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Conserved domains on  [gi|56090564|ref|NP_001007705|]
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galactose mutarotase [Rattus norvegicus]

Protein Classification

aldose epimerase family protein( domain architecture ID 10173257)

aldose epimerase family protein similar to Homo sapiens galactose mutarotase, which catalyzes the interconversion of beta-D-galactose and alpha-D-galactose during galactose metabolism

CATH:  2.70.98.10
EC:  5.1.3.-
Gene Ontology:  GO:0016857|GO:0030246|GO:0005975
PubMed:  12717027
SCOP:  4000040

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 21-339 2.74e-180

galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.


:

Pssm-ID: 185696  Cd Length: 326  Bit Score: 501.65  E-value: 2.74e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  21 KFQLRSDQ-LNVDIISWGCTITALQVKDRQGKASDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKEYHLPI 99
Cdd:cd09019   1 LYTLTNGNgLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 100 NREPNSLHGGFRGFDKVLWTPQVLS-NGVQFSRVSPDGEEGYPGELKVWVTYTLDG-GELVVNYRAQASQTTPVNLTNHS 177
Cdd:cd09019  81 NEGPNHLHGGPKGFDKRVWDVEEVEeNSVTFSLVSPDGEEGFPGNLTVTVTYTLTDdNELTIEYEATTDKPTPVNLTNHS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 178 YFNLAGQGSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELG----KHLQSYHIHGFDHNFCL-KESK 252
Cdd:cd09019 161 YFNLAGEGSGDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIGridlDDEQLKLGGGYDHNFVLdKGGG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 253 EKKFCARVHHAASGRILEVYTTQPGVQFYTGNFLDGTLkGKSGEVYPKHSGFCLETQNWPDAVNQPQFPPILLRPGEEYN 332
Cdd:cd09019 241 KLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTP-GGGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPGETYR 319


                ....*..
gi 56090564 333 HTTWFKF 339
Cdd:cd09019 320 HTTVYRF 326
 
Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 21-339 2.74e-180

galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.


Pssm-ID: 185696  Cd Length: 326  Bit Score: 501.65  E-value: 2.74e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  21 KFQLRSDQ-LNVDIISWGCTITALQVKDRQGKASDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKEYHLPI 99
Cdd:cd09019   1 LYTLTNGNgLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 100 NREPNSLHGGFRGFDKVLWTPQVLS-NGVQFSRVSPDGEEGYPGELKVWVTYTLDG-GELVVNYRAQASQTTPVNLTNHS 177
Cdd:cd09019  81 NEGPNHLHGGPKGFDKRVWDVEEVEeNSVTFSLVSPDGEEGFPGNLTVTVTYTLTDdNELTIEYEATTDKPTPVNLTNHS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 178 YFNLAGQGSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELG----KHLQSYHIHGFDHNFCL-KESK 252
Cdd:cd09019 161 YFNLAGEGSGDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIGridlDDEQLKLGGGYDHNFVLdKGGG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 253 EKKFCARVHHAASGRILEVYTTQPGVQFYTGNFLDGTLkGKSGEVYPKHSGFCLETQNWPDAVNQPQFPPILLRPGEEYN 332
Cdd:cd09019 241 KLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTP-GGGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPGETYR 319


                ....*..
gi 56090564 333 HTTWFKF 339
Cdd:cd09019 320 HTTVYRF 326
PLN00194 PLN00194
aldose 1-epimerase; Provisional
 15-341 1.21e-133

