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Conserved domains on  [gi|26325436|dbj|BAC26472|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 130-379 2.23e-71

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.


The actual alignment was detected with superfamily member PRK07044:

Pssm-ID: 469663  Cd Length: 252  Bit Score: 232.43  E-value: 2.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVekGSSCFPVDTTGF 209
Cdd:PRK07044  14 EWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVV--DDSPYPVNPAGF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV-GDMAYYDFNGEMEQEADRINLQKCLGPtCKILVLR 288
Cdd:PRK07044  92 TIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  289 NHGMVALGDTVEEAFYKVFHLQAACEVQVSALSsaGGTENLILleqekhrPHEVGSVQWAGSTFGPMQKSrlGEHEFEAL 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQA--GGGELVLP-------PPEVAERTARQSLFDPGAGA--GELAWPAL 239

                        250
                 ....*....|...
gi 26325436  369 MRMLD--NLGYRT 379
Cdd:PRK07044 240 LRKLDriDPGYRD 252
rad23 super family cl36702
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 562-664 2.22e-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]


The actual alignment was detected with superfamily member TIGR00601:

Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 44.12  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   562 DQELEEYK-KE-------VERKKLEQEQEGEKDIATEKPGSPVKSTPASPVQSPSKA--GTKSPAVSPSKTSEDTKKTEV 631
Cdd:TIGR00601  56 DKTVKEYKiKEkdfvvvmVSKPKTGTGKVAPPAATPTSAPTPTPSPPASPASGMSAApaSAVEEKSPSEESATATAPESP 135

                          90       100       110
                  ....*....|....*....|....*....|...
gi 26325436   632 SEANTEPEPVKPEGLVVnGKEEEPSVEEALSKG 664
Cdd:TIGR00601 136 STSVPSSGSDAASTLVV-GSERETTIEEIMEMG 167
fliD super family cl35740
flagellar filament capping protein FliD;
410-598 4.01e-03

flagellar filament capping protein FliD;


The actual alignment was detected with superfamily member PRK08724:

Pssm-ID: 236335 [Multi-domain]  Cd Length: 673  Bit Score: 40.63  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  410 EEDGVPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRNMGSPRPKTTWMKADEVEKSSSGMPI-RIENPNQ---- 484
Cdd:PRK08724 240 DEEGNAIPPADQEVAEEIQDAAQIAQQQEATAALAALEEPISAGGATAAAAGQAAIDAAEAKAYLRPEdRIPGWTEtasg 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  485 -FVPLYTDPQEVLDMRnKIREQNRQDIKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDA-DTKDESEETVPNPFSQLTD 562
Cdd:PRK08724 320 tLLDSYPEPEEELDEA-AIAKAPDVPGWSNTASGTLTDSYVTPKEAQAEIEQKLAQEKAQlDAAVEKGELTPEQAKQIAR 398

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 26325436  563 QELEEYkkevERKKLEQEQEGEKDIATEKPGSPVKS 598
Cdd:PRK08724 399 AKLEPE----ERERLEKIDKAQAALKQAQSAFDLYS 430
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 130-379 2.23e-71

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 232.43  E-value: 2.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVekGSSCFPVDTTGF 209
Cdd:PRK07044  14 EWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVV--DDSPYPVNPAGF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV-GDMAYYDFNGEMEQEADRINLQKCLGPtCKILVLR 288
Cdd:PRK07044  92 TIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  289 NHGMVALGDTVEEAFYKVFHLQAACEVQVSALSsaGGTENLILleqekhrPHEVGSVQWAGSTFGPMQKSrlGEHEFEAL 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQA--GGGELVLP-------PPEVAERTARQSLFDPGAGA--GELAWPAL 239

                        250
                 ....*....|...
gi 26325436  369 MRMLD--NLGYRT 379
Cdd:PRK07044 240 LRKLDriDPGYRD 252
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 130-340 2.64e-69

