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Conserved domains on  [gi|320015400|gb|ADV98971|]
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putative exported protein [Yersinia pestis biovar Medievalis str. Harbin 35]

Protein Classification

N-acetylneuraminate epimerase( domain architecture ID 11487115)

N-acetylneuraminate epimerase converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14131 PRK14131
N-acetylneuraminate epimerase;
11-392 0e+00

N-acetylneuraminate epimerase;


:

Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 590.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  11 QLTTKIVLFSAlsllmmASLPNTYAEQYPDVPVPFKNGTGGKVENSLYVGLGSAGVSWFRLDTDKTGAGWQKVANFPGQP 90
Cdd:PRK14131   1 TLTTLALLLAA------ASSFAANAEQLPDLPVPFKNGTGAIDNNTVYVGLGSAGTSWYKLDLNAPSKGWTKIAAFPGGP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  91 REQAVTVVLAGKLYVFGGVGKTNaNDTQVRALDDAYRFDPQTNQWQQLATRAPRGLVGTVATTLDGSQAVLLGGVNKAIF 170
Cdd:PRK14131  75 REQAVAAFIDGKLYVFGGIGKTN-SEGSPQVFDDVYKYDPKTNSWQKLDTRSPVGLAGHVAVSLHNGKAYITGGVNKNIF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 171 DGYFTDLASAGSDEVRKSAVINAYFNQAPADYFYNRDVLIYDPQKNQWKSGGLLPFLGTAGSAISRMDNRLILINGEIKP 250
Cdd:PRK14131 154 DGYFEDLAAAGKDKTPKDKINDAYFDKKPEDYFFNKEVLSYDPSTNQWKNAGESPFLGTAGSAVVIKGNKLWLINGEIKP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 251 GLRTAAVWQGLMQGNVLEWQPQPDLIGAETGSAQEGLAGAFSGISHKTVLVAGGANFPGAWKQFNRGHLYAHQGLEKQWH 330
Cdd:PRK14131 234 GLRTDAVKQGKFTGNNLKWQKLPDLPPAPGGSSQEGVAGAFAGYSNGVLLVAGGANFPGARENYQNGKLYAHEGLKKSWS 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320015400 331 QQVYALVDNQWRIAGKLPQPLGYGVSIQGPDKVILIGGETTGGTATSAVTQLSWQGGKLHIE 392
Cdd:PRK14131 314 DEIYALVNGKWQKVGELPQGLAYGVSVSWNNGVLLIGGETAGGKAVSDVTLLSWDGKKLTVE 375
 
Name Accession Description Interval E-value
PRK14131 PRK14131
N-acetylneuraminate epimerase;
11-392 0e+00

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 590.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  11 QLTTKIVLFSAlsllmmASLPNTYAEQYPDVPVPFKNGTGGKVENSLYVGLGSAGVSWFRLDTDKTGAGWQKVANFPGQP 90
Cdd:PRK14131   1 TLTTLALLLAA------ASSFAANAEQLPDLPVPFKNGTGAIDNNTVYVGLGSAGTSWYKLDLNAPSKGWTKIAAFPGGP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  91 REQAVTVVLAGKLYVFGGVGKTNaNDTQVRALDDAYRFDPQTNQWQQLATRAPRGLVGTVATTLDGSQAVLLGGVNKAIF 170
Cdd:PRK14131  75 REQAVAAFIDGKLYVFGGIGKTN-SEGSPQVFDDVYKYDPKTNSWQKLDTRSPVGLAGHVAVSLHNGKAYITGGVNKNIF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 171 DGYFTDLASAGSDEVRKSAVINAYFNQAPADYFYNRDVLIYDPQKNQWKSGGLLPFLGTAGSAISRMDNRLILINGEIKP 250
Cdd:PRK14131 154 DGYFEDLAAAGKDKTPKDKINDAYFDKKPEDYFFNKEVLSYDPSTNQWKNAGESPFLGTAGSAVVIKGNKLWLINGEIKP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 251 GLRTAAVWQGLMQGNVLEWQPQPDLIGAETGSAQEGLAGAFSGISHKTVLVAGGANFPGAWKQFNRGHLYAHQGLEKQWH 330
Cdd:PRK14131 234 GLRTDAVKQGKFTGNNLKWQKLPDLPPAPGGSSQEGVAGAFAGYSNGVLLVAGGANFPGARENYQNGKLYAHEGLKKSWS 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320015400 331 QQVYALVDNQWRIAGKLPQPLGYGVSIQGPDKVILIGGETTGGTATSAVTQLSWQGGKLHIE 392
Cdd:PRK14131 314 DEIYALVNGKWQKVGELPQGLAYGVSVSWNNGVLLIGGETAGGKAVSDVTLLSWDGKKLTVE 375
muta_rot_YjhT TIGR03547
mutatrotase, YjhT family; Members of this protein family contain multiple copies of the ...
 38-385 0e+00