aldose 1-epimerase; Provisional


Pssm-ID: 215098 [Multi-domain]  Cd Length: 337  Bit Score: 384.03  E-value: 1.21e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   15 GGGAVEKFQLRSDQLNVDIISWGCTITALQVKDRQGKASDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKE 94
Cdd:PLN00194   5 AEEKPGIYELKNGNISVKLTNYGATITSLILPDKNGKLADVVLGFDSVEPYKNDSPYFGAIVGRVANRIKGAKFTLNGVT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   95 YHLPINREPNSLHGGFRGFDKVLWTPQVLSNG----VQFSRVSPDGEEGYPGELKVWVTYTLDG-GELVVNYRAQA-SQT 168
Cdd:PLN00194  85 YKLPPNNGPNSLHGGPKGFSKVVWEVAKYKKGekpsITFKYHSFDGEEGFPGDLSVTVTYTLLSsNTLRLDMEAKPlNKA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  169 TPVNLTNHSYFNLAGQGSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKhlqsyHIH----GFDH 244
Cdd:PLN00194 165 TPVNLAQHTYWNLAGHNSGDILSHKIQIFGSHITPVDENLIPTGEILPVKGTPFDFTTPKKIGS-----RINelpkGYDH 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  245 NFCLKESKEKKF--CARVHHAASGRILEVYTTQPGVQFYTGNFLDGtLKGKSGEVYPKHSGFCLETQNWPDAVNQPQFPP 322
Cdd:PLN00194 240 NYVLDGEEKEGLkkAAKVKDPKSGRVLELWTNAPGMQFYTSNYVNG-VKGKGGAVYGKHAGLCLETQGFPDAVNQPNFPS 318

                        330
                 ....*....|....*....
gi 56090564  323 ILLRPGEEYNHTTWFKFSV 341
Cdd:PLN00194 319 VVVNPGEKYKHTMLFEFSA 337
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
20-341 6.82e-123

Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 355.74  E-value: 6.82e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  20 EKFQLRSDQLNVDIISWGCTITALQVKDRQGKasDVVLGFAELEGYlQKQPYFGAVVGRVANRIAKGRFTVDGKEYHLPI 99
Cdd:COG2017   8 ELYTLENGGLRAVIPEYGATLTSLRVPDKDGR--DVLLGFDDLEDD-PPWAYGGAILGPYANRIADGRFTLDGKTYQLPI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 100 NREPNSLHGGFRgfdKVLWTPQVLS-NGVQFSRVSPDgEEGYPGELKVWVTYTLDGGELVVNYRAQ--ASQTTPVNLTNH 176
Cdd:COG2017  85 NEGPNALHGGAR---DRPWEVEEQSeDSVTLSLTSPD-EEGYPGNLELTVTYTLTDNGLTITYTATnlGDKPTPFNLGNH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 177 SYFNLAGQGSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKhlqsyhiHGFDHNFCLKESKEkKF 256
Cdd:COG2017 161 PYFNLPGEGGGDIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFREPRPLGD-------GGFDHAFVGLDSDG-RP 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 257 CARVHHAASGRILEVYTTQ-PGVQFYTGNFLDgtlkgksgevyPKHSGFCLETQNWP-DAVNQPQFPP-ILLRPGEEYNH 333
Cdd:COG2017 233 AARLTDPDSGRRLEVSTDEfPGLQVYTGNFLD-----------PGRDGVCLEPQTGPpDAPNHPGFEGlIVLAPGETYSA 301


                ....*...
gi 56090564 334 TTWFKFSV 341
Cdd:COG2017 302 TTRIRFSV 309
galM_Leloir TIGR02636
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ...
 16-340 1.18e-116

galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose 1-epimerase) and participate in the Leloir pathway for galactose/glucose interconversion. All members of the seed alignment for this model are found in gene clusters with other enzymes of the Leloir pathway. This enzyme family belongs to the aldose 1-epimerase family, described by pfam01263. However, the enzyme described as aldose 1-epimerase itself (EC 5.1.3.3) is called broadly specific for D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. The restricted genome context for genes in this family suggests members should act primarily on D-galactose.


