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Conserved domains on  [gi|158081763|ref|NP_001103350|]
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beta-adducin isoform a [Rattus norvegicus]

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 3.39e-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: 3.39e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVekGSSCFPVDTTGF 209
Cdd:PRK07044  14 EWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVV--DDSPYPVNPAGF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV-GDMAYYDFNGEMEQEADRINLQKCLGPtCKILVLR 288
Cdd:PRK07044  92 TIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 289 NHGMVALGDTVEEAFYKVFHLQAACEVQVSALSsaGGTENLILleqekhrPHEVGSVQWAGSTFGPMQKSrlGEHEFEAL 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQA--GGGELVLP-------PPEVAERTARQSLFDPGAGA--GELAWPAL 239

                        250
                 ....*....|...
gi 158081763 369 MRMLD--NLGYRT 379
Cdd:PRK07044 240 LRKLDriDPGYRD 252
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
514-656 3.16e-04

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 43.81  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 514 GPQSQLLASVIAEKSRSPSTESQLASKGDADTKDELEETvpnpfSQLTDQELEEYKKEVERKKLEQ----EQEGEKDAAT 589
Cdd:PRK13108 299 EPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEV-----AEVTDEVAAESVVQVADRDGEStpavEETSEADIER 373

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158081763 590 EEPGSPVKSTPASPVQSPTRAGTK--SPAVSPSKASEDAKKTEVSEANTEPEPEKPEGVVVNGKEEEPS 656
Cdd:PRK13108 374 EQPGDLAGQAPAAHQVDAEAASAApeEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
DUF612 super family cl37536
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
 388-692 2.06e-03

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


The actual alignment was detected with superfamily member pfam04747:

Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 41.20  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  388 VQEKTKHKSEVEIPATVTAFVFEEDGVPVPALRQHAQKQQKEKTRwLNTPntylrVNVADEVQRNMGSPRPKTTWMKADE 467
Cdd:pfam04747 153 VKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTP-TNTP-----AEPAEQVQEITGKKNKKNKKKSESE 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  468 VEKSSSGMPIRIENPNQFVP---LYTDPQEVLDMRNKiREQNRQDIKSAgpqSQLLASVIAEKSrSPSTESQLASKGDaD 544
Cdd:pfam04747 227 ATAAPASVEQVVEQPKVVTEephQQAAPQEKKNKKNK-RKSESENVPAA---SETPVEPVVETT-PPASENQKKNKKD-K 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  545 TKDELEETVPNPfsqlTDQELEEYKKEVERKKLE-----QEQEGEKDAATEEPGSPVKSTPASPVQSPTRAGTKSPAVSP 619
Cdd:pfam04747 301 KKSESEKVVEEP----VQAEAPKSKKPTADDNMDfldfvTAKEEPKDEPAETPAAPVEEVVENVVENVVEKSTTPPATEN 376

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158081763  620 SKASEDAKKTEVSEANTEPEPEKPEGvvvngkeeEPSVEEVLSKGPGQMTTNADTDGDSYKDKTESVTSGPLS 692
Cdd:pfam04747 377 KKKNKKDKKKSESEKVTEQPVESAPA--------PPQVEQVVETTPPASENKKKNKKDKKKSESEKAVEEPVQ 441
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 130-379 3.39e-71

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 232.43  E-value: 3.39e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVekGSSCFPVDTTGF 209
Cdd:PRK07044  14 EWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVV--DDSPYPVNPAGF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV-GDMAYYDFNGEMEQEADRINLQKCLGPtCKILVLR 288
Cdd:PRK07044  92 TIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 289 NHGMVALGDTVEEAFYKVFHLQAACEVQVSALSsaGGTENLILleqekhrPHEVGSVQWAGSTFGPMQKSrlGEHEFEAL 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQA--GGGELVLP-------PPEVAERTARQSLFDPGAGA--GELAWPAL 239