mutatrotase, YjhT family; Members of this protein family contain multiple copies of the beta-propeller-forming Kelch repeat. All are full-length homologs to YjhT of Escherichia coli, which has been identified as a mutarotase for sialic acid. This protein improves bacterial ability to obtain host sialic acid, and thus serves as a virulence factor. Some bacteria carry what appears to be a cyclically permuted homolog of this protein.


Pssm-ID: 274641 [Multi-domain]  Cd Length: 346  Bit Score: 539.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400   38 YPDVPVPFKNGTGGKVENSLYVGLGSAGVSWFRLDTDKTGAGWQKVANFPGQPREQAVTVVLAGKLYVFGGVGKTNaNDT 117
Cdd:TIGR03547   1 LPDLPVGFKNGTGAIIGDKVYVGLGSAGTSWYKLDLKKPSKGWQKIADFPGGPRNQAVAAAIDGKLYVFGGIGKAN-SEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  118 QVRALDDAYRFDPQTNQWQQLATRAPRGLVGTVATTLDGSQAVLLGGVNKAIFDGYFTDLASAGSDEVRKSAVINAYFNQ 197
Cdd:TIGR03547  80 SPQVFDDVYRYDPKKNSWQKLDTRSPVGLLGASGFSLHNGQAYFTGGVNKNIFDGYFADLSAADKDSEPKDKLIAAYFSQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  198 APADYFYNRDVLIYDPQKNQWKSGGLLPFLGTAGSAISRMDNRLILINGEIKPGLRTAAVWQGLMQGNVLEWQPQPDLIG 277
Cdd:TIGR03547 160 PPEDYFWNKNVLSYDPSTNQWRNLGENPFLGTAGSAIVHKGNKLLLINGEIKPGLRTAEVKQYLFTGGKLEWNKLPPLPP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  278 AeTGSAQEGLAGAFSGISHKTVLVAGGANFPGAWKQFNRGHLYAHQGLEKQWHQQVYALVDNQWRIAGKLPQPLGYGVSI 357
Cdd:TIGR03547 240 P-KSSSQEGLAGAFAGISNGVLLVAGGANFPGAQENYKNGKLYAHEGLIKAWSSEVYALDNGKWSKVGKLPQGLAYGVSV 318

                         330       340
                  ....*....|....*....|....*...
gi 320015400  358 QGPDKVILIGGETTGGTATSAVTQLSWQ 385
Cdd:TIGR03547 319 SWNNGVLLIGGENSGGKAVTDVYLLSWD 346
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
36-260 1.32e-35

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 131.82  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  36 EQYPDVPVPFKNGTGGKVENSLYVGLG----SAGVSWFRLDTDKTGagWQKVANFPGQPREQAVTVVLAGKLYVFGGVGK 111
Cdd:COG3055    4 SSLPDLPTPRSEAAAALLDGKVYVAGGlsggSASNSFEVYDPATNT--WSELAPLPGPPRHHAAAVAQDGKLYVFGGFTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 112 TNAndtQVRALDDAYRFDPQTNQWQQLATrAPRGLVGTVATTLDGS---------------------------------- 157
Cdd:COG3055   82 ANP---SSTPLNDVYVYDPATNTWTKLAP-MPTPRGGATALLLDGKiyvvggwddggnvawvevydpatgtwtqlaplpt 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 158 -----QAVLL--------GGVNKAIFDGYFTDLAS-AGSDEVRKSAVINAYFNQAPADYFYNRDVLIYDPQKNQWKSGGL 223
Cdd:COG3055  158 prdhlAAAVLpdgkilviGGRNGSGFSNTWTTLAPlPTARAGHAAAVLGGKILVFGGESGFSDEVEAYDPATNTWTALGE 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 320015400 224 LPFLGTAGSAISrMDNRLILINGEIKPGLRTAAVWQG 260
Cdd:COG3055  238 LPTPRHGHAAVL-TDGKVYVIGGETKPGVRTPLVTSA 273
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 90-140 3.13e-07