Pssm-ID: 274240  Cd Length: 336  Bit Score: 340.88  E-value: 1.18e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564    16 GGAVEKFQLRSDQ-LNVDIISWGCTITALQVkDRQGKASDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKE 94
Cdd:TIGR02636   1 GQPAQLITLTNKNgMTISFMDIGATWLSCQV-PLAGELREVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564    95 YHLPINREPNSLHGGFRGFDKVLWTPQVLSNG---VQFSRVSPDGEEGYPGELKVWVTYTLDG-GELVVNYRAQASQTTP 170
Cdd:TIGR02636  80 YQLSINQGPNCLHGGPEGFDKRRWTIETLEQAevqVKFSLESPDGDQGFPGNLTVSVTYTLTDdNELKIDYEATTDKATP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   171 VNLTNHSYFNLAGQ-GSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKHL----QSYHIHGFDHN 245
Cdd:TIGR02636 160 FNLTNHVYFNLDGAdAGSDVLNHELQLNADRYLPLDEEGIPLGQLKPVDGTSFDFRKEKAIGQDFlandQQQLAKGYDHA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   246 FCL-KESKEKKFCARVHHAASGRILEVYTTQPGVQFYTGNFLDGTlKGKSGEVYPKHSGFCLETQNWPDAVNQPQFPPI- 323
Cdd:TIGR02636 240 FLLnGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGNFLAGT-PNRGGKKYVDHAGIALETQFLPDSPNHPEWGDIs 318

                         330
                  ....*....|....*...
gi 56090564   324 -LLRPGEEYNHTTWFKFS 340
Cdd:TIGR02636 319 cILSPGQEYQHQTRYQFI 336
Aldose_epim pfam01263
Aldose 1-epimerase;
31-338 1.31e-106

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 313.95  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564    31 VDIISWGCTITALQVKDRQGkasDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKEYHLPIN-REPNSLHGG 109
Cdd:pfam01263  13 ATISLYGATLLSLKVPGKLR---EVLLGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLPQNgPGKNPLHGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   110 FRGfdkVLWT--PQVLSNGVQFSRVS-PDGEEGYPGELKVWVTYTLDG-GELVVNYRAQA-SQTTPVNLTNHSYFNLAGq 184
Cdd:pfam01263  90 ARG---RIWEveEVKPDDGVTVTLVLdPDGEEGYPGDLEARVTYTLNEdNELTIEYEATNdGKPTPFNLGNHPYFNLSG- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   185 gspDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKhlqsyHIHGFDHNFCLkesKEKKFCARVHHAA 264
Cdd:pfam01263 166 ---DIDIHELQIEADEYLEVDDDLIPTGELKDVKGTPFDFRQPTPIGE-----DILGYDHVYLL---DPLKAVIIDPDPG 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56090564   265 SGRILEVYTTQPGVQFYTGNFLDGtlkgksgeVYPKHSGFCLETQNWPDAVNQPQFPPILLRPGEEYNHTTWFK 338
Cdd:pfam01263 235 SGIVLEVSTTQPGLVVYTPNFLKG--------KYLSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAETSYS 300
 
Name Accession Description Interval E-value
galactose_mutarotase_like cd09019
galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose ...
 21-339 2.74e-180

galactose mutarotase_like; Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.


Pssm-ID: 185696  Cd Length: 326  Bit Score: 501.65  E-value: 2.74e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  21 KFQLRSDQ-LNVDIISWGCTITALQVKDRQGKASDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKEYHLPI 99
Cdd:cd09019   1 LYTLTNGNgLRVSILNYGATIQSLKVPDKNGKLRDVVLGFDDLEDYLKNSPYFGATVGRVANRIANGRFTLDGKTYQLEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 100 NREPNSLHGGFRGFDKVLWTPQVLS-NGVQFSRVSPDGEEGYPGELKVWVTYTLDG-GELVVNYRAQASQTTPVNLTNHS 177
Cdd:cd09019  81 NEGPNHLHGGPKGFDKRVWDVEEVEeNSVTFSLVSPDGEEGFPGNLTVTVTYTLTDdNELTIEYEATTDKPTPVNLTNHS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 178 YFNLAGQGSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELG----KHLQSYHIHGFDHNFCL-KESK 252
Cdd:cd09019 161 YFNLAGEGSGDILDHELQINADRYLPVDEELIPTGEILPVAGTPFDFRKPKPIGridlDDEQLKLGGGYDHNFVLdKGGG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 253 EKKFCARVHHAASGRILEVYTTQPGVQFYTGNFLDGTLkGKSGEVYPKHSGFCLETQNWPDAVNQPQFPPILLRPGEEYN 332
Cdd:cd09019 241 KLRPAARLTSPESGRKLEVYTTQPGVQFYTGNFLDGTP-GGGGKVYGKRSGFCLETQHFPDAPNHPNFPSIILRPGETYR 319


