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Conserved domains on  [gi|15234996|ref|NP_195635|]
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Galactose oxidase/kelch repeat superfamily protein [Arabidopsis thaliana]

Protein Classification

F-box/kelch-repeat protein( domain architecture ID 17778853)

F-box/kelch-repeat protein may be a component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins

CATH:  1.20.1280.50|2.120.10.80
Gene Ontology:  GO:0006511|GO:0019005|GO:0005515|GO:0016567
PubMed:  10603472|31898225|11178263|31442578|24959344|10581972
SCOP:  4001927|3000448

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NanM super family cl34543
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
120-320 3.77e-18

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


The actual alignment was detected with superfamily member COG3055:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 83.67  E-value: 3.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996 120 PIPSFPSIPCWGMSIVAIDSEIYVLGGCIDN----ELVSTGFVVECPSHTCRLLPSMKQARGCAAVGFFDGKLYVIGGCN 195
Cdd:COG3055  52 ELAPLPGPPRHHAAAVAQDGKLYVFGGFTGAnpssTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWD 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996 196 PLS-VNWVEAFDLKTQTWESGLGVNNVEMHDLTIrsFAIDDKIYIMDRKNSFVYDPKEGTLETdeLLDTQWSVGSCVIDG 274
Cdd:COG3055 132 DGGnVAWVEVYDPATGTWTQLAPLPTPRDHLAAA--VLPDGKILVIGGRNGSGFSNTWTTLAP--LPTARAGHAAAVLGG 207

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15234996 275 KIYTFGSKNR----IWVFDPIAMVWdrlKGLDDLPDKRDGSRMSNLGGNL 320
Cdd:COG3055 208 KILVFGGESGfsdeVEAYDPATNTW---TALGELPTPRHGHAAVLTDGKV 254
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 33-77 3.67e-15

F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and similar proteins; AtAFR, also called SKP1-interacting partner 29 (AtSKIP29), or F-box protein AFR, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It is part of the phyA-mediated signaling transduction pathway leading to the regulation of gene expression and hypocotyl elongation in response to red and far-red light exposure. This subfamily also includes many other Arabidopsis thaliana SKP1-interacting partner proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


:

Pssm-ID: 438923  Cd Length: 45  Bit Score: 68.75  E-value: 3.67e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15234996  33 YLLLLPDEIILNCLARLPKCYYPVISLVSKTFRRLIASPEIYVER 77
Cdd:cd22152   1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
120-320 3.77e-18

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 83.67  E-value: 3.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996 120 PIPSFPSIPCWGMSIVAIDSEIYVLGGCIDN----ELVSTGFVVECPSHTCRLLPSMKQARGCAAVGFFDGKLYVIGGCN 195
Cdd:COG3055  52 ELAPLPGPPRHHAAAVAQDGKLYVFGGFTGAnpssTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWD 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996 196 PLS-VNWVEAFDLKTQTWESGLGVNNVEMHDLTIrsFAIDDKIYIMDRKNSFVYDPKEGTLETdeLLDTQWSVGSCVIDG 274
Cdd:COG3055 132 DGGnVAWVEVYDPATGTWTQLAPLPTPRDHLAAA--VLPDGKILVIGGRNGSGFSNTWTTLAP--LPTARAGHAAAVLGG 207

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15234996 275 KIYTFGSKNR----IWVFDPIAMVWdrlKGLDDLPDKRDGSRMSNLGGNL 320
Cdd:COG3055 208 KILVFGGESGfsdeVEAYDPATNTW---TALGELPTPRHGHAAVLTDGKV 254
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 33-77 3.67e-15

F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and similar proteins; AtAFR, also called SKP1-interacting partner 29 (AtSKIP29), or F-box protein AFR, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It is part of the phyA-mediated signaling transduction pathway leading to the regulation of gene expression and hypocotyl elongation in response to red and far-red light exposure. This subfamily also includes many other Arabidopsis thaliana SKP1-interacting partner proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438923  Cd Length: 45  Bit Score: 68.75  E-value: 3.67e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15234996  33 YLLLLPDEIILNCLARLPKCYYPVISLVSKTFRRLIASPEIYVER 77
Cdd:cd22152   1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 175-215 2.60e-09

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: 52.23  E-value: 2.60e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15234996   175 ARGCAAVGFFDGKLYVIGGCNPL-SVNWVEAFDLKTQTWESG 215
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNqSLNSVEVYDPETNTWSKL 42
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 34-75 5.68e-08