                        250
                 ....*....|...
gi 158081763 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 3.93e-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: 3.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 130 ERLMRcKISSVYRLLDLYGWaqlsDTYVTLRVSKEQD---HFLISPKGVSCSEVTASSLIKVNILGEVVE--KGSSCFPv 204
Cdd:cd00398    1 EKLKR-KIIAACLLLDLYGW----VTGTGGNVSARDRdrgYFLITPSGVDYEEMTASDLVVVDAQGKVVEgkKPSSETP- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 205 dttgfsLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV---GDMAYYDFNGEMeQEADRINLQKCLG-P 280
Cdd:cd00398   75 ------LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfP 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158081763 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 4.92e-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: 4.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  135 CKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKG---SSCFPvdttgfsL 211
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGlkpSSETP-------L 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  212 HSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNA--LLVGDMAYYDfNGEMEQEADRINLQKCLGPTCKILVLRN 289
Cdd:pfam00596  72 HLAIYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAadFLGGDIPIIP-YYTPGTEELGERIAEALGGDRKAVLLRN 150

                         170       180
                  ....*....|....*....|....*...
gi 158081763  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 6.58e-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: 6.58e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763   137 ISSVYRLLDLYGWAQLSDTYVTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIY 216
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGG--GPKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763   217 AARPDVRCAIHLHTPATAAVSAM--KCGLLPVSHNALLVG-DMAYYDFNGEMEQEADRI-NLQKCLGPT---CKILVLRN 289
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 158081763   290 HGMVALGDTVEEAFYKVFHLQAACEVQV 317
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 130-338 1.69e-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: 1.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfpVDTTGF 209
Cdd:COG0235    3 EEELREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL----KPSSET 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHN--ALLVGDMAYYDFNG-EMEQEADRInlQKCLGpTCKILV 286
Cdd:COG0235   77 PLHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGpGTEELAEAI--AEALG-DRPAVL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158081763 287 LRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALsSAGGTENLILLEQEKHR 338
Cdd:COG0235  154 LRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLAL-ALGGPLVLSDEEIDKLA 204
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 514-656 3.16e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.81  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 514 GPQSQLLASVIAEKSRSPSTESQLASKGDADTKDELEETvpnpfSQLTDQELEEYKKEVERKKLEQ----EQEGEKDAAT 589
Cdd:PRK13108 299 EPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEV-----AEVTDEVAAESVVQVADRDGEStpavEETSEADIER 373

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158081763 590 EEPGSPVKSTPASPVQSPTRAGTK--SPAVSPSKASEDAKKTEVSEANTEPEPEKPEGVVVNGKEEEPS 656
Cdd:PRK13108 374 EQPGDLAGQAPAAHQVDAEAASAApeEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 562-664 1.14e-03

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: 41.80  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  562 DQELEEYK-KE-------VERKKLEQEQEGEKDAATEEPGSPVKSTPASPvqsptragTKSPAVSPSKASEDAKKTEVSE 633
Cdd:TIGR00601  56 DKTVKEYKiKEkdfvvvmVSKPKTGTGKVAPPAATPTSAPTPTPSPPASP--------ASGMSAAPASAVEEKSPSEESA 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 158081763  634 ANTEPEPEKPEG---------VVVNGKEEEPSVEEVLSKG 664
Cdd:TIGR00601 128 TATAPESPSTSVpssgsdaasTLVVGSERETTIEEIMEMG 167
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
 388-692 2.06e-03

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 41.20  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  388 VQEKTKHKSEVEIPATVTAFVFEEDGVPVPALRQHAQKQQKEKTRwLNTPntylrVNVADEVQRNMGSPRPKTTWMKADE 467
Cdd:pfam04747 153 VKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTP-TNTP-----AEPAEQVQEITGKKNKKNKKKSESE 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  468 VEKSSSGMPIRIENPNQFVP---LYTDPQEVLDMRNKiREQNRQDIKSAgpqSQLLASVIAEKSrSPSTESQLASKGDaD 544
Cdd:pfam04747 227 ATAAPASVEQVVEQPKVVTEephQQAAPQEKKNKKNK-RKSESENVPAA---SETPVEPVVETT-PPASENQKKNKKD-K 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  545 TKDELEETVPNPfsqlTDQELEEYKKEVERKKLE-----QEQEGEKDAATEEPGSPVKSTPASPVQSPTRAGTKSPAVSP 619
Cdd:pfam04747 301 KKSESEKVVEEP----VQAEAPKSKKPTADDNMDfldfvTAKEEPKDEPAETPAAPVEEVVENVVENVVEKSTTPPATEN 376