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: 225.32  E-value: 2.64e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436 130 ERLMRcKISSVYRLLDLYGWaqlsDTYVTLRVSKEQD---HFLISPKGVSCSEVTASSLIKVNILGEVVE--KGSSCFPv 204
Cdd:cd00398   1 EKLKR-KIIAACLLLDLYGW----VTGTGGNVSARDRdrgYFLITPSGVDYEEMTASDLVVVDAQGKVVEgkKPSSETP- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436 205 dttgfsLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV---GDMAYYDFNGEMeQEADRINLQKCLG-P 280
Cdd:cd00398  75 ------LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfP 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26325436 281 TCKILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSSAGG--TENLILLEQEKHRPH 340
Cdd:cd00398 148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 135-317 3.91e-50

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: 172.73  E-value: 3.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   135 CKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKG---SSCFPvdttgfsL 211
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGlkpSSETP-------L 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   212 HSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNA--LLVGDMAYYDfNGEMEQEADRINLQKCLGPTCKILVLRN 289
Cdd:pfam00596  72 HLAIYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAadFLGGDIPIIP-YYTPGTEELGERIAEALGGDRKAVLLRN 150

                         170       180
                  ....*....|....*....|....*...
gi 26325436   290 HGMVALGDTVEEAFYKVFHLQAACEVQV 317
Cdd:pfam00596 151 HGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 137-317 5.45e-46

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: 161.65  E-value: 5.45e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436    137 ISSVYRLLDLYGWAQLSDTYVTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIY 216
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGG--GPKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436    217 AARPDVRCAIHLHTPATAAVSAM--KCGLLPVSHNALLVG-DMAYYDFNGEMEQEADRI-NLQKCLGPT---CKILVLRN 289
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 26325436    290 HGMVALGDTVEEAFYKVFHLQAACEVQV 317
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 130-338 1.42e-44

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: 158.45  E-value: 1.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfpVDTTGF 209
Cdd:COG0235   3 EEELREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL----KPSSET 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHN--ALLVGDMAYYDFNG-EMEQEADRInlQKCLGpTCKILV 286
Cdd:COG0235  77 PLHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGpGTEELAEAI--AEALG-DRPAVL 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 26325436 287 LRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALsSAGGTENLILLEQEKHR 338
Cdd:COG0235 154 LRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLAL-ALGGPLVLSDEEIDKLA 204
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 562-664 2.22e-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: 44.12  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   562 DQELEEYK-KE-------VERKKLEQEQEGEKDIATEKPGSPVKSTPASPVQSPSKA--GTKSPAVSPSKTSEDTKKTEV 631
Cdd:TIGR00601  56 DKTVKEYKiKEkdfvvvmVSKPKTGTGKVAPPAATPTSAPTPTPSPPASPASGMSAApaSAVEEKSPSEESATATAPESP 135

                          90       100       110
                  ....*....|....*....|....*....|...
gi 26325436   632 SEANTEPEPVKPEGLVVnGKEEEPSVEEALSKG 664
Cdd:TIGR00601 136 STSVPSSGSDAASTLVV-GSERETTIEEIMEMG 167
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 514-656 4.76e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.43  E-value: 4.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  514 GPQSQLLASVIAEKSRSPSTESQLMSKGDADT-------KDESEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKD 586
Cdd:PRK13108 299 EPAELAAAAVASAASAVGPVGPGEPNQPDDVAeavkaevAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGD 378

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  587 IATEKPGSPvKSTPASPVQSPSkagtkSPAVSPSKTSEDTKKTEVSEANTEPEPVKPEGLVVNGKEEEPS 656
Cdd:PRK13108 379 LAGQAPAAH-QVDAEAASAAPE-----EPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
fliD PRK08724
flagellar filament capping protein FliD;
410-598 4.01e-03

flagellar filament capping protein FliD;


Pssm-ID: 236335 [Multi-domain]  Cd Length: 673  Bit Score: 40.63  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  410 EEDGVPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRNMGSPRPKTTWMKADEVEKSSSGMPI-RIENPNQ---- 484
Cdd:PRK08724 240 DEEGNAIPPADQEVAEEIQDAAQIAQQQEATAALAALEEPISAGGATAAAAGQAAIDAAEAKAYLRPEdRIPGWTEtasg 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  485 -FVPLYTDPQEVLDMRnKIREQNRQDIKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDA-DTKDESEETVPNPFSQLTD 562
Cdd:PRK08724 320 tLLDSYPEPEEELDEA-AIAKAPDVPGWSNTASGTLTDSYVTPKEAQAEIEQKLAQEKAQlDAAVEKGELTPEQAKQIAR 398