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 48.69  E-value: 5.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15234996    34 LLLLPDEIILNCLARLPKCYYPVISLVSKTFRRLIASPEIYV 75
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42
PHA03098 PHA03098
kelch-like protein; Provisional
 135-301 2.85e-07

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 52.08  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996  135 VAIDSEIYVLGGCIDNELVSTGFV-VECPSHTCRLLPSMKQARGCAAVGFFDGKLYVIGGC-NPLSVNWVEAFDLKTQTW 212
Cdd:PHA03098 291 VVLNNVIYFIGGMNKNNLSVNSVVsYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIyNSISLNTVESWKPGESKW 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996  213 ESglgvnnvEMHDLTIRSFA----IDDKIYIMDrkNSFVYDPKEGTLETDELLDTQWS---------VGSCVI--DGKIY 277
Cdd:PHA03098 371 RE-------EPPLIFPRYNPcvvnVNNLIYVIG--GISKNDELLKTVECFSLNTNKWSkgsplpishYGGCAIyhDGKIY 441

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15234996  278 TFGSK---------NRIWVFDPIAMVWDRLKGL 301
Cdd:PHA03098 442 VIGGIsyidnikvyNIVESYNPVTNKWTELSSL 474
FBOX smart00256
A Receptor for Ubiquitination Targets;
37-77 2.03e-06

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 43.96  E-value: 2.03e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 15234996     37 LPDEIILNCLARLPKCYYPVISLVSKTFRRLIASPEIYVER 77
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
Kelch smart00612
Kelch domain;
141-186 2.93e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 38.31  E-value: 2.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 15234996    141 IYVLGGCIDNELVSTGFVVECPSHTCRLLPSMKQARGCAAVGFFDG 186
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
120-320 3.77e-18

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 83.67  E-value: 3.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996 120 PIPSFPSIPCWGMSIVAIDSEIYVLGGCIDN----ELVSTGFVVECPSHTCRLLPSMKQARGCAAVGFFDGKLYVIGGCN 195
Cdd:COG3055  52 ELAPLPGPPRHHAAAVAQDGKLYVFGGFTGAnpssTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWD 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996 196 PLS-VNWVEAFDLKTQTWESGLGVNNVEMHDLTIrsFAIDDKIYIMDRKNSFVYDPKEGTLETdeLLDTQWSVGSCVIDG 274
Cdd:COG3055 132 DGGnVAWVEVYDPATGTWTQLAPLPTPRDHLAAA--VLPDGKILVIGGRNGSGFSNTWTTLAP--LPTARAGHAAAVLGG 207

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15234996 275 KIYTFGSKNR----IWVFDPIAMVWdrlKGLDDLPDKRDGSRMSNLGGNL 320
Cdd:COG3055 208 KILVFGGESGfsdeVEAYDPATNTW---TALGELPTPRHGHAAVLTDGKV 254
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
169-310 1.38e-15

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 75.96  E-value: 1.38e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996 169 LPSMKQARGCAAVGFFDGKLYVIGGCNPLSVNW-VEAFDLKTQTWESGLGVNNVEMHDLTirSFAIDDKIYIM------- 240
Cdd:COG3055   6 LPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNsFEVYDPATNTWSELAPLPGPPRHHAA--AVAQDGKLYVFggftgan 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996 241 ----DRKNSFVYDPKEGT-LETDELLDTQWSVGSCVIDGKIYTFG------SKNRIWVFDPIAMVWDRLKgldDLPDKRD 309
Cdd:COG3055  84 psstPLNDVYVYDPATNTwTKLAPMPTPRGGATALLLDGKIYVVGgwddggNVAWVEVYDPATGTWTQLA---PLPTPRD 160


                .
gi 15234996 310 G 310
Cdd:COG3055 161 H 161
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 33-77 3.67e-15

F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and similar proteins; AtAFR, also called SKP1-interacting partner 29 (AtSKIP29), or F-box protein AFR, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It is part of the phyA-mediated signaling transduction pathway leading to the regulation of gene expression and hypocotyl elongation in response to red and far-red light exposure. This subfamily also includes many other Arabidopsis thaliana SKP1-interacting partner proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438923  Cd Length: 45  Bit Score: 68.75  E-value: 3.67e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15234996  33 YLLLLPDEIILNCLARLPKCYYPVISLVSKTFRRLIASPEIYVER 77
Cdd:cd22152   1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 175-215 2.60e-09

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: 52.23  E-value: 2.60e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15234996   175 ARGCAAVGFFDGKLYVIGGCNPL-SVNWVEAFDLKTQTWESG 215
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNqSLNSVEVYDPETNTWSKL 42
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 34-75 5.68e-08

