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Conserved domains on  [gi|485674666|ref|WP_001315214|]
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MULTISPECIES: N-acetylneuraminate epimerase [Enterobacteriaceae]

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;
4-368 0e+00

N-acetylneuraminate epimerase;


:

Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 568.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666   4 TITALTIIMA---SFAANASVLPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKRWTALAAFPGGPRDQATS 80
Cdd:PRK14131   1 TLTTLALLLAaasSFAANAEQLPDLPVPFKNGTGAIDNNTVYVGLGSAGTSWYKLDLNAPSKGWTKIAAFPGGPREQAVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  81 AFIDGNLYVFGGIGK-NSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFV-HNGKAYVTGGVNQNIFNGYFEDL 158
Cdd:PRK14131  81 AFIDGKLYVFGGIGKtNSEGSPQVFDDVYKYDPKTNSWQKLDTRSPVGLAGHVAVSlHNGKAYITGGVNKNIFDGYFEDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 159 NEAGKDSTAIDKINAYYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAV 238
Cdd:PRK14131 161 AAAGKDKTPKDKINDAYFDKKPEDYFFNKEVLSYDPSTNQWKNAGESPFLGTAGSAVVIKGNKLWLINGEIKPGLRTDAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 239 FELDFTGDNLKWNKLDPV------SSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSADIHLWY 312
Cdd:PRK14131 241 KQGKFTGNNLKWQKLPDLppapggSSQEGVAGAFAGYSNGVLLVAGGANFPGARENYQNGKLYAHEGLKKSWSDEIYALV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 485674666 313 NGKWDKSGELSQGRAYGVSLPWNNSLLIIGGETAGGKAVMDSVLISVKDNKVTVQN 368
Cdd:PRK14131 321 NGKWQKVGELPQGLAYGVSVSWNNGVLLIGGETAGGKAVSDVTLLSWDGKKLTVEN 376
 
Name Accession Description Interval E-value
PRK14131 PRK14131
N-acetylneuraminate epimerase;
4-368 0e+00

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 568.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666   4 TITALTIIMA---SFAANASVLPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKRWTALAAFPGGPRDQATS 80
Cdd:PRK14131   1 TLTTLALLLAaasSFAANAEQLPDLPVPFKNGTGAIDNNTVYVGLGSAGTSWYKLDLNAPSKGWTKIAAFPGGPREQAVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  81 AFIDGNLYVFGGIGK-NSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFV-HNGKAYVTGGVNQNIFNGYFEDL 158
Cdd:PRK14131  81 AFIDGKLYVFGGIGKtNSEGSPQVFDDVYKYDPKTNSWQKLDTRSPVGLAGHVAVSlHNGKAYITGGVNKNIFDGYFEDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 159 NEAGKDSTAIDKINAYYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAV 238
Cdd:PRK14131 161 AAAGKDKTPKDKINDAYFDKKPEDYFFNKEVLSYDPSTNQWKNAGESPFLGTAGSAVVIKGNKLWLINGEIKPGLRTDAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 239 FELDFTGDNLKWNKLDPV------SSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSADIHLWY 312
Cdd:PRK14131 241 KQGKFTGNNLKWQKLPDLppapggSSQEGVAGAFAGYSNGVLLVAGGANFPGARENYQNGKLYAHEGLKKSWSDEIYALV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 485674666 313 NGKWDKSGELSQGRAYGVSLPWNNSLLIIGGETAGGKAVMDSVLISVKDNKVTVQN 368
Cdd:PRK14131 321 NGKWQKVGELPQGLAYGVSVSWNNGVLLIGGETAGGKAVSDVTLLSWDGKKLTVEN 376
muta_rot_YjhT TIGR03547
mutatrotase, YjhT family; Members of this protein family contain multiple copies of the ...
22-360 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: 516.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666   22 LPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKRWTALAAFPGGPRDQATSAFIDGNLYVFGGIGK-NSEGL 100
Cdd:TIGR03547   1 LPDLPVGFKNGTGAIIGDKVYVGLGSAGTSWYKLDLKKPSKGWQKIADFPGGPRNQAVAAAIDGKLYVFGGIGKaNSEGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  101 TQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTF-VHNGKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINAYYFDKK 179
Cdd:TIGR03547  81 PQVFDDVYRYDPKKNSWQKLDTRSPVGLLGASGFsLHNGQAYFTGGVNKNIFDGYFADLSAADKDSEPKDKLIAAYFSQP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  180 AEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVFELDFTGDNLKWNKLDPV--- 256
Cdd:TIGR03547 161 PEDYFWNKNVLSYDPSTNQWRNLGENPFLGTAGSAIVHKGNKLLLINGEIKPGLRTAEVKQYLFTGGKLEWNKLPPLppp 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  257 --SSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSADIHLWYNGKWDKSGELSQGRAYGVSLPW 334
Cdd:TIGR03547 241 ksSSQEGLAGAFAGISNGVLLVAGGANFPGAQENYKNGKLYAHEGLIKAWSSEVYALDNGKWSKVGKLPQGLAYGVSVSW 320
                         330       340
                  ....*....|....*....|....*.
gi 485674666  335 NNSLLIIGGETAGGKAVMDSVLISVK 360
Cdd:TIGR03547 321 NNGVLLIGGENSGGKAVTDVYLLSWD 346
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
17-351 1.13e-44