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 26325436  563 QELEEYkkevERKKLEQEQEGEKDIATEKPGSPVKS 598
Cdd:PRK08724 399 AKLEPE----ERERLEKIDKAQAALKQAQSAFDLYS 430
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 530-702 9.20e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 39.00  E-value: 9.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   530 SPSTESQLMSkgdADTKDESeetvPNPFSQLTDQELEEYKKEVERKKleqEQEGEKDIAteKPGSPVKSTPASPVQSPSK 609
Cdd:pfam13254 147 SPTKSSWLES---ALNRPES----PKPKAQPSQPAQPAWMKELNKIR---QSRASVDLG--RPNSFKEVTPVGLMRSPAP 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   610 AG-TKSPAVS-PSKTSEDTKKTEVSEANTE-------PEPVKPEGLVVNGKEEEPSVEE--ALSKGLGQMTTNADTDGDS 678
Cdd:pfam13254 215 GGhSKSPSVSgISADSSPTKEEPSEEADTLstdkeqsPAPTSASEPPPKTKELPKDSEEpaAPSKSAEASTEKKEPDTES 294

                         170       180
                  ....*....|....*....|....
gi 26325436   679 YKDKTESVTSGPLSPEGSPFKSPS 702
Cdd:pfam13254 295 SPETSSEKSAPSLLSPVSKASIDK 318
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 130-379 2.23e-71

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 232.43  E-value: 2.23e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVekGSSCFPVDTTGF 209
Cdd:PRK07044  14 EWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVV--DDSPYPVNPAGF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV-GDMAYYDFNGEMEQEADRINLQKCLGPtCKILVLR 288
Cdd:PRK07044  92 TIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  289 NHGMVALGDTVEEAFYKVFHLQAACEVQVSALSsaGGTENLILleqekhrPHEVGSVQWAGSTFGPMQKSrlGEHEFEAL 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQA--GGGELVLP-------PPEVAERTARQSLFDPGAGA--GELAWPAL 239

                        250
                 ....*....|...
gi 26325436  369 MRMLD--NLGYRT 379
Cdd:PRK07044 240 LRKLDriDPGYRD 252
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 130-340 2.64e-69

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: 225.32  E-value: 2.64e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436 130 ERLMRcKISSVYRLLDLYGWaqlsDTYVTLRVSKEQD---HFLISPKGVSCSEVTASSLIKVNILGEVVE--KGSSCFPv 204
Cdd:cd00398   1 EKLKR-KIIAACLLLDLYGW----VTGTGGNVSARDRdrgYFLITPSGVDYEEMTASDLVVVDAQGKVVEgkKPSSETP- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436 205 dttgfsLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV---GDMAYYDFNGEMeQEADRINLQKCLG-P 280
Cdd:cd00398  75 ------LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfP 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26325436 281 TCKILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSSAGG--TENLILLEQEKHRPH 340
Cdd:cd00398 148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 135-317 3.91e-50

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: 172.73  E-value: 3.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   135 CKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKG---SSCFPvdttgfsL 211
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGlkpSSETP-------L 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   212 HSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNA--LLVGDMAYYDfNGEMEQEADRINLQKCLGPTCKILVLRN 289
Cdd:pfam00596  72 HLAIYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAadFLGGDIPIIP-YYTPGTEELGERIAEALGGDRKAVLLRN 150

                         170       180
                  ....*....|....*....|....*...
gi 26325436   290 HGMVALGDTVEEAFYKVFHLQAACEVQV 317
Cdd:pfam00596 151 HGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 137-317 5.45e-46

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: 161.65  E-value: 5.45e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436    137 ISSVYRLLDLYGWAQLSDTYVTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIY 216
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGG--GPKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436    217 AARPDVRCAIHLHTPATAAVSAM--KCGLLPVSHNALLVG-DMAYYDFNGEMEQEADRI-NLQKCLGPT---CKILVLRN 289
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 26325436    290 HGMVALGDTVEEAFYKVFHLQAACEVQV 317
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 130-338 1.42e-44

