|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07044 |
PRK07044 |
aldolase II superfamily protein; Provisional |
130-263 |
2.34e-48 |
|
aldolase II superfamily protein; Provisional
Pssm-ID: 235916 Cd Length: 252 Bit Score: 166.56 E-value: 2.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVekGSSCFPVDTTGF 209
Cdd:PRK07044 14 EWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVV--DDSPYPVNPAGF 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148666741 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV-GDMAYYDFNG 263
Cdd:PRK07044 92 TIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEG 146
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
130-283 |
6.98e-46 |
|
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.
Pssm-ID: 238232 [Multi-domain] Cd Length: 209 Bit Score: 158.68 E-value: 6.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 130 ERLMRcKISSVYRLLDLYGWaqlsDTYVTLRVSKEQD---HFLISPKGVSCSEVTASSLIKVNILGEVVE--KGSSCFPv 204
Cdd:cd00398 1 EKLKR-KIIAACLLLDLYGW----VTGTGGNVSARDRdrgYFLITPSGVDYEEMTASDLVVVDAQGKVVEgkKPSSETP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 205 dttgfsLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV---GDMAYYDFNGEMeQEADRINLQKCLG-P 280
Cdd:cd00398 75 ------LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfP 147
|
...
gi 148666741 281 TCK 283
Cdd:cd00398 148 NSK 150
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
135-283 |
2.32e-34 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 459862 [Multi-domain] Cd Length: 178 Bit Score: 126.89 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 135 CKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKG---SSCFPvdttgfsL 211
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGlkpSSETP-------L 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148666741 212 HSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNA--LLVGDMAYYDfNGEMEQEADRINLQKCLGPTCK 283
Cdd:pfam00596 72 HLAIYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAadFLGGDIPIIP-YYTPGTEELGERIAEALGGDRK 144
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
137-272 |
1.50e-31 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 214970 [Multi-domain] Cd Length: 185 Bit Score: 119.66 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 137 ISSVYRLLDLYGWAQLSDTYVTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIY 216
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGG--GPKPSSETPLHLAIY 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148666741 217 AARPDVRCAIHLHTPATAAVSAM--KCGLLPVSHNALLVG-DMAYYDFNGEMEQEADRI 272
Cdd:smart01007 78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEG 136
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
130-272 |
2.98e-30 |
|
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440005 [Multi-domain] Cd Length: 208 Bit Score: 116.85 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfpVDTTGF 209
Cdd:COG0235 3 EEELREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL----KPSSET 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148666741 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHN--ALLVGDMAYYDFNG-EMEQEADRI 272
Cdd:COG0235 77 PLHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGpGTEELAEAI 142
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
314-416 |
1.59e-04 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 43.73 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 314 DQELEEYK-KE-------VERKKLEQEQEGEKDIATEKPGSPVKSTPASPVQSPSKA--GTKSPAVSPSKTSEDTKKTEV 383
Cdd:TIGR00601 56 DKTVKEYKiKEkdfvvvmVSKPKTGTGKVAPPAATPTSAPTPTPSPPASPASGMSAApaSAVEEKSPSEESATATAPESP 135
|
90 100 110
....*....|....*....|....*....|...
gi 148666741 384 SEANTEPEPVKPEGLVVnGKEEEPSVEEALSKG 416
Cdd:TIGR00601 136 STSVPSSGSDAASTLVV-GSERETTIEEIMEMG 167
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
295-408 |
5.39e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 42.27 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 295 ADTKDESEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKDIATEKPGSPvKSTPASPVQSPSkagtkSPAVSPSKT 374
Cdd:PRK13108 335 AEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAH-QVDAEAASAAPE-----EPAALASEA 408
|
90 100 110
....*....|....*....|....*....|....
gi 148666741 375 SEDTKKTEVSEANTEPEPVKPEGLVVNGKEEEPS 408
Cdd:PRK13108 409 HDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07044 |
PRK07044 |
aldolase II superfamily protein; Provisional |
130-263 |
2.34e-48 |
|
aldolase II superfamily protein; Provisional
Pssm-ID: 235916 Cd Length: 252 Bit Score: 166.56 E-value: 2.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVekGSSCFPVDTTGF 209
Cdd:PRK07044 14 EWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVV--DDSPYPVNPAGF 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148666741 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV-GDMAYYDFNG 263
Cdd:PRK07044 92 TIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEG 146
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
130-283 |
6.98e-46 |
|
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.