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 46.45  E-value: 3.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 320015400   90 PREQAVTVVLAGKLYVFGGVGKTnandtqvRALDDAYRFDPQTNQWQQLAT 140
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGN-------QSLNSVEVYDPETNTWSKLPS 44
 
Name Accession Description Interval E-value
PRK14131 PRK14131
N-acetylneuraminate epimerase;
11-392 0e+00

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 590.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  11 QLTTKIVLFSAlsllmmASLPNTYAEQYPDVPVPFKNGTGGKVENSLYVGLGSAGVSWFRLDTDKTGAGWQKVANFPGQP 90
Cdd:PRK14131   1 TLTTLALLLAA------ASSFAANAEQLPDLPVPFKNGTGAIDNNTVYVGLGSAGTSWYKLDLNAPSKGWTKIAAFPGGP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  91 REQAVTVVLAGKLYVFGGVGKTNaNDTQVRALDDAYRFDPQTNQWQQLATRAPRGLVGTVATTLDGSQAVLLGGVNKAIF 170
Cdd:PRK14131  75 REQAVAAFIDGKLYVFGGIGKTN-SEGSPQVFDDVYKYDPKTNSWQKLDTRSPVGLAGHVAVSLHNGKAYITGGVNKNIF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 171 DGYFTDLASAGSDEVRKSAVINAYFNQAPADYFYNRDVLIYDPQKNQWKSGGLLPFLGTAGSAISRMDNRLILINGEIKP 250
Cdd:PRK14131 154 DGYFEDLAAAGKDKTPKDKINDAYFDKKPEDYFFNKEVLSYDPSTNQWKNAGESPFLGTAGSAVVIKGNKLWLINGEIKP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 251 GLRTAAVWQGLMQGNVLEWQPQPDLIGAETGSAQEGLAGAFSGISHKTVLVAGGANFPGAWKQFNRGHLYAHQGLEKQWH 330
Cdd:PRK14131 234 GLRTDAVKQGKFTGNNLKWQKLPDLPPAPGGSSQEGVAGAFAGYSNGVLLVAGGANFPGARENYQNGKLYAHEGLKKSWS 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320015400 331 QQVYALVDNQWRIAGKLPQPLGYGVSIQGPDKVILIGGETTGGTATSAVTQLSWQGGKLHIE 392
Cdd:PRK14131 314 DEIYALVNGKWQKVGELPQGLAYGVSVSWNNGVLLIGGETAGGKAVSDVTLLSWDGKKLTVE 375
muta_rot_YjhT TIGR03547
mutatrotase, YjhT family; Members of this protein family contain multiple copies of the ...
 38-385 0e+00

mutatrotase, YjhT family; Members of this protein family contain multiple copies of the beta-propeller-forming Kelch repeat. All are full-length homologs to YjhT of Escherichia coli, which has been identified as a mutarotase for sialic acid. This protein improves bacterial ability to obtain host sialic acid, and thus serves as a virulence factor. Some bacteria carry what appears to be a cyclically permuted homolog of this protein.


Pssm-ID: 274641 [Multi-domain]  Cd Length: 346  Bit Score: 539.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400   38 YPDVPVPFKNGTGGKVENSLYVGLGSAGVSWFRLDTDKTGAGWQKVANFPGQPREQAVTVVLAGKLYVFGGVGKTNaNDT 117
Cdd:TIGR03547   1 LPDLPVGFKNGTGAIIGDKVYVGLGSAGTSWYKLDLKKPSKGWQKIADFPGGPRNQAVAAAIDGKLYVFGGIGKAN-SEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  118 QVRALDDAYRFDPQTNQWQQLATRAPRGLVGTVATTLDGSQAVLLGGVNKAIFDGYFTDLASAGSDEVRKSAVINAYFNQ 197
Cdd:TIGR03547  80 SPQVFDDVYRYDPKKNSWQKLDTRSPVGLLGASGFSLHNGQAYFTGGVNKNIFDGYFADLSAADKDSEPKDKLIAAYFSQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  198 APADYFYNRDVLIYDPQKNQWKSGGLLPFLGTAGSAISRMDNRLILINGEIKPGLRTAAVWQGLMQGNVLEWQPQPDLIG 277
Cdd:TIGR03547 160 PPEDYFWNKNVLSYDPSTNQWRNLGENPFLGTAGSAIVHKGNKLLLINGEIKPGLRTAEVKQYLFTGGKLEWNKLPPLPP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  278 AeTGSAQEGLAGAFSGISHKTVLVAGGANFPGAWKQFNRGHLYAHQGLEKQWHQQVYALVDNQWRIAGKLPQPLGYGVSI 357
Cdd:TIGR03547 240 P-KSSSQEGLAGAFAGISNGVLLVAGGANFPGAQENYKNGKLYAHEGLIKAWSSEVYALDNGKWSKVGKLPQGLAYGVSV 318