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158081763  620 SKASEDAKKTEVSEANTEPEPEKPEGvvvngkeeEPSVEEVLSKGPGQMTTNADTDGDSYKDKTESVTSGPLS 692
Cdd:pfam04747 377 KKKNKKDKKKSESEKVTEQPVESAPA--------PPQVEQVVETTPPASENKKKNKKDKKKSESEKAVEEPVQ 441
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 130-379 3.39e-71

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 232.43  E-value: 3.39e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVekGSSCFPVDTTGF 209
Cdd:PRK07044  14 EWQARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVV--DDSPYPVNPAGF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV-GDMAYYDFNGEMEQEADRINLQKCLGPtCKILVLR 288
Cdd:PRK07044  92 TIHSAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 289 NHGMVALGDTVEEAFYKVFHLQAACEVQVSALSsaGGTENLILleqekhrPHEVGSVQWAGSTFGPMQKSrlGEHEFEAL 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQA--GGGELVLP-------PPEVAERTARQSLFDPGAGA--GELAWPAL 239

                        250
                 ....*....|...
gi 158081763 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 3.93e-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: 3.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 130 ERLMRcKISSVYRLLDLYGWaqlsDTYVTLRVSKEQD---HFLISPKGVSCSEVTASSLIKVNILGEVVE--KGSSCFPv 204
Cdd:cd00398    1 EKLKR-KIIAACLLLDLYGW----VTGTGGNVSARDRdrgYFLITPSGVDYEEMTASDLVVVDAQGKVVEgkKPSSETP- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 205 dttgfsLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLV---GDMAYYDFNGEMeQEADRINLQKCLG-P 280
Cdd:cd00398   75 ------LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfP 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158081763 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 4.92e-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: 4.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  135 CKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKG---SSCFPvdttgfsL 211
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGlkpSSETP-------L 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  212 HSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNA--LLVGDMAYYDfNGEMEQEADRINLQKCLGPTCKILVLRN 289
Cdd:pfam00596  72 HLAIYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAadFLGGDIPIIP-YYTPGTEELGERIAEALGGDRKAVLLRN 150

                         170       180
                  ....*....|....*....|....*...
gi 158081763  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 6.58e-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: 6.58e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763   137 ISSVYRLLDLYGWAQLSDTYVTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIY 216
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGG--GPKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763   217 AARPDVRCAIHLHTPATAAVSAM--KCGLLPVSHNALLVG-DMAYYDFNGEMEQEADRI-NLQKCLGPT---CKILVLRN 289
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 158081763   290 HGMVALGDTVEEAFYKVFHLQAACEVQV 317
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 130-338 1.69e-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: 1.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVskEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfpVDTTGF 209
Cdd:COG0235    3 EEELREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDL----KPSSET 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 210 SLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHN--ALLVGDMAYYDFNG-EMEQEADRInlQKCLGpTCKILV 286
Cdd:COG0235   77 PLHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGpGTEELAEAI--AEALG-DRPAVL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158081763 287 LRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALsSAGGTENLILLEQEKHR 338
Cdd:COG0235  154 LRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLAL-ALGGPLVLSDEEIDKLA 204
PRK06661 PRK06661
hypothetical protein; Provisional
 141-374 4.61e-37

