEGKDVVIVDDI 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663515100 236 ISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLAN-HVDGVHSTDSLPNPRA-----VVSAAPALARGLQR 306
Cdd:TIGR01251 220 IDTGGTIAKAAEILKSAGAKRVIAAATHGVFSGPAIERIANaGVEEVIVTNTIPHEKHkpkvsVISVAPLIAEAIRR 296
|
|
| PrsA |
COG0462 |
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ... |
3-309 |
8.32e-81 |
|
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis
Pssm-ID: 440230 [Multi-domain] Cd Length: 311 Bit Score: 247.28 E-value: 8.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 3 VVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVRSEPVVLVSNTYP--DSGIVSTLLLLEAI--AD 78
Cdd:COG0462 6 IFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIE----ESVRGRDVFVIQSTSPpvNDNLMELLIMIDALkrAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 79 VRRgdlsnlkgeepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEIL-ARGCDGIAILDLHEPAVLEGMDVP 157
Cdd:COG0462 82 ARR--------------------ITAVIPYYGYARQDRKFRPREPITAKLVADLLeAAGADRVLTVDLHAPQIQGFFDIP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 158 IEFVSSMPEIAELLQSEVSPDFVL-SPDKGAISRATEVAGLIGCDFSYLEKTRIDAHTIEHTPKDLDVGGKVVAIVDDMI 236
Cdd:COG0462 142 VDHLYAAPLLADYIKSKDLEDLVVvSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVEGKTCIIVDDMI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 237 STGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLANH-VDGVHSTDSLPNPRA-------VVSAAPALARGLQRLM 308
Cdd:COG0462 222 DTGGTLVEAAEALKEAGAKSVYAAATHGVLSGPAVERLENSpIDELVVTDTIPLPEEkrcdkikVLSVAPLLAEAIRRIH 301
|
.
gi 663515100 309 E 309
Cdd:COG0462 302 E 302
|
|
| PRK07199 |
PRK07199 |
ribose-phosphate diphosphokinase; |
8-309 |
7.02e-51 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 235960 [Multi-domain] Cd Length: 301 Bit Score: 170.12 E-value: 7.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 8 SGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPTEAIDAvrsEPVVLVSNTYPDSGIVStlLLLEAIAdVRRGDLSNl 87
Cdd:PRK07199 10 GNEAAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGR---TVVLVCSLDRPDEKLLP--LLFAAEA-ARELGARR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 88 kgeepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEILARGCDGIAILD--LHEPAVL-EGMDVPIEFVSSM 164
Cdd:PRK07199 83 --------------VGLVAPYLAYMRQDIAFHPGEAISQRHFARLLSGSFDRLVTVDphLHRYPSLsEVYPIPAVVLSAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 165 PEIAELLQSEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDAHTIEHT-PKDLDVGGKVVAIVDDMISTGGTIC 243
Cdd:PRK07199 149 PAIAAWIRAHVPRPLLIGPDEESEQWVAAVAERAGAPHAVLRKTRHGDRDVEISlPDAAPWAGRTPVLVDDIVSTGRTLI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663515100 244 RASDALRRQGATEVHAACTHGLFTGGAILRLAN-HVDGVHSTDSLPNPRAVVSAAPALARGLQRLME 309
Cdd:PRK07199 229 EAARQLRAAGAASPDCVVVHALFAGDAYSALAAaGIARVVSTDTVPHPSNAISLAPLLAEALRREFD 295
|
|
| PRK01259 |
PRK01259 |
ribose-phosphate diphosphokinase; |
1-309 |
1.96e-41 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 234929 [Multi-domain] Cd Length: 309 Bit Score: 145.65 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 1 MPVVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEgyVRVPTEaiDAVRSEPVVLVSNT-YP--DSgIVSTLLLLEAIa 77
Cdd:PRK01259 1 MKLFAGNANPELAEKIAKYLGIPLGKASVGRFSDGE--ISVEIN--ENVRGKDVFIIQSTcAPtnDN-LMELLIMIDAL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 78 dvRRGDlsnlkgeepqsmddvGGGVFLAIPYYGYSRQDKRFSKGEAVSARVIAEILAR-GCDGIAILDLHEPAVLEGMDV 156
Cdd:PRK01259 75 --KRAS---------------AGRITAVIPYFGYARQDRKARSRVPITAKLVANLLETaGADRVLTMDLHADQIQGFFDI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 157 PIEFVSSMPEIAELLQSEVSPDF-VLSPDKGAISRATEVAGLIGCDFSYLEKTRIDAHTIEHTPKDLDVGGKVVAIVDDM 235
Cdd:PRK01259 138 PVDNLYGSPILLEDIKQKNLENLvVVSPDVGGVVRARALAKRLDADLAIIDKRRPRANVSEVMNIIGDVEGRDCILVDDM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 236 ISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLANHV-DGVHSTDSLPNPRA--------VVSAAPALARGLQR 306
Cdd:PRK01259 218 IDTAGTLCKAAEALKERGAKSVYAYATHPVLSGGAIERIENSViDELVVTDSIPLSEEakkcdkirVLSVAPLLAEAIRR 297
|
...