                         330       340
                  ....*....|....*....|....*...
gi 320015400  358 QGPDKVILIGGETTGGTATSAVTQLSWQ 385
Cdd:TIGR03547 319 SWNNGVLLIGGENSGGKAVTDVYLLSWD 346
mutarot_permut TIGR03548
cyclically-permuted mutarotase family protein; Members of this protein family show essentially ...
 36-254 9.81e-48

cyclically-permuted mutarotase family protein; Members of this protein family show essentially full-length homology, cyclically permuted, to YjhT from Escherichia coli. YjhT was shown to act as a mutarotase for sialic acid, and by this ability to be able to act as a virulence factor. Members of the YjhT family (TIGR03547) and this cyclically-permuted family have multiple repeats of the beta-propeller-forming Kelch repeat.


Pssm-ID: 274642 [Multi-domain]  Cd Length: 331  Bit Score: 165.35  E-value: 9.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400   36 EQYPDVPVPFKNGTGGKVENSLYVGLG----SAGVSWFRLDTDKTGAGWQKVANFPGQPREQAVTVVLAGKLYVFGGVgk 111
Cdd:TIGR03548 106 ETLPSLPVAFDNGSATYKDGKIYVGGGnangKPSNKFYCLDLSNDTSGWEELPEFPGEARVQPVCQALHGKLYVFGGF-- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  112 TNANDTQVRalDDAYRFDPQTNQWQQLATRA-----PRGLVGTVATTLDGSQAVLLGGVNKAIFDGYFTDLaSAGSDEVR 186
Cdd:TIGR03548 184 QLGGDAIIY--TDGYAYSPKTNTWQTVADPVlsdgePITLLGGNSVKLGDSLMLVIGGVNYDIFFDAVDRL-RQMKDESL 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320015400  187 KSAViNAYFNQAPADYFYNRDVLIYDPQKNQWKSGGLLPFLGTAGSAISRMDNRLILINGEIKPGLRT 254
Cdd:TIGR03548 261 KSEK-AEYFGHPPQWYRFNDKVLIYNVRSNEWKSIGAVPFVARAGAALLLHGDNIFSINGEIKPGIRT 327
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
36-260 1.32e-35

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 131.82  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  36 EQYPDVPVPFKNGTGGKVENSLYVGLG----SAGVSWFRLDTDKTGagWQKVANFPGQPREQAVTVVLAGKLYVFGGVGK 111
Cdd:COG3055    4 SSLPDLPTPRSEAAAALLDGKVYVAGGlsggSASNSFEVYDPATNT--WSELAPLPGPPRHHAAAVAQDGKLYVFGGFTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 112 TNAndtQVRALDDAYRFDPQTNQWQQLATrAPRGLVGTVATTLDGS---------------------------------- 157
Cdd:COG3055   82 ANP---SSTPLNDVYVYDPATNTWTKLAP-MPTPRGGATALLLDGKiyvvggwddggnvawvevydpatgtwtqlaplpt 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 158 -----QAVLL--------GGVNKAIFDGYFTDLAS-AGSDEVRKSAVINAYFNQAPADYFYNRDVLIYDPQKNQWKSGGL 223
Cdd:COG3055  158 prdhlAAAVLpdgkilviGGRNGSGFSNTWTTLAPlPTARAGHAAAVLGGKILVFGGESGFSDEVEAYDPATNTWTALGE 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 320015400 224 LPFLGTAGSAISrMDNRLILINGEIKPGLRTAAVWQG 260
Cdd:COG3055  238 LPTPRHGHAAVL-TDGKVYVIGGETKPGVRTPLVTSA 273
mutarot_permut TIGR03548
cyclically-permuted mutarotase family protein; Members of this protein family show essentially ...
 286-366 3.04e-08