Pssm-ID: 238232 [Multi-domain] Cd Length: 209 Bit Score: 158.68 E-value: 6.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 130 ERLMRcKISSVYRLLDLYGWaqlsDTYVTLRVSKEQD---HFLISPKGVSCSEVTASSLIKVNILGEVVE--KGSSCFPv 204
Cdd:cd00398 1 EKLKR-KIIAACLLLDLYGW----VTGTGGNVSARDRdrgYFLITPSGVDYEEMTASDLVVVDAQGKVVEgkKPSSETP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 205 dttgfsLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV---GDMAYYDFNGEMeQEADRINLQKCLG-P 280
Cdd:cd00398 75 ------LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfP 147
|
...
gi 148666741 281 TCK 283
Cdd:cd00398 148 NSK 150
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
135-283 |
2.32e-34 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 459862 [Multi-domain] Cd Length: 178 Bit Score: 126.89 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 135 CKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKG---SSCFPvdttgfsL 211
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGlkpSSETP-------L 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148666741 212 HSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNA--LLVGDMAYYDfNGEMEQEADRINLQKCLGPTCK 283
Cdd:pfam00596 72 HLAIYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAadFLGGDIPIIP-YYTPGTEELGERIAEALGGDRK 144
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
137-272 |
1.50e-31 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 214970 [Multi-domain] Cd Length: 185 Bit Score: 119.66 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 137 ISSVYRLLDLYGWAQLSDTYVTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIY 216
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGG--GPKPSSETPLHLAIY 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148666741 217 AARPDVRCAIHLHTPATAAVSAM--KCGLLPVSHNALLVG-DMAYYDFNGEMEQEADRI 272
Cdd:smart01007 78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEG 136
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
130-272 |
2.98e-30 |
|
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440005 [Multi-domain] Cd Length: 208 Bit Score: 116.85 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfpVDTTGF 209
Cdd:COG0235 3 EEELREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL----KPSSET 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148666741 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHN--ALLVGDMAYYDFNG-EMEQEADRI 272
Cdd:COG0235 77 PLHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGpGTEELAEAI 142
|
|
| PRK06661 |
PRK06661 |
hypothetical protein; Provisional |
141-262 |
2.03e-25 |
|
hypothetical protein; Provisional
Pssm-ID: 168637 Cd Length: 231 Bit Score: 104.14 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 141 YRLLDLYGWAQLSDTYVTLRvSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIYAARP 220
Cdd:PRK06661 11 YRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEE--YQYNKTGYFIHGSIYKTRP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 148666741 221 DVRCAIHLHTPATAAVSAMKCGLLPVSHNAL-LVGDMAYYDFN 262
Cdd:PRK06661 88 DISAIFHYHTPASIAVSALKCGLLPISQWALhFYDRISYHNYN 130
|
|
| PRK06208 |
PRK06208 |
class II aldolase/adducin family protein; |
86-272 |
2.66e-18 |
|
class II aldolase/adducin family protein;
Pssm-ID: 235743 Cd Length: 274 Bit Score: 84.66 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 86 ALRQIADFMASTSHAVFPASSMNFSMMTPINDlhtadslnlAKGERLMR-CKISSVYRLLDLYGWAQLSDTYVTLRVSKE 164
Cdd:PRK06208 4 VLSRAADTAAALSIPQPPREGLWFPRPPPFAT---------VAEERLHRkQRLAAAFRLFARFGFDEGLAGHITARDPEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 165 QDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSscFPVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLL 244
Cdd:PRK06208 75 PDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE-GD--RPLNRAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLD 151
|
170 180 190
....*....|....*....|....*....|..
gi 148666741 245 PVSHNAL-LVGDMAYYD-FNGEM--EQEADRI 272
Cdd:PRK06208 152 PITQDACaFYEDHALFDdFTGVVvdTSEGRRI 183
|
|
| PRK06486 |
PRK06486 |
aldolase; |
165-272 |
3.00e-11 |
|
aldolase;
Pssm-ID: 235814 Cd Length: 262 Bit Score: 63.58 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 165 QDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSScfPVDTTGFSLHSAIYAARPDVRCAIHLHTP-ATAAVSAMKCGL 243
Cdd:PRK06486 59 DDLFLVNPYGYAFSEITASDLLICDFDGNVLA-GRG--EPEATAFFIHARIHRAIPRAKAAFHTHMPyATALSLTEGRPL 135
|
90 100 110
....*....|....*....|....*....|....*...
gi 148666741 244 LPVSHNAllvgdMAYY-------DFNGEM--EQEADRI 272
Cdd:PRK06486 136 TTLGQTA-----LKFYgrtavdeDYNGLAldAAEGDRI 168
|
|
| PRK07490 |
PRK07490 |
hypothetical protein; Provisional |
130-279 |
2.79e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236031 [Multi-domain] Cd Length: 245 Bit Score: 60.50 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNilgevvEKGSSCFP----VD 205
Cdd:PRK07490 8 EEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD------ADDPSTAErpdvPD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148666741 206 TTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCG-LLPVSHNALLVGDMAYYDFN-GEMEQEADRINLQKCLG 279
Cdd:PRK07490 82 ATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTARFFNRVAVDTLyGGMALEEEGERLAGLLG 157
|
|
| PRK07090 |
PRK07090 |
class II aldolase/adducin domain protein; Provisional |
150-258 |
7.92e-10 |
|
class II aldolase/adducin domain protein; Provisional
Pssm-ID: 180832 Cd Length: 260 Bit Score: 59.26 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 150 AQLSDTYVTLRVskeqdhflispkGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDttgfSLHSAIYAARPDVRCAIHLH 229
Cdd:PRK07090 59 AEAPGTYYTQRL------------GLGFDEITASNLLLVDEDLNVLDGEGMPNPAN----RFHSWIYRARPDVNCIIHTH 122
|
90 100 110
....*....|....*....|....*....|.