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 48.69  E-value: 5.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15234996    34 LLLLPDEIILNCLARLPKCYYPVISLVSKTFRRLIASPEIYV 75
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42
PHA03098 PHA03098
kelch-like protein; Provisional
 135-301 2.85e-07

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 52.08  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996  135 VAIDSEIYVLGGCIDNELVSTGFV-VECPSHTCRLLPSMKQARGCAAVGFFDGKLYVIGGC-NPLSVNWVEAFDLKTQTW 212
Cdd:PHA03098 291 VVLNNVIYFIGGMNKNNLSVNSVVsYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIyNSISLNTVESWKPGESKW 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996  213 ESglgvnnvEMHDLTIRSFA----IDDKIYIMDrkNSFVYDPKEGTLETDELLDTQWS---------VGSCVI--DGKIY 277
Cdd:PHA03098 371 RE-------EPPLIFPRYNPcvvnVNNLIYVIG--GISKNDELLKTVECFSLNTNKWSkgsplpishYGGCAIyhDGKIY 441

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15234996  278 TFGSK---------NRIWVFDPIAMVWDRLKGL 301
Cdd:PHA03098 442 VIGGIsyidnikvyNIVESYNPVTNKWTELSSL 474
PHA03098 PHA03098
kelch-like protein; Provisional
 106-227 1.98e-06

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 49.77  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234996  106 FKPFGNDSNNHRLVPIPSFpsipcwGMSIVAIDSEIYVLGGC--IDNELVSTgfVVECPS-HTC--RLLPSMKQARGCAA 180
Cdd:PHA03098 411 FSLNTNKWSKGSPLPISHY------GGCAIYHDGKIYVIGGIsyIDNIKVYN--IVESYNpVTNkwTELSSLNFPRINAS 482

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15234996  181 VGFFDGKLYVIGG-CNPLSVNWVEAFDLKTQTWESGLG----VNNVEMHDLT 227
Cdd:PHA03098 483 LCIFNNKIYVVGGdKYEYYINEIEVYDDKTNTWTLFCKfpkvIGSLEKNIFT 534
FBOX smart00256
A Receptor for Ubiquitination Targets;
37-77 2.03e-06

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 43.96  E-value: 2.03e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 15234996     37 LPDEIILNCLARLPKCYYPVISLVSKTFRRLIASPEIYVER 77
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 131-173 1.54e-04

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: 38.75  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15234996   131 GMSIVAIDSEIYVLGGCIDNELVSTGFVVECPSHTCRLLPSMK 173
Cdd:pfam01344   4 GAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPSMP 46
Kelch smart00612
Kelch domain;
141-186 2.93e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 38.31  E-value: 2.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 15234996    141 IYVLGGCIDNELVSTGFVVECPSHTCRLLPSMKQARGCAAVGFFDG 186
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
F-box_ScMDM30-like cd22143
F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology ...
 34-77 1.11e-03

F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology protein 30 (ScMDM30) and similar proteins; ScMDM30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. It is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. ScMDM30 recognizes FZO1 and regulates the amount of FZO1. It acts as a regulatory factor for the mitochondrial fusion machinery and is required for mitochondrial DNA maintenance. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438915  Cd Length: 44  Bit Score: 36.44  E-value: 1.11e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15234996  34 LLLLPDEIILNCLARLPKCYYPVISLVSKTFRRlIASPEIYVER 77
Cdd:cd22143   2 FDSLPDEILSIIFSHLPQSDLYNLLFVNKHFYS-LALPELWRSI 44
Kelch smart00612
Kelch domain;
187-215 4.62e-03

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 34.84  E-value: 4.62e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 15234996    187 KLYVIGGCNP-LSVNWVEAFDLKTQTWESG 215
Cdd:smart00612   1 KIYVVGGFDGgQRLKSVEVYDPETNKWTPL 30
Kelch_4 pfam13418
Galactose oxidase, central domain;
177-213 5.79e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 34.51  E-value: 5.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 15234996   177 GCAAVGFFDGKLYVIGGCNPLSV--NWVEAFDLKTQTWE 213
Cdd:pfam13418   4 YHTSTSIPDDTIYLFGGEGEDGTllSDLWVFDLSTNEWT 42
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 269-301 6.89e-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: 34.23  E-value: 6.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 15234996   269 SCVIDGKIYTFG--------SKNRIWVFDPIAMVWDRLKGL 301
Cdd:pfam07646   7 SSVPGGKLYVVGgsdglgdlSSSDVLVYDPETNVWTEVPRL 47
 
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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