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: 158.45  E-value: 1.42e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfpVDTTGF 209
Cdd:COG0235   3 EEELREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL----KPSSET 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHN--ALLVGDMAYYDFNG-EMEQEADRInlQKCLGpTCKILV 286
Cdd:COG0235  77 PLHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGpGTEELAEAI--AEALG-DRPAVL 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 26325436 287 LRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALsSAGGTENLILLEQEKHR 338
Cdd:COG0235 154 LRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLAL-ALGGPLVLSDEEIDKLA 204
PRK06661 PRK06661
hypothetical protein; Provisional
 141-374 4.15e-37

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 138.81  E-value: 4.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  141 YRLLDLYGWAQLSDTYVTLRvSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIYAARP 220
Cdd:PRK06661  11 YRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEE--YQYNKTGYFIHGSIYKTRP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  221 DVRCAIHLHTPATAAVSAMKCGLLPVSHNAL-LVGDMAYYDFNG---EMEQEADRinLQKCLGPTcKILVLRNHGMVALG 296
Cdd:PRK06661  88 DISAIFHYHTPASIAVSALKCGLLPISQWALhFYDRISYHNYNSlalDADKQSSR--LVNDLKQN-YVMLLRNHGAITCG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  297 DTVEEAFYKVFHLQAACEVQVSALSSAggtenlillEQEKHRPhevgSVQWAGSTFGPMQ--KSRLGEHEFEALMRMLDN 374
Cdd:PRK06661 165 KTIHEAMFYTYHLEQACKTQCLLNSTK---------KQELIIP----SVEICKKTVKDLLsfEEDLGKRDWAAWLRLIKM 231
PRK06208 PRK06208
class II aldolase/adducin family protein;
130-354 2.42e-29

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 117.78  E-value: 2.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  130 ERLMR-CKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSscFPVDTTG 208
Cdd:PRK06208  39 ERLHRkQRLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE-GD--RPLNRAA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  209 FSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNAL-LVGDMAYYD-FNGEM--EQEADRInlQKCLGPTcKI 284
Cdd:PRK06208 116 FAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACaFYEDHALFDdFTGVVvdTSEGRRI--AAALGTH-KA 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  285 LVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVsaLSSAGGTENLILLEQEKHRPHEVGSVQWAGSTFGP 354
Cdd:PRK06208 193 VILQNHGLLTVGPSVDAAAWWFIALERACQTQL--LAEAAGPPQPIDHETARHTRSQVGSEYGGWFNFQP 260
PRK06486 PRK06486
aldolase;
165-373 9.63e-24

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 101.33  E-value: 9.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  165 QDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSScfPVDTTGFSLHSAIYAARPDVRCAIHLHTP-ATAAVSAMKCGL 243
Cdd:PRK06486  59 DDLFLVNPYGYAFSEITASDLLICDFDGNVLA-GRG--EPEATAFFIHARIHRAIPRAKAAFHTHMPyATALSLTEGRPL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  244 LPVSHNAllvgdMAYY-------DFNGEM--EQEADRInlQKCLGpTCKILVLRNHGMVALGDTVEEAFYKVFHLQAACE 314
Cdd:PRK06486 136 TTLGQTA-----LKFYgrtavdeDYNGLAldAAEGDRI--ARAMG-DADIVFLKNHGVMVCGPRIAEAWDDLYYLERACE 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26325436  315 VQVSALSSAggtenlillEQEKHRPHEVgsvqwAGSTFGPMqksRLGEHE-----FEALMRMLD 373
Cdd:PRK06486 208 VQVLAMSTG---------RPLVPVDPAI-----AAAVARQM---REGDREsarlhLEALRRTLD 254
PRK07490 PRK07490
hypothetical protein; Provisional
 130-322 6.45e-22

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 95.56  E-value: 6.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNilgevvEKGSSCFP----VD 205
Cdd:PRK07490   8 EEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD------ADDPSTAErpdvPD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  206 TTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCG-LLPVSHNALLVGDMAYYDFN-GEMEQEADRINLQKCLGpTCK 283
Cdd:PRK07490  82 ATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTARFFNRVAVDTLyGGMALEEEGERLAGLLG-DKR 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 26325436  284 ILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSS 322
Cdd:PRK07490 161 RLLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALST 199
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 150-324 3.46e-14