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 138.81  E-value: 4.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 141 YRLLDLYGWAQLSDTYVTLRvSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscFPVDTTGFSLHSAIYAARP 220
Cdd:PRK06661  11 YRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEE--YQYNKTGYFIHGSIYKTRP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 221 DVRCAIHLHTPATAAVSAMKCGLLPVSHNAL-LVGDMAYYDFNG---EMEQEADRinLQKCLGPTcKILVLRNHGMVALG 296
Cdd:PRK06661  88 DISAIFHYHTPASIAVSALKCGLLPISQWALhFYDRISYHNYNSlalDADKQSSR--LVNDLKQN-YVMLLRNHGAITCG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 297 DTVEEAFYKVFHLQAACEVQVSALSSAggtenlillEQEKHRPhevgSVQWAGSTFGPMQ--KSRLGEHEFEALMRMLDN 374
Cdd:PRK06661 165 KTIHEAMFYTYHLEQACKTQCLLNSTK---------KQELIIP----SVEICKKTVKDLLsfEEDLGKRDWAAWLRLIKM 231
PRK06208 PRK06208
class II aldolase/adducin family protein;
86-354 1.92e-29

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 118.17  E-value: 1.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  86 ALRQIADFMASTSHAVFPASSMNFSMMTPINDlhtadslnlAKGERLMR-CKISSVYRLLDLYGWAQLSDTYVTLRVSKE 164
Cdd:PRK06208   4 VLSRAADTAAALSIPQPPREGLWFPRPPPFAT---------VAEERLHRkQRLAAAFRLFARFGFDEGLAGHITARDPEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 165 QDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSscFPVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLL 244
Cdd:PRK06208  75 PDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE-GD--RPLNRAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 245 PVSHNAL-LVGDMAYYD-FNGEM--EQEADRInlQKCLGPTcKILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVsaL 320
Cdd:PRK06208 152 PITQDACaFYEDHALFDdFTGVVvdTSEGRRI--AAALGTH-KAVILQNHGLLTVGPSVDAAAWWFIALERACQTQL--L 226

                        250       260       270
                 ....*....|....*....|....*....|....
gi 158081763 321 SSAGGTENLILLEQEKHRPHEVGSVQWAGSTFGP 354
Cdd:PRK06208 227 AEAAGPPQPIDHETARHTRSQVGSEYGGWFNFQP 260
PRK06486 PRK06486
aldolase;
165-373 1.01e-23

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 101.33  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 165 QDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSScfPVDTTGFSLHSAIYAARPDVRCAIHLHTP-ATAAVSAMKCGL 243
Cdd:PRK06486  59 DDLFLVNPYGYAFSEITASDLLICDFDGNVLA-GRG--EPEATAFFIHARIHRAIPRAKAAFHTHMPyATALSLTEGRPL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 244 LPVSHNAllvgdMAYY-------DFNGEM--EQEADRInlQKCLGpTCKILVLRNHGMVALGDTVEEAFYKVFHLQAACE 314
Cdd:PRK06486 136 TTLGQTA-----LKFYgrtavdeDYNGLAldAAEGDRI--ARAMG-DADIVFLKNHGVMVCGPRIAEAWDDLYYLERACE 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158081763 315 VQVSALSSAggtenlillEQEKHRPHEVgsvqwAGSTFGPMqksRLGEHE-----FEALMRMLD 373
Cdd:PRK06486 208 VQVLAMSTG---------RPLVPVDPAI-----AAAVARQM---REGDREsarlhLEALRRTLD 254
PRK07490 PRK07490
hypothetical protein; Provisional
 130-322 7.27e-22

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 95.17  E-value: 7.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 130 ERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNilgevvEKGSSCFP----VD 205
Cdd:PRK07490   8 EEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD------ADDPSTAErpdvPD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 206 TTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCG-LLPVSHNALLVGDMAYYDFN-GEMEQEADRINLQKCLGpTCK 283
Cdd:PRK07490  82 ATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTARFFNRVAVDTLyGGMALEEEGERLAGLLG-DKR 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 158081763 284 ILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSS 322
Cdd:PRK07490 161 RLLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALST 199
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 150-324 3.61e-14