                ....*..
gi 56090564 333 HTTWFKF 339
Cdd:cd09019 320 HTTVYRF 326
PLN00194 PLN00194
aldose 1-epimerase; Provisional
 15-341 1.21e-133

aldose 1-epimerase; Provisional


Pssm-ID: 215098 [Multi-domain]  Cd Length: 337  Bit Score: 384.03  E-value: 1.21e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   15 GGGAVEKFQLRSDQLNVDIISWGCTITALQVKDRQGKASDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKE 94
Cdd:PLN00194   5 AEEKPGIYELKNGNISVKLTNYGATITSLILPDKNGKLADVVLGFDSVEPYKNDSPYFGAIVGRVANRIKGAKFTLNGVT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   95 YHLPINREPNSLHGGFRGFDKVLWTPQVLSNG----VQFSRVSPDGEEGYPGELKVWVTYTLDG-GELVVNYRAQA-SQT 168
Cdd:PLN00194  85 YKLPPNNGPNSLHGGPKGFSKVVWEVAKYKKGekpsITFKYHSFDGEEGFPGDLSVTVTYTLLSsNTLRLDMEAKPlNKA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  169 TPVNLTNHSYFNLAGQGSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKhlqsyHIH----GFDH 244
Cdd:PLN00194 165 TPVNLAQHTYWNLAGHNSGDILSHKIQIFGSHITPVDENLIPTGEILPVKGTPFDFTTPKKIGS-----RINelpkGYDH 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  245 NFCLKESKEKKF--CARVHHAASGRILEVYTTQPGVQFYTGNFLDGtLKGKSGEVYPKHSGFCLETQNWPDAVNQPQFPP 322
Cdd:PLN00194 240 NYVLDGEEKEGLkkAAKVKDPKSGRVLELWTNAPGMQFYTSNYVNG-VKGKGGAVYGKHAGLCLETQGFPDAVNQPNFPS 318

                        330
                 ....*....|....*....
gi 56090564  323 ILLRPGEEYNHTTWFKFSV 341
Cdd:PLN00194 319 VVVNPGEKYKHTMLFEFSA 337
GalM COG2017
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
20-341 6.82e-123

Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];


Pssm-ID: 441620 [Multi-domain]  Cd Length: 309  Bit Score: 355.74  E-value: 6.82e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  20 EKFQLRSDQLNVDIISWGCTITALQVKDRQGKasDVVLGFAELEGYlQKQPYFGAVVGRVANRIAKGRFTVDGKEYHLPI 99
Cdd:COG2017   8 ELYTLENGGLRAVIPEYGATLTSLRVPDKDGR--DVLLGFDDLEDD-PPWAYGGAILGPYANRIADGRFTLDGKTYQLPI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 100 NREPNSLHGGFRgfdKVLWTPQVLS-NGVQFSRVSPDgEEGYPGELKVWVTYTLDGGELVVNYRAQ--ASQTTPVNLTNH 176
Cdd:COG2017  85 NEGPNALHGGAR---DRPWEVEEQSeDSVTLSLTSPD-EEGYPGNLELTVTYTLTDNGLTITYTATnlGDKPTPFNLGNH 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 177 SYFNLAGQGSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKhlqsyhiHGFDHNFCLKESKEkKF 256
Cdd:COG2017 161 PYFNLPGEGGGDIDDHRLQIPADEYLPVDEGLIPTGELAPVAGTPFDFREPRPLGD-------GGFDHAFVGLDSDG-RP 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 257 CARVHHAASGRILEVYTTQ-PGVQFYTGNFLDgtlkgksgevyPKHSGFCLETQNWP-DAVNQPQFPP-ILLRPGEEYNH 333
Cdd:COG2017 233 AARLTDPDSGRRLEVSTDEfPGLQVYTGNFLD-----------PGRDGVCLEPQTGPpDAPNHPGFEGlIVLAPGETYSA 301