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 73.13  E-value: 3.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  150 AQLSDTYVTLRVskeqdhflispkGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDttgfSLHSAIYAARPDVRCAIHLH 229
Cdd:PRK07090  59 AEAPGTYYTQRL------------GLGFDEITASNLLLVDEDLNVLDGEGMPNPAN----RFHSWIYRARPDVNCIIHTH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  230 TPATAAVSAMKCGLLpVSH--NALLVGDMAYY---------DFNGEMEQEAdrinlqkcLGPTCKILvLRNHGMVALGDT 298
Cdd:PRK07090 123 PPHVAALSMLEVPLV-VSHmdTCPLYDDCAFLkdwpgvpvgNEEGEIISAA--------LGDKRAIL-LSHHGQLVAGKS 192

                        170       180
                 ....*....|....*....|....*.
gi 26325436  299 VEEAFYKVFHLQAACEVQVSAlSSAG 324
Cdd:PRK07090 193 IEEACVLALLIERAARLQLLA-MAAG 217
PRK08130 PRK08130
putative aldolase; Validated
 167-304 2.26e-08

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 54.88  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  167 HFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfPVDTTgfSLHSAIYAARPDVRCAIHLHTPATAAVS--------- 237
Cdd:PRK08130  38 GWLVTPTGSCLGRLDPARLSKVDADGNWLSGDK---PSKEV--PLHRAIYRNNPECGAVVHLHSTHLTALSclggldptn 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26325436  238 ---------AMKCGLLPVshnallvgdMAYY---DfngemEQEADRInlqKCLGPTCKILVLRNHGMVALGDTVEEAFY 304
Cdd:PRK08130 113 vlppftpyyVMRVGHVPL---------IPYYrpgD-----PAIAEAL---AGLAARYRAVLLANHGPVVWGSSLEAAVN 174
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 157-302 2.36e-08

L-ribulose-5-phosphate 4-epimerase; Validated


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 55.01  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  157 VTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSSCFPVDTtgfSLHSAIYAARPDVRCAIHLHTP-ATA- 234
Cdd:PRK06557  35 VSARD-PGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDT---ASHLYVYRHMPDVGGVVHTHSTyATAw 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  235 ---------AVSAMK---CGLLPVSHNAlLVGDmayydfngemeqeaDRIN---LQKCLGPTCKILVLRNHGMVALGDTV 299
Cdd:PRK06557 110 aargepipcVLTAMAdefGGPIPVGPFA-LIGD--------------EAIGkgiVETLKGGRSPAVLMQNHGVFTIGKDA 174


                 ...
gi 26325436  300 EEA 302
Cdd:PRK06557 175 EDA 177
PRK08333 PRK08333
aldolase;
166-305 1.46e-07

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 52.13  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  166 DHFLISPKGVSCSEVTASSLIKVNILGEVVekgSSCFPvdTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLP 245
Cdd:PRK08333  34 NLVFIKATGSVMDELTREQVAVIDLNGNQL---SSVRP--SSEYRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELP 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26325436  246 V--SHNALLVGDMAYYDFngemeQEADRINLQKCLGPTCK---ILVLRNHGMVALGDTVEEAFYK 305
Cdd:PRK08333 109 IitPEAELYLKKIPILPF-----RPAGSVELAEQVAEAMKeydAVIMERHGIVTVGRSLREAFYK 168
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
163-306 8.12e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 50.52  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  163 KEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSScfpVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCG 242
Cdd:PRK06833  35 REQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GER---KPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGWE 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26325436  243 LLPVSHNALLVGD---MAYYDFNG--EMEQEA-----DRinlqkclgptcKILVLRNHGMVALGDTVEEAFYKV 306
Cdd:PRK06833 111 LPAVHYLIAVAGPnvrCAEYATFGtkELAENAfeameDR-----------RAVLLANHGLLAGANNLKNAFNIA 173
PRK08660 PRK08660
aldolase;
165-315 1.21e-06