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 73.13  E-value: 3.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 150 AQLSDTYVTLRVskeqdhflispkGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDttgfSLHSAIYAARPDVRCAIHLH 229
Cdd:PRK07090  59 AEAPGTYYTQRL------------GLGFDEITASNLLLVDEDLNVLDGEGMPNPAN----RFHSWIYRARPDVNCIIHTH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 230 TPATAAVSAMKCGLLpVSH--NALLVGDMAYY---------DFNGEMEQEAdrinlqkcLGPTCKILvLRNHGMVALGDT 298
Cdd:PRK07090 123 PPHVAALSMLEVPLV-VSHmdTCPLYDDCAFLkdwpgvpvgNEEGEIISAA--------LGDKRAIL-LSHHGQLVAGKS 192

                        170       180
                 ....*....|....*....|....*.
gi 158081763 299 VEEAFYKVFHLQAACEVQVSAlSSAG 324
Cdd:PRK07090 193 IEEACVLALLIERAARLQLLA-MAAG 217
PRK08130 PRK08130
putative aldolase; Validated
 167-304 2.94e-08

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 54.88  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 167 HFLISPKGVSCSEVTASSLIKVNILGEVVEKGSscfPVDTTgfSLHSAIYAARPDVRCAIHLHTPATAAVS--------- 237
Cdd:PRK08130  38 GWLVTPTGSCLGRLDPARLSKVDADGNWLSGDK---PSKEV--PLHRAIYRNNPECGAVVHLHSTHLTALSclggldptn 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158081763 238 ---------AMKCGLLPVshnallvgdMAYY---DfngemEQEADRInlqKCLGPTCKILVLRNHGMVALGDTVEEAFY 304
Cdd:PRK08130 113 vlppftpyyVMRVGHVPL---------IPYYrpgD-----PAIAEAL---AGLAARYRAVLLANHGPVVWGSSLEAAVN 174
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 157-302 3.10e-08

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 54.63  E-value: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 157 VTLRVsKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSSCFPVDTtgfSLHSAIYAARPDVRCAIHLHTP-ATA- 234
Cdd:PRK06557  35 VSARD-PGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDT---ASHLYVYRHMPDVGGVVHTHSTyATAw 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 235 ---------AVSAMK---CGLLPVSHNAlLVGDmayydfngemeqeaDRIN---LQKCLGPTCKILVLRNHGMVALGDTV 299
Cdd:PRK06557 110 aargepipcVLTAMAdefGGPIPVGPFA-LIGD--------------EAIGkgiVETLKGGRSPAVLMQNHGVFTIGKDA 174


                 ...
gi 158081763 300 EEA 302
Cdd:PRK06557 175 EDA 177
PRK08333 PRK08333
aldolase;
166-305 1.57e-07

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 52.13  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 166 DHFLISPKGVSCSEVTASSLIKVNILGEVVekgSSCFPvdTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLP 245
Cdd:PRK08333  34 NLVFIKATGSVMDELTREQVAVIDLNGNQL---SSVRP--SSEYRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELP 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158081763 246 V--SHNALLVGDMAYYDFngemeQEADRINLQKCLGPTCK---ILVLRNHGMVALGDTVEEAFYK 305
Cdd:PRK08333 109 IitPEAELYLKKIPILPF-----RPAGSVELAEQVAEAMKeydAVIMERHGIVTVGRSLREAFYK 168
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
163-306 8.29e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 50.52  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 163 KEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEkGSScfpVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCG 242
Cdd:PRK06833  35 REQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GER---KPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGWE 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158081763 243 LLPVSHNALLVGD---MAYYDFNG--EMEQEA-----DRinlqkclgptcKILVLRNHGMVALGDTVEEAFYKV 306
Cdd:PRK06833 111 LPAVHYLIAVAGPnvrCAEYATFGtkELAENAfeameDR-----------RAVLLANHGLLAGANNLKNAFNIA 173
PRK08660 PRK08660
aldolase;
165-315 1.38e-06