gi 663515100 307 LME 309
Cdd:PRK01259 298 ISN 300
|
|
| PLN02369 |
PLN02369 |
ribose-phosphate pyrophosphokinase |
10-306 |
6.52e-39 |
|
ribose-phosphate pyrophosphokinase
Pssm-ID: 215209 [Multi-domain] Cd Length: 302 Bit Score: 139.06 E-value: 6.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 10 RGVASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVRSEPVVLVSNTYPDS--GIVSTLLLLEAIadvRRGDLSNl 87
Cdd:PLN02369 1 PALSQEIACYLGLELGKITIKRFADGEIYVQLQ----ESVRGCDVFLVQPTCPPAneNLMELLIMIDAC---RRASAKR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 88 kgeepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEILAR-GCDGIAILDLHEPAVLEGMDVPIEFVSSMPE 166
Cdd:PLN02369 73 --------------ITAVIPYFGYARADRKTQGRESIAAKLVANLITEaGADRVLACDLHSGQSMGYFDIPVDHVYGQPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 167 IAELLQSEV--SPDF-VLSPDKGAISRATEVA-GLIGCDFSYLEKTRIDAHTIEhtPKDL--DVGGKVVAIVDDMISTGG 240
Cdd:PLN02369 139 ILDYLASKTisSPDLvVVSPDVGGVARARAFAkKLSDAPLAIVDKRRQGHNVAE--VMNLigDVKGKVAIMVDDMIDTAG 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663515100 241 TICRASDALRRQGATEVHAACTHGLFTGGAILRLANHV-DGVHSTDSLP--NPRA-----VVSAAPALARGLQR 306
Cdd:PLN02369 217 TITKGAALLHQEGAREVYACATHAVFSPPAIERLSSGLfQEVIVTNTIPvsEKNYfpqltVLSVANLLGETIWR 290
|
|
| PRK03092 |
PRK03092 |
ribose-phosphate diphosphokinase; |
13-309 |
1.36e-37 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 179535 [Multi-domain] Cd Length: 304 Bit Score: 135.46 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 13 ASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVR-SEPVVLVSNTYP-DSGIVSTLLLLEAI--ADVRRgdlsnlk 88
Cdd:PRK03092 2 AEEVAKELGVEVTPTTAYDFANGEIYVRFE----ESVRgCDAFVLQSHTAPiNKWLMEQLIMIDALkrASAKR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 89 geepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEIL-ARGCDGIAILDLHEPAVLEGMDVPIEFVSSMPEI 167
Cdd:PRK03092 71 -------------ITVVLPFYPYARQDKKHRGREPISARLVADLFkTAGADRIMTVDLHTAQIQGFFDGPVDHLFAMPLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 168 AELLQSEVSPD--FVLSPDKGAISRATEVAG-LIGCDFSYLEKTR-------IDAHTIEHtpkdlDVGGKVVAIVDDMIS 237
Cdd:PRK03092 138 ADYVRDKYDLDnvTVVSPDAGRVRVAEQWADrLGGAPLAFIHKTRdptvpnqVVANRVVG-----DVEGRTCVLVDDMID 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 238 TGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLAN-HVDGVHSTDSLPNPR-------AVVSAAPALARGLQRLME 309
Cdd:PRK03092 213 TGGTIAGAVRALKEAGAKDVIIAATHGVLSGPAAERLKNcGAREVVVTDTLPIPEekrfdklTVLSIAPLLARAIREVFE 292