                ....*...
gi 56090564 334 TTWFKFSV 341
Cdd:COG2017 302 TTRIRFSV 309
galM_Leloir TIGR02636
galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose ...
 16-340 1.18e-116

galactose mutarotase; Members of this protein family act as galactose mutarotase (D-galactose 1-epimerase) and participate in the Leloir pathway for galactose/glucose interconversion. All members of the seed alignment for this model are found in gene clusters with other enzymes of the Leloir pathway. This enzyme family belongs to the aldose 1-epimerase family, described by pfam01263. However, the enzyme described as aldose 1-epimerase itself (EC 5.1.3.3) is called broadly specific for D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. The restricted genome context for genes in this family suggests members should act primarily on D-galactose.


Pssm-ID: 274240  Cd Length: 336  Bit Score: 340.88  E-value: 1.18e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564    16 GGAVEKFQLRSDQ-LNVDIISWGCTITALQVkDRQGKASDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKE 94
Cdd:TIGR02636   1 GQPAQLITLTNKNgMTISFMDIGATWLSCQV-PLAGELREVLLGFASAEEYLKQDAYLGATVGRYANRIANGSFEIDGKT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564    95 YHLPINREPNSLHGGFRGFDKVLWTPQVLSNG---VQFSRVSPDGEEGYPGELKVWVTYTLDG-GELVVNYRAQASQTTP 170
Cdd:TIGR02636  80 YQLSINQGPNCLHGGPEGFDKRRWTIETLEQAevqVKFSLESPDGDQGFPGNLTVSVTYTLTDdNELKIDYEATTDKATP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   171 VNLTNHSYFNLAGQ-GSPDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKHL----QSYHIHGFDHN 245
Cdd:TIGR02636 160 FNLTNHVYFNLDGAdAGSDVLNHELQLNADRYLPLDEEGIPLGQLKPVDGTSFDFRKEKAIGQDFlandQQQLAKGYDHA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   246 FCL-KESKEKKFCARVHHAASGRILEVYTTQPGVQFYTGNFLDGTlKGKSGEVYPKHSGFCLETQNWPDAVNQPQFPPI- 323
Cdd:TIGR02636 240 FLLnGERLDGKEAARLTSPDEDLSLEVFTNQPALQIYTGNFLAGT-PNRGGKKYVDHAGIALETQFLPDSPNHPEWGDIs 318

                         330
                  ....*....|....*...
gi 56090564   324 -LLRPGEEYNHTTWFKFS 340
Cdd:TIGR02636 319 cILSPGQEYQHQTRYQFI 336
Aldose_epim pfam01263
Aldose 1-epimerase;
31-338 1.31e-106

Aldose 1-epimerase;