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 49.18  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  165 QDHFLISPKGVSCSEVTASSLIKVNIL--GEVVEKGSSCFPVdttgfslHSAIYAaRPDVRCAIHLHTPATAAVSAMKCG 242
Cdd:PRK08660  30 GDGLLITRTGSMLDEITEGDVIEVGIDddGSVDPLASSETPV-------HRAIYR-RTSAKAIVHAHPPYAVALSLLEDE 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26325436  243 LLPV-SHNALLVGDMAYYDFNGEMEQEADriNLQKCLGPTcKILVLRNHGMVALGDTVEEAFYKVFHLQAACEV 315
Cdd:PRK08660 102 IVPLdSEGLYFLGTIPVVGGDIGSGELAE--NVARALSEH-KGVVVRGHGTFAIGKTLEEAYIYTSQLEHSCKV 172
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 167-314 2.56e-05

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 46.17  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  167 HFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPvdTTGFSLHSAIYAARPDVRCAIHLHtPATAAVSAMKCGLLPV 246
Cdd:PRK05874  39 NVVITPSSVDYAEMLLHDLVLVDAGGAVLHAKDGRSP--STELNLHLACYRAFDDIGSVIHSH-PVWATMFAVAHEPIPA 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26325436  247 SHNALLV---GDMAYYDFNGEMEQEADRINLQKCLGPTCKILVlrNHGMVALGDTVEeafyKVFHLQAACE 314
Cdd:PRK05874 116 CIDEFAIycgGDVRCTEYAASGTPEVGRNAVRALEGRAAALIA--NHGLVAVGPRPD----QVLRVTALVE 180
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
165-319 5.08e-05

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 45.12  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  165 QDHFLISPKGVSCSEVTASSLIKVNILGEVvEKGSscFPvdTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGlL 244
Cdd:PRK08087  35 QDGMLITPTGIPYEKLTESHIVFVDGNGKH-EEGK--LP--SSEWRFHMAAYQTRPDANAVVHNHAVHCTAVSILNRP-I 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  245 PVSHNALLV--GD----MAYYDFNGEMEQEADRINLQKclgptCKILVLRNHGMVALGDTVEEAfykvfhLQAACEVQVS 318
Cdd:PRK08087 109 PAIHYMIAAagGNsipcAPYATFGTRELSEHVALALKN-----RKATLLQHHGLIACEVNLEKA------LWLAHEVEVL 177


                 .
gi 26325436  319 A 319
Cdd:PRK08087 178 A 178
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 562-664 2.22e-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: 44.12  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   562 DQELEEYK-KE-------VERKKLEQEQEGEKDIATEKPGSPVKSTPASPVQSPSKA--GTKSPAVSPSKTSEDTKKTEV 631
Cdd:TIGR00601  56 DKTVKEYKiKEkdfvvvmVSKPKTGTGKVAPPAATPTSAPTPTPSPPASPASGMSAApaSAVEEKSPSEESATATAPESP 135

                          90       100       110
                  ....*....|....*....|....*....|...
gi 26325436   632 SEANTEPEPVKPEGLVVnGKEEEPSVEEALSKG 664
Cdd:TIGR00601 136 STSVPSSGSDAASTLVV-GSERETTIEEIMEMG 167
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 514-656 4.76e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.43  E-value: 4.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  514 GPQSQLLASVIAEKSRSPSTESQLMSKGDADT-------KDESEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKD 586
Cdd:PRK13108 299 EPAELAAAAVASAASAVGPVGPGEPNQPDDVAeavkaevAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGD 378

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  587 IATEKPGSPvKSTPASPVQSPSkagtkSPAVSPSKTSEDTKKTEVSEANTEPEPVKPEGLVVNGKEEEPS 656
Cdd:PRK13108 379 LAGQAPAAH-QVDAEAASAAPE-----EPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 161-304 5.25e-04

L-ribulose-5-phosphate 4-epimerase; Provisional


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 42.13  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  161 VSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVE---KGSSCFPVdttgfslHSAIYAARPDVRCAIHLHTpaTAAVS 237
Cdd:PRK13145  33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEgdlNPSSDLPT-------HVELYKAWPEVGGIVHTHS--TEAVG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  238 AMKCGL-LP---VSHNALLVGD------MAYYDFNGEMEQEADRINLQ----KCLGP-TCKILVLRNHGMVALGDTVEEA 302
Cdd:PRK13145 104 WAQAGRdIPfygTTHADYFYGPipcarsLTKDEVNGAYEKETGSVIIEefekRGLDPmAVPGIVVRNHGPFTWGKNPEQA 183