|
|
| PRK02269 |
PRK02269 |
ribose-phosphate diphosphokinase; |
7-309 |
5.68e-36 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 167353 [Multi-domain] Cd Length: 320 Bit Score: 131.45 E-value: 5.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 7 SSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVRSEPV-VLVSNTYP-DSGIVSTLLLLEAIadvRRGDL 84
Cdd:PRK02269 12 SSNKELAEKVAQEIGIELGKSSVRQFSDGEIQVNIE----ESIRGHHVfILQSTSSPvNDNLMEILIMVDAL---KRASA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 85 SNlkgeepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEILAR-GCDGIAILDLHEPAVLEGMDVPIEFVSS 163
Cdd:PRK02269 85 ES---------------INVVMPYYGYARQDRKARSREPITSKLVANMLEVaGVDRLLTVDLHAAQIQGFFDIPVDHLMG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 164 MPEIAELL--QSEVSPDFVL-SPDKGAISRATEVAGLIGCDFSYLEKTR--IDAHTIEHTPKDLDVGGKVVAIVDDMIST 238
Cdd:PRK02269 150 APLIADYFdrRGLVGDDVVVvSPDHGGVTRARKLAQFLKTPIAIIDKRRsvDKMNTSEVMNIIGNVKGKKCILIDDMIDT 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663515100 239 GGTICRASDALRRQGATEVHAACTHGLFTGGAILRLANH-VDGVHSTDS--LPNPRAV-----VSAAPALARGLQRLME 309
Cdd:PRK02269 230 AGTICHAADALAEAGATEVYASCTHPVLSGPALDNIQKSaIEKLVVLDTiyLPEERLIdkieqISIADLLGEAIIRIHE 308
|
|
| PRK02812 |
PRK02812 |
ribose-phosphate pyrophosphokinase; Provisional |
3-309 |
3.59e-32 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 235072 [Multi-domain] Cd Length: 330 Bit Score: 121.77 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 3 VVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVRSEPVVLVSntyPDSGIVSTLL--LLEAIADVR 80
Cdd:PRK02812 24 LFSGSSNPALAQEVARYLGMDLGPMIRKRFADGELYVQIQ----ESIRGCDVYLIQ---PTCAPVNDHLmeLLIMVDACR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 81 RGDLSNLKGeepqsmddvgggvflAIPYYGYSRQDKRFSKGEAVSARVIAEILAR-GCDGIAILDLHEPAVLEGMDVPIE 159
Cdd:PRK02812 97 RASARQITA---------------VIPYYGYARADRKTAGRESITAKLVANLITKaGADRVLAMDLHSAQIQGYFDIPCD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 160 FVSSMPEIAELLQSEVSPDFVL-SPDKGAISRATEVAG-LIGCDFSYLEKTRiDAHTIEHTPKDL-DVGGKVVAIVDDMI 236
Cdd:PRK02812 162 HVYGSPVLLDYLASKNLEDIVVvSPDVGGVARARAFAKkLNDAPLAIIDKRR-QAHNVAEVLNVIgDVKGKTAILVDDMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 237 STGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLANHV-DGVHSTDSLPNPR-------AVVSAAPALARGLQRLM 308
Cdd:PRK02812 241 DTGGTICEGARLLRKEGAKQVYACATHAVFSPPAIERLSSGLfEEVIVTNTIPVPEerrfpqlKVLSVANMLGEAIWRIH 320
|
.