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 154.93  E-value: 1.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  17 ANASVLPETPVPFKSGTGAIDNDTVYIGLG----SAGTAWYKLDTqaKDKRWTALAAFPGGPRDQATSAFIDGNLYVFGG 92
Cdd:COG3055    1 ATWSSLPDLPTPRSEAAAALLDGKVYVAGGlsggSASNSFEVYDP--ATNTWSELAPLPGPPRHHAAAVAQDGKLYVFGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  93 IGKNSEGlTQVFNDVHKYNPKTNSWVKLMShAPMGMAGHVTFVHNGKAYVTGGVNQNIFNGYFEDlneagkdstaidkin 172
Cdd:COG3055   79 FTGANPS-STPLNDVYVYDPATNTWTKLAP-MPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEV--------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 173 ayyfdkkaedyffnkfllsFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEakpglrtdavfelDFTGDNLKWNK 252
Cdd:COG3055  142 -------------------YDPATGTWTQLAPLPTPRDHLAAAVLPDGKILVIGGR-------------NGSGFSNTWTT 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 253 LDPvsSPDGVAGGFAGISNDSLIFAGGagfkgsrENYQNGKNYAheglkksYSADihlwyNGKWDKSGELSQGRAYGVSL 332
Cdd:COG3055  190 LAP--LPTARAGHAAAVLGGKILVFGG-------ESGFSDEVEA-------YDPA-----TNTWTALGELPTPRHGHAAV 248
                        330
                 ....*....|....*....
gi 485674666 333 PWNNSLLIIGGETAGGKAV 351
Cdd:COG3055  249 LTDGKVYVIGGETKPGVRT 267
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
74-122 1.24e-06

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: 44.91  E-value: 1.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 485674666   74 PRDQATSAFIDGNLYVFGGIGKNsegltQVFNDVHKYNPKTNSWVKLMS 122
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGN-----QSLNSVEVYDPETNTWSKLPS 44
Kelch smart00612
Kelch domain;
87-133 4.86e-03

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 34.84  E-value: 4.86e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 485674666    87 LYVFGGIgkNSeglTQVFNDVHKYNPKTNSWVKL--MSHAPMGMAGHVT 133
Cdd:smart00612   2 IYVVGGF--DG---GQRLKSVEVYDPETNKWTPLpsMPTPRSGHGVAVI 45
 
Name Accession Description Interval E-value
PRK14131 PRK14131
N-acetylneuraminate epimerase;
4-368 0e+00