Pssm-ID: 396013  Cd Length: 300  Bit Score: 313.95  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564    31 VDIISWGCTITALQVKDRQGkasDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKEYHLPIN-REPNSLHGG 109
Cdd:pfam01263  13 ATISLYGATLLSLKVPGKLR---EVLLGSDDAEGYLKDSNYFGATLGPYANRIANGRFELDGIPYCLPQNgPGKNPLHGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   110 FRGfdkVLWT--PQVLSNGVQFSRVS-PDGEEGYPGELKVWVTYTLDG-GELVVNYRAQA-SQTTPVNLTNHSYFNLAGq 184
Cdd:pfam01263  90 ARG---RIWEveEVKPDDGVTVTLVLdPDGEEGYPGDLEARVTYTLNEdNELTIEYEATNdGKPTPFNLGNHPYFNLSG- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   185 gspDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKhlqsyHIHGFDHNFCLkesKEKKFCARVHHAA 264
Cdd:pfam01263 166 ---DIDIHELQIEADEYLEVDDDLIPTGELKDVKGTPFDFRQPTPIGE-----DILGYDHVYLL---DPLKAVIIDPDPG 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56090564   265 SGRILEVYTTQPGVQFYTGNFLDGtlkgksgeVYPKHSGFCLETQNWPDAVNQPQFPPILLRPGEEYNHTTWFK 338
Cdd:pfam01263 235 SGIVLEVSTTQPGLVVYTPNFLKG--------KYLSDEGFALETQFLPDEPNHPEFPSIILKPGESYTAETSYS 300
galM PRK11055
galactose-1-epimerase; Provisional
 31-341 1.08e-105

galactose-1-epimerase; Provisional


Pssm-ID: 182931  Cd Length: 342  Bit Score: 313.01  E-value: 1.08e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   31 VDIISWGCTITALQVKDRQGKASDVVLGFAELEGYLQKQPYFGAVVGRVANRIAKGRFTVDGKEYHLPINREPNSLHGGF 110
Cdd:PRK11055  22 VTLMDWGATWLSCRVPLSDGSVREVLLGCASPEDYPDQAAYLGASVGRYANRIANSRFTLDGETYQLSPNQGGNQLHGGP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  111 RGFDKVLWT-PQVLSNGVQFSRVSPDGEEGYPGELKVWVTYTL-DGGELVVNYRAQASQTTPVNLTNHSYFNLAGQGSP- 187
Cdd:PRK11055 102 EGFDKRRWQiVNQNDRQVTFSLSSPDGDQGFPGNLGATVTYRLtDDNRVSITYRATVDKPCPVNLTNHAYFNLDGAEEGs 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  188 DIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELGKHL----QSYHIHGFDHNFCLKESKE-KKFCARVhH 262
Cdd:PRK11055 182 DVRNHKLQINADEYLPVDEGGIPNGGLKSVAGTSFDFRQPKTIAQDFladdDQQKVKGYDHAFLLQAKGDgKKPAAHL-W 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  263 AASGRI-LEVYTTQPGVQFYTGNFLDGTlKGKSGEVYPKHSGFCLETQNWPDAVNQPQF--PPILLRPGEEYNHTTWFKF 339
Cdd:PRK11055 261 SPDEKLqMKVYTTAPALQFYSGNFLAGT-PSRGGGPYADYAGLALESQFLPDSPNHPEWpqPDCILKPGEEYRSLTEYQF 339


                 ..
gi 56090564  340 SV 341
Cdd:PRK11055 340 IA 341
Aldose_epim cd01081
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ...
 29-337 7.25e-56

aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism; they catalyze the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen.


Pssm-ID: 185695 [Multi-domain]  Cd Length: 284  Bit Score: 183.43  E-value: 7.25e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  29 LNVDIISWGCTITALQVKDRQgkasDVVLGFAELEGYLQKQP-YFGAVVGRVANRIAKGRFTVDGKEYHLPINREPNSLH 107
Cdd:cd01081   1 AVAVIAPRGANIISLKVKGDV----DLLWGYPDAEEYPLAPTgGGGAILFPFANRISDGRYTFDGKQYPLNEDEGGNAIH 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 108 GGFRgfdKVLWTP---QVLSNGVQFSRVSPDGEEGYPGELKVWVTYTLDGGELVVNYRAQ--ASQTTPVNLTNHSYFNLA 182
Cdd:cd01081  77 GFVR---NLPWRVvatDEEEASVTLSYDLNDGPGGYPFPLELTVTYTLDADTLTITFTVTnlGDEPMPFGLGWHPYFGLP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 183 GQgspDIYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVELgkhlqsyhiHGFDHNFCLKESKEKKFCARVHH 262
Cdd:cd01081 154 GV---AIEDLRLRVPASKVLPLDDLLPPTGELEVPGEEDFRLGRPLGG---------GELDDCFLLLGNDAGTAEARLED 221