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 49.18  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 165 QDHFLISPKGVSCSEVTASSLIKVNIL--GEVVEKGSSCFPVdttgfslHSAIYAaRPDVRCAIHLHTPATAAVSAMKCG 242
Cdd:PRK08660  30 GDGLLITRTGSMLDEITEGDVIEVGIDddGSVDPLASSETPV-------HRAIYR-RTSAKAIVHAHPPYAVALSLLEDE 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158081763 243 LLPV-SHNALLVGDMAYYDFNGEMEQEADriNLQKCLGPTcKILVLRNHGMVALGDTVEEAFYKVFHLQAACEV 315
Cdd:PRK08660 102 IVPLdSEGLYFLGTIPVVGGDIGSGELAE--NVARALSEH-KGVVVRGHGTFAIGKTLEEAYIYTSQLEHSCKV 172
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 167-314 2.66e-05

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 46.17  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 167 HFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPvdTTGFSLHSAIYAARPDVRCAIHLHtPATAAVSAMKCGLLPV 246
Cdd:PRK05874  39 NVVITPSSVDYAEMLLHDLVLVDAGGAVLHAKDGRSP--STELNLHLACYRAFDDIGSVIHSH-PVWATMFAVAHEPIPA 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158081763 247 SHNALLV---GDMAYYDFNGEMEQEADRINLQKCLGPTCKILVlrNHGMVALGDTVEeafyKVFHLQAACE 314
Cdd:PRK05874 116 CIDEFAIycgGDVRCTEYAASGTPEVGRNAVRALEGRAAALIA--NHGLVAVGPRPD----QVLRVTALVE 180
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
165-319 5.23e-05

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 45.12  E-value: 5.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 165 QDHFLISPKGVSCSEVTASSLIKVNILGEVvEKGSscFPvdTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGlL 244
Cdd:PRK08087  35 QDGMLITPTGIPYEKLTESHIVFVDGNGKH-EEGK--LP--SSEWRFHMAAYQTRPDANAVVHNHAVHCTAVSILNRP-I 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 245 PVSHNALLV--GD----MAYYDFNGEMEQEADRINLQKclgptCKILVLRNHGMVALGDTVEEAfykvfhLQAACEVQVS 318
Cdd:PRK08087 109 PAIHYMIAAagGNsipcAPYATFGTRELSEHVALALKN-----RKATLLQHHGLIACEVNLEKA------LWLAHEVEVL 177


                 .
gi 158081763 319 A 319
Cdd:PRK08087 178 A 178
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 514-656 3.16e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.81  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 514 GPQSQLLASVIAEKSRSPSTESQLASKGDADTKDELEETvpnpfSQLTDQELEEYKKEVERKKLEQ----EQEGEKDAAT 589
Cdd:PRK13108 299 EPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEV-----AEVTDEVAAESVVQVADRDGEStpavEETSEADIER 373

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158081763 590 EEPGSPVKSTPASPVQSPTRAGTK--SPAVSPSKASEDAKKTEVSEANTEPEPEKPEGVVVNGKEEEPS 656
Cdd:PRK13108 374 EQPGDLAGQAPAAHQVDAEAASAApeEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 161-304 6.54e-04

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 42.13  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 161 VSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVE---KGSSCFPVdttgfslHSAIYAARPDVRCAIHLHTpaTAAVS 237
Cdd:PRK13145  33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEgdlNPSSDLPT-------HVELYKAWPEVGGIVHTHS--TEAVG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 238 AMKCGL-LP---VSHNALLVGD------MAYYDFNGEMEQEADRINLQ----KCLGP-TCKILVLRNHGMVALGDTVEEA 302
Cdd:PRK13145 104 WAQAGRdIPfygTTHADYFYGPipcarsLTKDEVNGAYEKETGSVIIEefekRGLDPmAVPGIVVRNHGPFTWGKNPEQA 183


                 ..
gi 158081763 303 FY 304
Cdd:PRK13145 184 VY 185
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 141-304 7.75e-04