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 568.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666   4 TITALTIIMA---SFAANASVLPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKRWTALAAFPGGPRDQATS 80
Cdd:PRK14131   1 TLTTLALLLAaasSFAANAEQLPDLPVPFKNGTGAIDNNTVYVGLGSAGTSWYKLDLNAPSKGWTKIAAFPGGPREQAVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  81 AFIDGNLYVFGGIGK-NSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFV-HNGKAYVTGGVNQNIFNGYFEDL 158
Cdd:PRK14131  81 AFIDGKLYVFGGIGKtNSEGSPQVFDDVYKYDPKTNSWQKLDTRSPVGLAGHVAVSlHNGKAYITGGVNKNIFDGYFEDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 159 NEAGKDSTAIDKINAYYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAV 238
Cdd:PRK14131 161 AAAGKDKTPKDKINDAYFDKKPEDYFFNKEVLSYDPSTNQWKNAGESPFLGTAGSAVVIKGNKLWLINGEIKPGLRTDAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 239 FELDFTGDNLKWNKLDPV------SSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSADIHLWY 312
Cdd:PRK14131 241 KQGKFTGNNLKWQKLPDLppapggSSQEGVAGAFAGYSNGVLLVAGGANFPGARENYQNGKLYAHEGLKKSWSDEIYALV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 485674666 313 NGKWDKSGELSQGRAYGVSLPWNNSLLIIGGETAGGKAVMDSVLISVKDNKVTVQN 368
Cdd:PRK14131 321 NGKWQKVGELPQGLAYGVSVSWNNGVLLIGGETAGGKAVSDVTLLSWDGKKLTVEN 376
muta_rot_YjhT TIGR03547
mutatrotase, YjhT family; Members of this protein family contain multiple copies of the ...
22-360 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: 516.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666   22 LPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKRWTALAAFPGGPRDQATSAFIDGNLYVFGGIGK-NSEGL 100
Cdd:TIGR03547   1 LPDLPVGFKNGTGAIIGDKVYVGLGSAGTSWYKLDLKKPSKGWQKIADFPGGPRNQAVAAAIDGKLYVFGGIGKaNSEGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  101 TQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTF-VHNGKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINAYYFDKK 179
Cdd:TIGR03547  81 PQVFDDVYRYDPKKNSWQKLDTRSPVGLLGASGFsLHNGQAYFTGGVNKNIFDGYFADLSAADKDSEPKDKLIAAYFSQP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  180 AEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVFELDFTGDNLKWNKLDPV--- 256
Cdd:TIGR03547 161 PEDYFWNKNVLSYDPSTNQWRNLGENPFLGTAGSAIVHKGNKLLLINGEIKPGLRTAEVKQYLFTGGKLEWNKLPPLppp 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  257 --SSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSADIHLWYNGKWDKSGELSQGRAYGVSLPW 334
Cdd:TIGR03547 241 ksSSQEGLAGAFAGISNGVLLVAGGANFPGAQENYKNGKLYAHEGLIKAWSSEVYALDNGKWSKVGKLPQGLAYGVSVSW 320
                         330       340
                  ....*....|....*....|....*.
gi 485674666  335 NNSLLIIGGETAGGKAVMDSVLISVK 360
Cdd:TIGR03547 321 NNGVLLIGGENSGGKAVTDVYLLSWD 346
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
17-351 1.13e-44