                 ..
gi 26325436  303 FY 304
Cdd:PRK13145 184 VY 185
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 141-304 7.12e-04

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183460  Cd Length: 228  Bit Score: 41.71  E-value: 7.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  141 YRLLdLYGWAQLSDtyvtlrVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVE---KGSScfpvDTtgfSLHSAIYA 217
Cdd:PRK12348  18 YGLV-TFTWGNVSA------IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEgeyRPSS----DT---ATHLELYR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  218 ARPDVRCAIHLHTP-ATA-AVSAMKCGLLPVSHNALLVGD------MAYYDFNGEMEQEADRINLQKcLGPTCKI----L 285
Cdd:PRK12348  84 RYPSLGGIVHTHSThATAwAQAGLAIPALGTTHADYFFGDipctrgLSEEEVQGEYELNTGKVIIET-LGNAEPLhtpgI 162

                        170
                 ....*....|....*....
gi 26325436  286 VLRNHGMVALGDTVEEAFY 304
Cdd:PRK12348 163 VVYQHGPFAWGKDAHDAVH 181
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
161-234 3.52e-03

L-ribulose-5-phosphate 4-epimerase AraD;


Pssm-ID: 236181  Cd Length: 231  Bit Score: 39.43  E-value: 3.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26325436  161 VSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVE---KGSScfpvDT-TgfslHSAIYAARPDVRCAIHLHTP-ATA 234
Cdd:PRK08193  32 IDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEgklKPSS----DTpT----HLVLYKAFPEIGGIVHTHSRhATA 102
fliD PRK08724
flagellar filament capping protein FliD;
410-598 4.01e-03

flagellar filament capping protein FliD;


Pssm-ID: 236335 [Multi-domain]  Cd Length: 673  Bit Score: 40.63  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  410 EEDGVPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRNMGSPRPKTTWMKADEVEKSSSGMPI-RIENPNQ---- 484
Cdd:PRK08724 240 DEEGNAIPPADQEVAEEIQDAAQIAQQQEATAALAALEEPISAGGATAAAAGQAAIDAAEAKAYLRPEdRIPGWTEtasg 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436  485 -FVPLYTDPQEVLDMRnKIREQNRQDIKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDA-DTKDESEETVPNPFSQLTD 562
Cdd:PRK08724 320 tLLDSYPEPEEELDEA-AIAKAPDVPGWSNTASGTLTDSYVTPKEAQAEIEQKLAQEKAQlDAAVEKGELTPEQAKQIAR 398

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 26325436  563 QELEEYkkevERKKLEQEQEGEKDIATEKPGSPVKS 598
Cdd:PRK08724 399 AKLEPE----ERERLEKIDKAQAALKQAQSAFDLYS 430
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 530-702 9.20e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 39.00  E-value: 9.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   530 SPSTESQLMSkgdADTKDESeetvPNPFSQLTDQELEEYKKEVERKKleqEQEGEKDIAteKPGSPVKSTPASPVQSPSK 609
Cdd:pfam13254 147 SPTKSSWLES---ALNRPES----PKPKAQPSQPAQPAWMKELNKIR---QSRASVDLG--RPNSFKEVTPVGLMRSPAP 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26325436   610 AG-TKSPAVS-PSKTSEDTKKTEVSEANTE-------PEPVKPEGLVVNGKEEEPSVEE--ALSKGLGQMTTNADTDGDS 678
Cdd:pfam13254 215 GGhSKSPSVSgISADSSPTKEEPSEEADTLstdkeqsPAPTSASEPPPKTKELPKDSEEpaAPSKSAEASTEKKEPDTES 294

                         170       180
                  ....*....|....*....|....
gi 26325436   679 YKDKTESVTSGPLSPEGSPFKSPS 702
Cdd:pfam13254 295 SPETSSEKSAPSLLSPVSKASIDK 318
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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