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56090564 263 AASGRILEVYTTQPGVQFYTGnfldgtlkgksgeVYPKHSGFCLETQNW-PDAVNQPQFPPILLRPgEEYNHTTWF 337
Cdd:cd01081 222 PDSRISVEFETGWPFWQVYTG-------------DGGRRGSVAIEPMTSaPDAFFNNNGGLITLKP-PGETRTFSI 283
PTZ00485 PTZ00485
aldolase 1-epimerase; Provisional
 17-341 4.93e-44

aldolase 1-epimerase; Provisional


Pssm-ID: 240435  Cd Length: 376  Bit Score: 155.16  E-value: 4.93e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   17 GAVEKFQLRSDQLNVDIISWGCTITALQVKDRQ-GKASDVVLGFAELEGYLQKQP-YFGAVVGRVANRIAKGRFTVDGKE 94
Cdd:PTZ00485  11 GYDKLVWLETDRLKVGLTNYAASVASIQVYHPAdNKWIEVNCGYPKNPEEAYADPdYMGATVGRCAGRVAGGVFTLDGVK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   95 YHLPINREPNSLHGGFRGFDKVLWTPQVLSN----GVQFSRVSPDGEEGYPGELKVWVTYTLDGGE---LVVNYRAQASQ 167
Cdd:PTZ00485  91 YYTQKNRGENTCHCGDDAYHKKHWGMKLIETanviGVRFNYTSPHMENGFPGELVSKVTYSIERSKpnvLKTIYDSYIPE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  168 T-----TPVNLTNHSYFNLAG----QGSPD--------IYDHEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPVEL 230
Cdd:PTZ00485 171 TspadaTPVNIFNHAYWNLNGiperNGKKNavwvqpesVRNHWLRVPASRVAEADRMAIPTGEFLSVEGTGLDFRQGRVI 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  231 GKHLQSYHIH-----GFDHNFCLKESKEKKFC--ARVHHAASGRILEVYTTQPGVQFYTGNFLDGTLKGKSGEVYPKHSG 303
Cdd:PTZ00485 251 GDCIDDVALLdrdpcGYDHPLAIDGWEKGKLMlhAEAKSPVTNICMKVYSTFPCMWVYTANNKPLPASGGPGQRYARWTG 330

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 56090564  304 FCLETQNWPDAVNQ-PQFPPILLRPGE-EYNHTTWFKFSV 341
Cdd:PTZ00485 331 MGLEPQYFPDVANHyPKYPSCIVRRGErRFTETILNEFTV 370
Aldose_epim_Ec_YihR cd09022
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ...
 33-231 5.62e-29

Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli YihR are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.


Pssm-ID: 185699  Cd Length: 284  Bit Score: 113.05  E-value: 5.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  33 IISWGCTITALQVKDRqgkasDVVLGFAELEgylqKQPYF-GAVVGRVANRIAKGRFTVDGKEYHLPINrEP---NSLHG 108
Cdd:cd09022   5 VTEVGAGLRSLTVGGR-----DLVEPYPADE----VPPGAaGQVLAPWPNRIADGRYTFDGVEHQLPIT-EPergNAIHG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 109 --GFRGFDKVLWTPqvlsNGVQFS-RVSPdgEEGYPGELKVWVTYTLDGGELVVNYRAQ--ASQTTPVNLTNHSYFnLAG 183
Cdd:cd09022  75 lvRWADWQLVEHTD----SSVTLRtRIPP--QPGYPFTLELTVTYELDDDGLTVTLTATnvGDEPAPFGVGFHPYL-SAG 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 56090564 184 QGSPDiyDHEVTIAADAYLPVDETLIPTGViAPVEGTAFDLRKPVELG 231
Cdd:cd09022 148 GAPLD--ECTLTLPADTWLPVDERLLPTGT-EPVAGTPYDFRTGRRLG 192
Aldose_epim_Ec_YphB cd09021
aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli ...
 80-330 1.66e-12

aldose 1-epimerase, similar to Escherichia coli YphB; Proteins similar to Escherichia coli YphB are uncharacterized members of the aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.