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 154.93  E-value: 1.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  17 ANASVLPETPVPFKSGTGAIDNDTVYIGLG----SAGTAWYKLDTqaKDKRWTALAAFPGGPRDQATSAFIDGNLYVFGG 92
Cdd:COG3055    1 ATWSSLPDLPTPRSEAAAALLDGKVYVAGGlsggSASNSFEVYDP--ATNTWSELAPLPGPPRHHAAAVAQDGKLYVFGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  93 IGKNSEGlTQVFNDVHKYNPKTNSWVKLMShAPMGMAGHVTFVHNGKAYVTGGVNQNIFNGYFEDlneagkdstaidkin 172
Cdd:COG3055   79 FTGANPS-STPLNDVYVYDPATNTWTKLAP-MPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEV--------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 173 ayyfdkkaedyffnkfllsFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEakpglrtdavfelDFTGDNLKWNK 252
Cdd:COG3055  142 -------------------YDPATGTWTQLAPLPTPRDHLAAAVLPDGKILVIGGR-------------NGSGFSNTWTT 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 253 LDPvsSPDGVAGGFAGISNDSLIFAGGagfkgsrENYQNGKNYAheglkksYSADihlwyNGKWDKSGELSQGRAYGVSL 332
Cdd:COG3055  190 LAP--LPTARAGHAAAVLGGKILVFGG-------ESGFSDEVEA-------YDPA-----TNTWTALGELPTPRHGHAAV 248
                        330
                 ....*....|....*....
gi 485674666 333 PWNNSLLIIGGETAGGKAV 351
Cdd:COG3055  249 LTDGKVYVIGGETKPGVRT 267
mutarot_permut TIGR03548
cyclically-permuted mutarotase family protein; Members of this protein family show essentially ...
22-239 8.35e-33

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: 124.90  E-value: 8.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666   22 LPETPVPFKSGTGAIDNDTVYIGLG----SAGTAWYKLDTQAKDKRWTALAAFPGGPRDQATSAFIDGNLYVFGGIgkNS 97
Cdd:TIGR03548 108 LPSLPVAFDNGSATYKDGKIYVGGGnangKPSNKFYCLDLSNDTSGWEELPEFPGEARVQPVCQALHGKLYVFGGF--QL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666   98 EGLTQVFNDVHKYNPKTNSWVK-----LMSHAPMGMAGHVTFVHN-GKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKi 171
Cdd:TIGR03548 186 GGDAIIYTDGYAYSPKTNTWQTvadpvLSDGEPITLLGGNSVKLGdSLMLVIGGVNYDIFFDAVDRLRQMKDESLKSEK- 264
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485674666  172 nAYYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVF 239
Cdd:TIGR03548 265 -AEYFGHPPQWYRFNDKVLIYNVRSNEWKSIGAVPFVARAGAALLLHGDNIFSINGEIKPGIRTPRIY 331
PHA03098 PHA03098
kelch-like protein; Provisional
74-200 1.29e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 59.40  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  74 PRDQATSAFIDGNLYVFGGIGKNSEGLtqvfNDVHKYNPKTNSWvKLMSHAPMGMAGHVTFVHNGKAYVTGGVnqnifng 153
Cdd:PHA03098 379 PRYNPCVVNVNNLIYVIGGISKNDELL----KTVECFSLNTNKW-SKGSPLPISHYGGCAIYHDGKIYVIGGI------- 446
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 485674666 154 yfedlneagkdsTAIDKINAYyfdkkaedyffnKFLLSFDPSTQQWS 200
Cdd:PHA03098 447 ------------SYIDNIKVY------------NIVESYNPVTNKWT 469
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
74-122 1.24e-06

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: 44.91  E-value: 1.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 485674666   74 PRDQATSAFIDGNLYVFGGIGKNsegltQVFNDVHKYNPKTNSWVKLMS 122
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGN-----QSLNSVEVYDPETNTWSKLPS 44
Kelch_4 pfam13418
Galactose oxidase, central domain;
74-120 3.15e-06

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 43.75  E-value: 3.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 485674666   74 PRDQATSAFI-DGNLYVFGGIGKNSegltQVFNDVHKYNPKTNSWVKL 120
Cdd:pfam13418   1 PRAYHTSTSIpDDTIYLFGGEGEDG----TLLSDLWVFDLSTNEWTRL 44
Kelch_6 pfam13964
Kelch motif;
74-120 5.45e-06