gi 663515100 309 E 309
Cdd:PRK02812 321 E 321
|
|
| PTZ00145 |
PTZ00145 |
phosphoribosylpyrophosphate synthetase; Provisional |
3-287 |
1.17e-29 |
|
phosphoribosylpyrophosphate synthetase; Provisional
Pssm-ID: 240290 [Multi-domain] Cd Length: 439 Bit Score: 116.90 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 3 VVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEgyvrVPTEAIDAVRSEPVVLVSNTYP--DSGIVSTLLLleaIADVR 80
Cdd:PTZ00145 122 LFSGSSNPLLSKNIADHLGTILGRVHLKRFADGE----VSMQFLESIRGKDVYIIQPTCPpvNENLIELLLM---ISTCR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 81 RGDLSNLKGeepqsmddvgggvflAIPYYGYSRQDKRFSKGEAVSARVIAEIL-ARGCDGIAILDLHEPAV--LEGMDVP 157
Cdd:PTZ00145 195 RASAKKITA---------------VIPYYGYARQDRKLSSRVPISAADVARMIeAMGVDRVVAIDLHSGQIqgFFGPRVP 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 158 IE-FVSSMPEIAELLQSEVSPDFVLSPDKGAISRATEVA-GLIG-----CDFSYLEKTRIDAHTIEHTPKDLDVGGKVVA 230
Cdd:PTZ00145 260 VDnLEAQLIGLDYFTKKDLYKPVIVSPDAGGVYRARKFQdGLNHrgisdCGIAMLIKQRTKPNEIEKMDLVGNVYDSDVI 339
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 663515100 231 IVDDMISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLANH-VDGVHSTDSL 287
Cdd:PTZ00145 340 IVDDMIDTSGTLCEAAKQLKKHGARRVFAFATHGLFSGPAIERIEASpLEEVVVTDTV 397
|
|
| PRK04923 |
PRK04923 |
ribose-phosphate diphosphokinase; |
3-288 |
2.72e-29 |
|
ribose-phosphate diphosphokinase;
Pssm-ID: 179893 [Multi-domain] Cd Length: 319 Bit Score: 113.87 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 3 VVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEgyvrVPTEAIDAVRSEPVVLVSNTYPDSG--IVSTLLLLEAIadvR 80
Cdd:PRK04923 9 VFSGNANKPLAQSICKELGVRMGKALVTRFSDGE----VQVEIEESVRRQEVFVIQPTCAPSAenLMELLVLIDAL---K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 81 RGDLSNlkgeepqsmddvgggVFLAIPYYGYSRQDKRF-SKGEAVSARVIAE-ILARGCDGIAILDLHEPAVLEGMDVPI 158
Cdd:PRK04923 82 RASAAS---------------VTAVIPYFGYSRQDRRMrSSRVPITAKVAAKmISAMGADRVLTVDLHADQIQGFFDVPV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 159 EFVSSMP-EIAELLQSEVSPDF-VLSPDKGAISRATEVAGLIG-CDFSYLEKTRIDAHTIEHTPKDLDVGGKVVAIVDDM 235
Cdd:PRK04923 147 DNVYASPlLLADIWRAYGTDNLiVVSPDVGGVVRARAVAKRLDdADLAIIDKRRPRANVATVMNIIGDVQGKTCVLVDDL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 663515100 236 ISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLANHV-DGVHSTDSLP 288
Cdd:PRK04923 227 VDTAGTLCAAAAALKQRGALKVVAYITHPVLSGPAVDNINNSQlDELVVTDTIP 280
|
|
| PRK00553 |
PRK00553 |
ribose-phosphate pyrophosphokinase; Provisional |
3-288 |
2.43e-28 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 179062 [Multi-domain] Cd Length: 332 Bit Score: 111.55 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 3 VVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRvPTEAidaVRSEPVVLVSNTYPDSGIvSTLLLLEAIADVRRG 82
Cdd:PRK00553 12 IFSLSKAKKLVDSICRKLSMKPGEIVIQKFADGETYIR-FDES---VRNKDVVIFQSTCSPVND-SLMELLIAIDALKRG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 83 DLSNLKGeepqsmddvgggvflAIPYYGYSRQDKRFSKGEAVSARVIAEILAR-GCDGIAILDLHEPAVLEGMDVPIEFV 161
Cdd:PRK00553 87 SAKSITA---------------ILPYYGYARQDRKTAGREPITSKLVADLLTKaGVTRVTLTDIHSDQTQGFFDIPVDIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 162 SS----MPEIAELLQSEvspDFVL-SPDKGAISRATEVAGLIGCDFSYLEKTRiDAHTIEHTPKDL-DVGGKVVAIVDDM 235