Pssm-ID: 185698  Cd Length: 273  Bit Score: 66.55  E-value: 1.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  80 ANRIAKGRFTVDGKEYHLPINR--EPNSLHG-GFRGfdkvLWtpQVLSNG---VQFSRVSPDGEEGYPGElkVWVTYTLD 153
Cdd:cd09021  47 SNRIRGGRFLFAGREVALPPNTadEPHPLHGdGWRR----PW--QVVAASadsAELQLDHEADDPPWAYR--AEQRFHLA 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 154 GGEL-----VVNYraqASQTTPVNLTNHSYFNLagqgSPDIydhEVTIAADAYLPVDETLIPTGVIAPVEGTAFDLRKPV 228
Cdd:cd09021 119 GDGLsitlsVTNR---GDRPMPAGLGFHPYFPR----TPDT---RLQADADGVWLEDEDHLPTGLRPHPPDWDFSQPRPL 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564 229 elgkhlqsyHIHGFDHNFCLKESkekkfCARVHHAASGRILEVyTTQPGVQFYTgnfldgtlkgksgeVY--PKHSGFCL 306
Cdd:cd09021 189 ---------PDRWIDNCFTGWDG-----AALIWPPERGLALTI-EADAPFSHLV--------------VYrpPGEDFFCL 239

                       250       260
                ....*....|....*....|....*.
gi 56090564 307 ETQ-NWPDAVNQPQFP-PILLRPGEE 330
Cdd:cd09021 240 EPVsHAPDAHHGPGDPgLRVLAPGES 265
PRK15172 PRK15172
aldose-1-epimerase;
81-286 1.08e-09

aldose-1-epimerase;


Pssm-ID: 237918  Cd Length: 300  Bit Score: 58.67  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564   81 NRIAKGRFTVDGKEYHLPINrEPNS---LHGGFRGFDkvlWTPQVLS-NGVQFSRVSPDgEEGYPGELKVWVTYTLDGGE 156
Cdd:PRK15172  64 NRIANGCYRYQGQEYQLPIN-EHVSkaaIHGLLAWRD---WQISELTaTSVTLTAFLPP-SYGYPFMLASQVIYSLDAAT 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  157 -LVVNYRAQ--ASQTTPVNLTNHSYF--NLAgqgspDIYDHEVTIAADAYLPVDETLIPTgVIAPVEGTAFDLRKPVELG 231
Cdd:PRK15172 139 gLSVEIASQniGDVPAPYGVGIHPYLtcNLT-----SVDEYLLQLPANQVLAVDEHANPT-TLHHVDELDLDFSQAKKIA 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 56090564  232 khlqSYHIhgfDHNFclkESKEKKFCARVHHAASGRILEVYTTQPGVQFYTGNFL 286
Cdd:PRK15172 213 ----ATKI---DHTF---KTANDLWEVRITHPQQALSVSLCSDQPWLQIYSGEKL 257
Aldose_epim_lacX cd09024
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ...
 75-162 3.47e-05

Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis lacX are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.


Pssm-ID: 185701  Cd Length: 288  Bit Score: 44.84  E-value: 3.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090564  75 VVGRVANriakGRFTVDGKEYHLPInrepnslHGgF---RGFDKVLWTPqvlsNGVQFSRVS-PDGEEGYPGELKVWVTY 150
Cdd:cd09024  50 IVGRLKD----DTYTIDGKTYPMPQ-------HG-FardMEFEVVEQSD----DSVTFELTDnEETLKVYPFDFELRVTY 113

                        90
                ....*....|..
gi 56090564 151 TLDGGELVVNYR 162
Cdd:cd09024 114 TLEGNTLKVTYE 125
 
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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