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 43.09  E-value: 5.45e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 485674666   74 PRDQATSAFIDGNLYVFGGigknSEGLTQVFNDVHKYNPKTNSWVKL 120
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGG----YTNASPALNKLEVYNPLTKSWEEL 43
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
74-120 1.13e-05

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: 41.94  E-value: 1.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 485674666   74 PRDQATSAFIDGNLYVFGGIGKNSEgltQVFNDVHKYNPKTNSWVKL 120
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDGLGD---LSSSDVLVYDPETNVWTEV 44
Kelch_3 pfam13415
Galactose oxidase, central domain;
84-131 1.10e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 36.50  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 485674666   84 DGNLYVFGGIGKNSEGLTqvfNDVHKYNPKTNSWVKLMShAPMGMAGH 131
Cdd:pfam13415   1 GDKLYIFGGLGFDGQTRL---NDLYVYDLDTNTWTQIGD-LPPPRSGH 44
PHA03098 PHA03098
kelch-like protein; Provisional
35-184 1.22e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 40.91  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  35 AIDNDTVYIgLGSAGTAWYKLDT----QAKDKRWTALAAFPGgPRDQATSAFIDGNLYVFGGIgkNSEGLTQVFNDVHKY 110
Cdd:PHA03098 386 VNVNNLIYV-IGGISKNDELLKTvecfSLNTNKWSKGSPLPI-SHYGGCAIYHDGKIYVIGGI--SYIDNIKVYNIVESY 461
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485674666 111 NPKTNSWVKL-MSHAPMGMAGhVTFVHNgKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINAYYFDKKAEDYF 184
Cdd:PHA03098 462 NPVTNKWTELsSLNFPRINAS-LCIFNN-KIYVVGGDKYEYYINEIEVYDDKTNTWTLFCKFPKVIGSLEKNIFT 534
PHA03098 PHA03098
kelch-like protein; Provisional
42-280 2.92e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 39.37  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666  42 YIGLGSAGTAWYKLDTQAKDKRWTALAAFPGgpRDQATSAFIDGNLYVFGGIGKNSEgltqVFNDVHKYNPKTNSWVKL- 120
Cdd:PHA03098 254 YIHITMSIFTYNYITNYSPLSEINTIIDIHY--VYCFGSVVLNNVIYFIGGMNKNNL----SVNSVVSYDTKTKSWNKVp 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 121 -MSHAPMGMAghvTFVHNGKAYVTGGVNQNIFNGYFE-------------DLNEAgKDSTAIDKINA--YYFDKKAEDYF 184
Cdd:PHA03098 328 eLIYPRKNPG---VTVFNNRIYVIGGIYNSISLNTVEswkpgeskwreepPLIFP-RYNPCVVNVNNliYVIGGISKNDE 403
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485674666 185 FNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGdKTWLING--EAKPGLRTDAVFELDFTGDnlKWNKLDPVSSPDGV 262
Cdd:PHA03098 404 LLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDG-KIYVIGGisYIDNIKVYNIVESYNPVTN--KWTELSSLNFPRIN 480
                        250
                 ....*....|....*...
gi 485674666 263 AggFAGISNDSLIFAGGA 280
Cdd:PHA03098 481 A--SLCIFNNKIYVVGGD 496
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
74-115 3.83e-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: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 34.85  E-value: 3.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 485674666   74 PRDQATSAFIDGNLYVFGGIGKNSeglTQVFNDVHKYNPKTN 115
Cdd:pfam13854   3 PRYGHCAVTVGDYIYLYGGYTGGE---GQPSDDVYVLSLPTF 41
Kelch smart00612
Kelch domain;
87-133 4.86e-03

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 34.84  E-value: 4.86e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 485674666    87 LYVFGGIgkNSeglTQVFNDVHKYNPKTNSWVKL--MSHAPMGMAGHVT 133
Cdd:smart00612   2 IYVVGGF--DG---GQRLKSVEVYDPETNKWTPLpsMPTPRSGHGVAVI 45
 
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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