Cdd:PRK00553 152 RTyhvfLSRVLELLGKK---DLVVvSPDYGGVKRARLIAESLELPLAIIDKRR-PKHNVAESINVLgEVKNKNCLIVDDM 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 663515100 236 ISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRL-----ANHVDGVHSTDSLP 288
Cdd:PRK00553 228 IDTGGTVIAAAKLLKKQKAKKVCVMATHGLFNKNAIQLFdeafkKKLIDKLFVSNSIP 285
|
|
| PRK02458 |
PRK02458 |
ribose-phosphate pyrophosphokinase; Provisional |
1-309 |
1.81e-27 |
|
ribose-phosphate pyrophosphokinase; Provisional
Pssm-ID: 235039 [Multi-domain] Cd Length: 323 Bit Score: 109.06 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 1 MPVVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVRSEPVVLVSNT-YPDSGIVSTLLLLeaIADV 79
Cdd:PRK02458 10 IKLFSLNSNLEIAEKIAQAAGVPLGKLSSRQFSDGEIMINIE----ESVRGDDIYIIQSTsFPVNDHLWELLIM--IDAC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 80 RRGDLSNlkgeepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEILAR-GCDGIAILDLHEPAVLEGMDVPI 158
Cdd:PRK02458 84 KRASANT---------------VNVVLPYFGYARQDRIAKPREPITAKLVANMLVKaGVDRVLTLDLHAVQVQGFFDIPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 159 EFVSSMPEIAE------LLQSEVspdFVLSPDKGAISRATEVAGLIGC-----DFSYLEKTRIDAHTIEhtpkdlDVGGK 227
Cdd:PRK02458 149 DNLFTVPLFAKhyckkgLSGSDV---VVVSPKNSGIKRARSLAEYLDApiaiiDYAQDDSEREEGYIIG------DVAGK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 228 VVAIVDDMISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLANH-------VDGVHSTDSLPNPRAVVSAAPAL 300
Cdd:PRK02458 220 KAILIDDILNTGKTFAEAAKIVEREGATEIYAVASHGLFAGGAAEVLENApikeilvTDSVATKERVPKNVTYLSASELI 299
|
....*....
gi 663515100 301 ARGLQRLME 309
Cdd:PRK02458 300 ADAIIRIHE 308
|
|
| PRK06827 |
PRK06827 |
phosphoribosylpyrophosphate synthetase; Provisional |
106-269 |
1.39e-22 |
|
phosphoribosylpyrophosphate synthetase; Provisional
Pssm-ID: 180714 [Multi-domain] Cd Length: 382 Bit Score: 96.56 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 106 IPYYGYSRQDKRFSKgEAVSARVIAEILAR-GCDGIAILDLHEPAV--------LEGMDVPIEFVSSMpeIAELLQSEVS 176
Cdd:PRK06827 129 MPFLYESRQHKRKGR-ESLDCALALQELEElGVDNIITFDAHDPRIenaiplmgFENLYPSYQIIKAL--LKNEKDLEID 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 177 PD--FVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDAHT-------IEHTPKDLDVGGKVVAIVDDMISTGGTICRASD 247
Cdd:PRK06827 206 KDhlMVISPDTGAMDRAKYYASVLGVDLGLFYKRRDYSRVvngrnpiVAHEFLGRDVEGKDVLIVDDMIASGGSMIDAAK 285
|
170 180
....*....|....*....|..
gi 663515100 248 ALRRQGATEVHAACTHGLFTGG 269
Cdd:PRK06827 286 ELKSRGAKKIIVAATFGFFTNG 307
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
167-286 |
3.71e-21 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 87.07 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 167 IAELLQSEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDA------HTIEHTPKDLDVGGKVVAIVDDMISTGG 240
Cdd:cd06223 6 AEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPgrtpsePYGLELPLGGDVKGKRVLLVDDVIATGG 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 663515100 241 TICRASDALRRQGATEVHAACTHGLFTGGAILrLANHVDGVHSTDS 286
Cdd:cd06223 86 TLLAAIELLKEAGAKVVGVAVLLDKPEGGARE-LASPGDPVYSLFT 130
|
|
| Pribosyltran_N |
pfam13793 |
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ... |
1-133 |
8.41e-14 |
|
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.