gi 148666741 230 TPATAAVSAMKCGLLpVSH--NALLVGDMAY 258
Cdd:PRK07090 123 PPHVAALSMLEVPLV-VSHmdTCPLYDDCAF 152
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
157-234 |
8.30e-08 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 52.70 E-value: 8.30e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148666741 157 VTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSSCFPVDTtgfSLHSAIYAARPDVRCAIHLHTP-ATA 234
Cdd:PRK06557 35 VSARD-PGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDT---ASHLYVYRHMPDVGGVVHTHSTyATA 108
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
167-319 |
2.80e-06 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 47.95 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 167 HFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfPVDTTgfSLHSAIYAARPDVRCAIHLHTPATAAVS--------- 237
Cdd:PRK08130 38 GWLVTPTGSCLGRLDPARLSKVDADGNWLSGDK---PSKEV--PLHRAIYRNNPECGAVVHLHSTHLTALSclggldptn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 238 ---------AMKCGLLPVshnallvgdMAYY-----DFNGEMEQEADRIN--LQKCLGP--TCKSTESQlmskgdADTKD 299
Cdd:PRK08130 113 vlppftpyyVMRVGHVPL---------IPYYrpgdpAIAEALAGLAARYRavLLANHGPvvWGSSLEAA------VNATE 177
|
170 180
....*....|....*....|....*..
gi 148666741 300 ESEETV-------PNPFSQLTDQELEE 319
Cdd:PRK08130 178 ELEETAklilllgGRPPRYLTDEEIAE 204
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
163-248 |
1.76e-05 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 45.90 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 163 KEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSScfpVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCG 242
Cdd:PRK06833 35 REQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GER---KPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGWE 110
|
....*.
gi 148666741 243 LLPVSH 248
Cdd:PRK06833 111 LPAVHY 116
|
|
| PRK08333 |
PRK08333 |
aldolase; |
166-246 |
2.37e-05 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 44.81 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 166 DHFLISPKGVSCSEVTASSLIKVNILGEVVekgSSCFPvdTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLP 245
Cdd:PRK08333 34 NLVFIKATGSVMDELTREQVAVIDLNGNQL---SSVRP--SSEYRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELP 108
|
.
gi 148666741 246 V 246
Cdd:PRK08333 109 I 109
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
314-416 |
1.59e-04 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 43.73 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 314 DQELEEYK-KE-------VERKKLEQEQEGEKDIATEKPGSPVKSTPASPVQSPSKA--GTKSPAVSPSKTSEDTKKTEV 383
Cdd:TIGR00601 56 DKTVKEYKiKEkdfvvvmVSKPKTGTGKVAPPAATPTSAPTPTPSPPASPASGMSAApaSAVEEKSPSEESATATAPESP 135
|
90 100 110
....*....|....*....|....*....|...
gi 148666741 384 SEANTEPEPVKPEGLVVnGKEEEPSVEEALSKG 416
Cdd:TIGR00601 136 STSVPSSGSDAASTLVV-GSERETTIEEIMEMG 167
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
295-408 |
5.39e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 42.27 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 295 ADTKDESEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKDIATEKPGSPvKSTPASPVQSPSkagtkSPAVSPSKT 374
Cdd:PRK13108 335 AEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAH-QVDAEAASAAPE-----EPAALASEA 408
|
90 100 110
....*....|....*....|....*....|....
gi 148666741 375 SEDTKKTEVSEANTEPEPVKPEGLVVNGKEEEPS 408
Cdd:PRK13108 409 HDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
141-256 |
1.17e-03 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 40.55 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148666741 141 YRLLdLYGWAQLSDtyvtlrVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVE---KGSScfpvDTtgfSLHSAIYA 217
Cdd:PRK12348 18 YGLV-TFTWGNVSA------IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEgeyRPSS----DT---ATHLELYR 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 148666741 218 ARPDVRCAIHLHTP-ATA-AVSAMKCGLLPVSHNALLVGDM 256
Cdd:PRK12348 84 RYPSLGGIVHTHSThATAwAQAGLAIPALGTTHADYFFGDI 124
|
|
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
161-234 |
2.17e-03 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 39.43 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148666741 161 VSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVE---KGSScfpvDT-TgfslHSAIYAARPDVRCAIHLHTP-ATA 234
Cdd:PRK08193 32 IDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEgklKPSS----DTpT----HLVLYKAFPEIGGIVHTHSRhATA 102
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
165-237 |
8.15e-03 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 37.80 E-value: 8.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148666741 165 QDHFLISPKGVSCSEVTASSLIKVNILGEVvEKGSscFPvdTTGFSLHSAIYAARPDVRCAIHLHTPATAAVS 237
Cdd:PRK08087 35 QDGMLITPTGIPYEKLTESHIVFVDGNGKH-EEGK--LP--SSEWRFHMAAYQTRPDANAVVHNHAVHCTAVS 102
|
|
|