cyclically-permuted mutarotase family protein; Members of this protein family show essentially full-length homology, cyclically permuted, to YjhT from Escherichia coli. YjhT was shown to act as a mutarotase for sialic acid, and by this ability to be able to act as a virulence factor. Members of the YjhT family (TIGR03547) and this cyclically-permuted family have multiple repeats of the beta-propeller-forming Kelch repeat.


Pssm-ID: 274642 [Multi-domain]  Cd Length: 331  Bit Score: 54.80  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  286 GLAGAFSGISHKTVLVAGGANFPgawkqfnrgHLYAHQGLEKQWHQQVYALVDN-----QWRIAGKLPQPLGYGVSIQGP 360
Cdd:TIGR03548   3 GVSGLLAGKTGDYLVVAGGCNFP---------EKPVAEGGKKKYYKDIYTLKLDansalKWVKAGQLPYEIAYGASVSTP 73


                  ....*.
gi 320015400  361 DKVILI 366
Cdd:TIGR03548  74 YGIYYV 79
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 90-140 3.13e-07

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 46.45  E-value: 3.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 320015400   90 PREQAVTVVLAGKLYVFGGVGKTnandtqvRALDDAYRFDPQTNQWQQLAT 140
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGN-------QSLNSVEVYDPETNTWSKLPS 44
Kelch_4 pfam13418
Galactose oxidase, central domain;
94-140 1.18e-05

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 42.21  E-value: 1.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 320015400   94 AVTVVLAGKLYVFGGvgkTNANDTqvrALDDAYRFDPQTNQWQQLAT 140
Cdd:pfam13418   6 TSTSIPDDTIYLFGG---EGEDGT---LLSDLWVFDLSTNEWTRLGS 46
Kelch_6 pfam13964
Kelch motif;
90-139 4.57e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 40.40  E-value: 4.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 320015400   90 PREQAVTVVLAGKLYVFGGvgktnaNDTQVRALDDAYRFDPQTNQWQQLA 139
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGG------YTNASPALNKLEVYNPLTKSWEELP 44
PHA03098 PHA03098
kelch-like protein; Provisional
 39-228 2.34e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 43.22  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400  39 PDVPVPFKNGTGGKVENSLYV--GLGSAG----VSWFRLDTDKtgagWQKVANFPgQPREQAVTVVLAGKLYVFGGVGKT 112
Cdd:PHA03098 327 PELIYPRKNPGVTVFNNRIYVigGIYNSIslntVESWKPGESK----WREEPPLI-FPRYNPCVVNVNNLIYVIGGISKN 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320015400 113 NANdtqvraLDDAYRFDPQTNQWQQLAtRAPRGLVGTVATTLDGSQAVlLGGVNKA-------------IFDGYFTDLAS 179
Cdd:PHA03098 402 DEL------LKTVECFSLNTNKWSKGS-PLPISHYGGCAIYHDGKIYV-IGGISYIdnikvynivesynPVTNKWTELSS 473

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 320015400 180 AGSDEVRKS--------AVINAYFNQapadyFYNRDVLIYDPQKNQWK-SGGLLPFLG 228
Cdd:PHA03098 474 LNFPRINASlcifnnkiYVVGGDKYE-----YYINEIEVYDDKTNTWTlFCKFPKVIG 526
Kelch_3 pfam13415
Galactose oxidase, central domain;
101-140 1.07e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 36.50  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 320015400  101 GKLYVFGGvgktnANDTQVRALDDAYRFDPQTNQWQQLAT 140
Cdd:pfam13415   2 DKLYIFGG-----LGFDGQTRLNDLYVYDLDTNTWTQIGD 36
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 90-135 5.58e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 34.62  E-value: 5.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 320015400   90 PREQAVTVVLAGKLYVFGGVGKTNandtqVRALDDAYRFDPQTNQW 135
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDGLG-----DLSSSDVLVYDPETNVW 41
 
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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