Pssm-ID: 433483 [Multi-domain] Cd Length: 117 Bit Score: 66.67 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 1 MPVVSGSSGRGVASSLAPLMGMQYIELESRRFPDGEGYVRVPteaiDAVRSEPVVLVSNTYPD--SGIVSTLLLLEAI-- 76
Cdd:pfam13793 1 LKIFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIE----ESVRGKDVFIIQSTCPPvnDNLMELLIMIDALkr 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 663515100 77 ADVRRgdlsnlkgeepqsmddvgggVFLAIPYYGYSRQDKRFSKGEAVSARVIAEIL 133
Cdd:pfam13793 77 ASAKR--------------------ITAVIPYFGYARQDRKDKPREPITAKLVADLL 113
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
176-263 |
2.96e-12 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 63.15 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 176 SPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTR-IDAHTIEHTPKDL--DVGGKVVAIVDDMISTGGTICRASDALRRQ 252
Cdd:pfam00156 29 KPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSyNPDTSEVMKTSSAlpDLKGKTVLIVDDILDTGGTLLKVLELLKNV 108
|
90
....*....|.
gi 663515100 253 GATEVHAACTH 263
Cdd:pfam00156 109 GPKEVKIAVLI 119
|
|
| Pribosyl_synth |
pfam14572 |
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ... |
223-288 |
2.62e-07 |
|
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.
Pssm-ID: 434046 Cd Length: 184 Bit Score: 49.82 E-value: 2.62e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663515100 223 DVGGKVVAIVDDMISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRL-ANHVDGVHSTDSLP 288
Cdd:pfam14572 80 DVGGRIAIIVDDMIDDVDSFVAAAELLKERGAYKIYVMATHGLLSSDAPRLLeASPIDEVVVTNTIP 146
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
161-277 |
3.10e-07 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 49.77 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 161 VSSMPEIAELL---------QSEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRID---AHTIEHTPKDldvgGKV 228
Cdd:COG0461 39 VLSYPEALELLgealaelikELGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAKDhgtGGQIEGGLLP----GER 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 663515100 229 VAIVDDMISTGGTICRASDALRRQGATEVHAACthgLFT--GGAILRLANH 277
Cdd:COG0461 115 VLVVEDVITTGGSVLEAVEALREAGAEVVGVAV---IVDreEGAAENLEEA 162
|
|
| PLN02297 |
PLN02297 |
ribose-phosphate pyrophosphokinase |
220-305 |
3.32e-07 |
|
ribose-phosphate pyrophosphokinase
Pssm-ID: 177934 [Multi-domain] Cd Length: 326 Bit Score: 50.84 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 220 KDLDVGGKVVAIVDDMISTGGTICRASDALRRQGATEVHAACTHGLFTGGAILRLaNHVDGVHS--------TDSLPN-- 289
Cdd:PLN02297 224 KEGNPAGRHVVIVDDLVQSGGTLIECQKVLAAHGAAKVSAYVTHGVFPNESWERF-THDNGGPEagfayfwiTDSCPQtv 302
|
90 100
....*....|....*....|...
gi 663515100 290 -------PRAVVSAAPALARGLQ 305
Cdd:PLN02297 303 kavrgkaPFEVLSLAGSIADALQ 325
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
166-261 |
8.67e-07 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 48.61 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 166 EIAELLQ-SEVSPDFVLSPDKGAISRATEVAGLIGCDFSYLEKTridahtiehtPKDLDVG---------GKVVAIVDDM 235
Cdd:PRK00455 53 FLAEAIKdSGIEFDVVAGPATGGIPLAAAVARALDLPAIFVRKE----------AKDHGEGgqiegrrlfGKRVLVVEDV 122
|
90 100
....*....|....*....|....*.
gi 663515100 236 ISTGGTICRASDALRRQGATEVHAAC 261
Cdd:PRK00455 123 ITTGGSVLEAVEAIRAAGAEVVGVAV 148
|
|
| PRK02304 |
PRK02304 |
adenine phosphoribosyltransferase; Provisional |
226-261 |
1.69e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 235028 Cd Length: 175 Bit Score: 44.30 E-value: 1.69e-05
10 20 30
....*....|....*....|....*....|....*.