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 41.71  E-value: 7.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 141 YRLLdLYGWAQLSDtyvtlrVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVE---KGSScfpvDTtgfSLHSAIYA 217
Cdd:PRK12348  18 YGLV-TFTWGNVSA------IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEgeyRPSS----DT---ATHLELYR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763 218 ARPDVRCAIHLHTP-ATA-AVSAMKCGLLPVSHNALLVGD------MAYYDFNGEMEQEADRINLQKcLGPTCKI----L 285
Cdd:PRK12348  84 RYPSLGGIVHTHSThATAwAQAGLAIPALGTTHADYFFGDipctrgLSEEEVQGEYELNTGKVIIET-LGNAEPLhtpgI 162

                        170
                 ....*....|....*....
gi 158081763 286 VLRNHGMVALGDTVEEAFY 304
Cdd:PRK12348 163 VVYQHGPFAWGKDAHDAVH 181
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 562-664 1.14e-03

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: 41.80  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  562 DQELEEYK-KE-------VERKKLEQEQEGEKDAATEEPGSPVKSTPASPvqsptragTKSPAVSPSKASEDAKKTEVSE 633
Cdd:TIGR00601  56 DKTVKEYKiKEkdfvvvmVSKPKTGTGKVAPPAATPTSAPTPTPSPPASP--------ASGMSAAPASAVEEKSPSEESA 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 158081763  634 ANTEPEPEKPEG---------VVVNGKEEEPSVEEVLSKG 664
Cdd:TIGR00601 128 TATAPESPSTSVpssgsdaasTLVVGSERETTIEEIMEMG 167
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
 388-692 2.06e-03

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 41.20  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  388 VQEKTKHKSEVEIPATVTAFVFEEDGVPVPALRQHAQKQQKEKTRwLNTPntylrVNVADEVQRNMGSPRPKTTWMKADE 467
Cdd:pfam04747 153 VKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTP-TNTP-----AEPAEQVQEITGKKNKKNKKKSESE 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  468 VEKSSSGMPIRIENPNQFVP---LYTDPQEVLDMRNKiREQNRQDIKSAgpqSQLLASVIAEKSrSPSTESQLASKGDaD 544
Cdd:pfam04747 227 ATAAPASVEQVVEQPKVVTEephQQAAPQEKKNKKNK-RKSESENVPAA---SETPVEPVVETT-PPASENQKKNKKD-K 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081763  545 TKDELEETVPNPfsqlTDQELEEYKKEVERKKLE-----QEQEGEKDAATEEPGSPVKSTPASPVQSPTRAGTKSPAVSP 619
Cdd:pfam04747 301 KKSESEKVVEEP----VQAEAPKSKKPTADDNMDfldfvTAKEEPKDEPAETPAAPVEEVVENVVENVVEKSTTPPATEN 376

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158081763  620 SKASEDAKKTEVSEANTEPEPEKPEGvvvngkeeEPSVEEVLSKGPGQMTTNADTDGDSYKDKTESVTSGPLS 692
Cdd:pfam04747 377 KKKNKKDKKKSESEKVTEQPVESAPA--------PPQVEQVVETTPPASENKKKNKKDKKKSESEKAVEEPVQ 441
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
161-234 3.66e-03

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 39.43  E-value: 3.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158081763 161 VSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVE---KGSScfpvDT-TgfslHSAIYAARPDVRCAIHLHTP-ATA 234
Cdd:PRK08193  32 IDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEgklKPSS----DTpT----HLVLYKAFPEIGGIVHTHSRhATA 102
PHA00666 PHA00666
putative protease
 578-645 3.76e-03

putative protease


Pssm-ID: 222808 [Multi-domain]  Cd Length: 233  Bit Score: 39.64  E-value: 3.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158081763 578 EQEQEGEKDAATEEPGSPVKSTPAsPVQSPTRA-GTKSPAVSPSKASEDAKKTEVSEANTEPEPEKPEG 645
Cdd:PHA00666  15 EQPGDGGSQPAASEPAAGAGDNPA-PQGDPTQEeGDKPQPAAGADKPEGDKKADGDKPEEKKPGEKPEG 82
 
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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