gi 663515100 226 GKVVAIVDDMISTGGTICRASDALRRQGATEVHAAC 261
Cdd:PRK02304 114 GDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAF 149
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
164-262 |
1.74e-05 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 44.86 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 164 MPEIAELLQSEVspDFVLSPDKGAISRATEVAGLIGCDFSYLEKTRIDAHTIEHTPKDL-----DVGGKVVAIVDDMIST 238
Cdd:PRK02277 75 MADMLEKEDEEV--DVVVGIAKSGVPLATLVADELGKDLAIYHPKKWDHGEGEKKTGSFsrnfaSVEGKRCVIVDDVITS 152
|
90 100
....*....|....*....|....
gi 663515100 239 GGTICRASDALRRQGATEVhaACT 262
Cdd:PRK02277 153 GTTMKETIEYLKEHGGKPV--AVV 174
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
219-261 |
2.28e-05 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 44.69 E-value: 2.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 663515100 219 PKDLDvgGKVVAIVDDMISTGGTICRASDALRRQGATEVHAAC 261
Cdd:PRK00129 119 PEDID--ERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLC 159
|
|
| PRK11595 |
PRK11595 |
DNA utilization protein GntX; Provisional |
198-261 |
3.23e-05 |
|
DNA utilization protein GntX; Provisional
Pssm-ID: 183221 [Multi-domain] Cd Length: 227 Bit Score: 44.26 E-value: 3.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663515100 198 IGCDFSYLEKTRIDAHTIEHTPK--------------DLDVGGKVVAIVDDMISTGGTICRASDALRRQGATEVHAAC 261
Cdd:PRK11595 145 LGCDYDSEALTRTRATATQHFLSarlrkrnlknafrlELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWC 222
|
|
| PLN02293 |
PLN02293 |
adenine phosphoribosyltransferase |
226-265 |
1.05e-04 |
|
adenine phosphoribosyltransferase
Pssm-ID: 177930 Cd Length: 187 Bit Score: 42.35 E-value: 1.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 663515100 226 GKVVAIVDDMISTGGTICRASDALRRQGATEVHAACTHGL 265
Cdd:PLN02293 125 GERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIEL 164
|
|
| pyrE |
TIGR00336 |
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ... |
167-255 |
2.22e-03 |
|
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129436 [Multi-domain] Cd Length: 173 Bit Score: 38.18 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 167 IAELLQSEVSPDFVLSPDKGAISRATEVagligCDFSYLEKTRIDAHTIEHTPKDLDVGGKV---------VAIVDDMIS 237
Cdd:TIGR00336 45 AAAIIKSHLEFDVIAGPALGGIPIATAV-----SVKLAKPGGDIPLCFNRKEAKDHGEGGNIegellegdkVVVVEDVIT 119
|
90
....*....|....*...
gi 663515100 238 TGGTICRASDALRRQGAT 255
Cdd:TIGR00336 120 TGTSILEAVEIIQAAGGQ 137
|
|
| PRK07322 |
PRK07322 |
adenine phosphoribosyltransferase; Provisional |
165-264 |
2.30e-03 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 180928 Cd Length: 178 Bit Score: 38.42 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515100 165 PEIAELLQSEVspDFVLSPDKGAISRATEVAGLIGCDFSYLEKTR----IDAHTIE------HTPKDL-----DV---GG 226
Cdd:PRK07322 43 EALAKRLPTEV--DVLVTPETKGIPLAHALSRRLGKPYVVARKSRkpymQDPIIQEvvsittGKPQLLvldgaDAeklKG 120
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 663515100 227 KVVAIVDDMISTGGTICRASDALRRQGATEVH--AACTHG 264
Cdd:PRK07322 121 KRVAIVDDVVSTGGTLTALERLVERAGGQVVAkaAIFAEG 160
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
224-258 |
4.85e-03 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 38.48 E-value: 4.85e-03
10 20 30
....*....|....*....|....*....|....*
gi 663515100 224 VGGKVVAIVDDMISTGGTICRASDALRRQGATEVH 258
Cdd:PRK05793 351 VEGKRVVLIDDSIVRGTTSKRLVELLRKAGAKEVH 385
|
|
| Apt |
COG0503 |
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ... |
226-261 |
6.81e-03 |
|
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 440269 Cd Length: 171 Bit Score: 36.59 E-value: 6.81e-03
10 20 30
....*....|....*....|....*....|....*.
gi 663515100 226 GKVVAIVDDMISTGGTICRASDALRRQGATEVHAAC 261
Cdd:COG0503 112 GDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAF 147
|
|
|