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Conserved domains on  [gi|15229392|ref|NP_191881|]
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Galactose oxidase/kelch repeat superfamily protein [Arabidopsis thaliana]

Protein Classification

F-box/kelch-repeat protein( domain architecture ID 19211583)

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|10581972|31442578|24959344
SCOP:  4001927|3000448

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
64-299 3.16e-26

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 105.24  E-value: 3.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392  64 DPENIWQVYSPNCDRWLTLPLLPSRIRHlaHFGAVTTAGMLFVLGGgsdavspVTGDHDGTFATDQVWSYDFVQRQWTPR 143
Cdd:COG3055  35 SASNSFEVYDPATNTWSELAPLPGPPRH--HAAAVAQDGKLYVFGG-------FTGANPSSTPLNDVYVYDPATNTWTKL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 144 ASMLVPRAMFACCVLQGKIVVAGGFTTCRKSISgAEMYDPENDVWTSIPDLHQTHNSACSGLVVNGKVHVL-----HKGL 218
Cdd:COG3055 106 APMPTPRGGATALLLDGKIYVVGGWDDGGNVAW-VEVYDPATGTWTQLAPLPTPRDHLAAAVLPDGKILVIggrngSGFS 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 219 STVQVLESVKLGWDVKDYGWPQGPMVVVEDVLYVMSHGLVFKQEGDTWKmVASASEFKRRiGMAMTSLSDEVLIVGGVIG 298
Cdd:COG3055 185 NTWTTLAPLPTARAGHAAAVLGGKILVFGGESGFSDEVEAYDPATNTWT-ALGELPTPRH-GHAAVLTDGKVYVIGGETK 262


                .
gi 15229392 299 P 299
Cdd:COG3055 263 P 263
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 4-48 7.31e-13

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: 62.20  E-value: 7.31e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15229392   4 LLDGIPEAVALRCLAHVPLHLHPNLELVSRSWRAAIRSHELFRVR 48
Cdd:cd22152   1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
64-299 3.16e-26

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 105.24  E-value: 3.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392  64 DPENIWQVYSPNCDRWLTLPLLPSRIRHlaHFGAVTTAGMLFVLGGgsdavspVTGDHDGTFATDQVWSYDFVQRQWTPR 143
Cdd:COG3055  35 SASNSFEVYDPATNTWSELAPLPGPPRH--HAAAVAQDGKLYVFGG-------FTGANPSSTPLNDVYVYDPATNTWTKL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 144 ASMLVPRAMFACCVLQGKIVVAGGFTTCRKSISgAEMYDPENDVWTSIPDLHQTHNSACSGLVVNGKVHVL-----HKGL 218
Cdd:COG3055 106 APMPTPRGGATALLLDGKIYVVGGWDDGGNVAW-VEVYDPATGTWTQLAPLPTPRDHLAAAVLPDGKILVIggrngSGFS 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 219 STVQVLESVKLGWDVKDYGWPQGPMVVVEDVLYVMSHGLVFKQEGDTWKmVASASEFKRRiGMAMTSLSDEVLIVGGVIG 298
Cdd:COG3055 185 NTWTTLAPLPTARAGHAAAVLGGKILVFGGESGFSDEVEAYDPATNTWT-ALGELPTPRH-GHAAVLTDGKVYVIGGETK 262


                .
gi 15229392 299 P 299
Cdd:COG3055 263 P 263
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 4-48 7.31e-13

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: 62.20  E-value: 7.31e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15229392   4 LLDGIPEAVALRCLAHVPLHLHPNLELVSRSWRAAIRSHELFRVR 48
Cdd:cd22152   1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
PHA03098 PHA03098
kelch-like protein; Provisional
 17-295 5.16e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 57.47  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392   17 LAHVPLHLHPNLELVSRSWRAAIRSHELFRVRKELRSSEH-----LLCVCAFDPENIWQVYSPNcDRWLTLpllpSRIRH 91
Cdd:PHA03098 210 LKRWKLRIKKKKIVFNKRCIKIIYSKKYNLNKILPRSSTFgsiiyIHITMSIFTYNYITNYSPL-SEINTI----IDIHY 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392   92 LAHFGAVTTAGMLFVLGGGSDAVSPVtgdhdgtfatDQVWSYDFVQRQWTPRASMLVPRAMFACCVLQGKIVVAGGFTTc 171
Cdd:PHA03098 285 VYCFGSVVLNNVIYFIGGMNKNNLSV----------NSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYN- 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392  172 RKSISGAEMYDPENDVWTSIPDLHQTHNSACSgLVVNGKVHVL------HKGLSTVQVLESVKLGWDVKD---YGWPQGP 242
Cdd:PHA03098 354 SISLNTVESWKPGESKWREEPPLIFPRYNPCV-VNVNNLIYVIggisknDELLKTVECFSLNTNKWSKGSplpISHYGGC 432

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229392  243 MVVVEDVLYV---MSH-------GLVFKQ--EGDTWKMVASAseFKRRIGMAMTSLSDEVLIVGG 295
Cdd:PHA03098 433 AIYHDGKIYViggISYidnikvyNIVESYnpVTNKWTELSSL--NFPRINASLCIFNNKIYVVGG 495
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 149-194 3.53e-08

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: 49.15  E-value: 3.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 15229392   149 PRAMFACCVLQGKIVVAGGFTTCRkSISGAEMYDPENDVWTSIPDL 194
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQ-SLNSVEVYDPETNTWSKLPSM 45
Kelch smart00612
Kelch domain;
117-160 9.10e-07

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 45.24  E-value: 9.10e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 15229392    117 VTGDHDGTFATDQVWSYDFVQRQWTPRASMLVPRAMFACCVLQG 160
Cdd:smart00612   4 VVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 5-46 2.70e-03

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: 35.21  E-value: 2.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15229392     5 LDGIPEAVALRCLAHVPLHLHPNLELVSRSWRAAIRSHELFR 46
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42
FBOX smart00256
A Receptor for Ubiquitination Targets;
8-46 5.43e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 34.33  E-value: 5.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 15229392      8 IPEAVALRCLAHVPLHLHPNLELVSRSWRAAIRSHELFR 46
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
64-299 3.16e-26

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 105.24  E-value: 3.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392  64 DPENIWQVYSPNCDRWLTLPLLPSRIRHlaHFGAVTTAGMLFVLGGgsdavspVTGDHDGTFATDQVWSYDFVQRQWTPR 143
Cdd:COG3055  35 SASNSFEVYDPATNTWSELAPLPGPPRH--HAAAVAQDGKLYVFGG-------FTGANPSSTPLNDVYVYDPATNTWTKL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 144 ASMLVPRAMFACCVLQGKIVVAGGFTTCRKSISgAEMYDPENDVWTSIPDLHQTHNSACSGLVVNGKVHVL-----HKGL 218
Cdd:COG3055 106 APMPTPRGGATALLLDGKIYVVGGWDDGGNVAW-VEVYDPATGTWTQLAPLPTPRDHLAAAVLPDGKILVIggrngSGFS 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 219 STVQVLESVKLGWDVKDYGWPQGPMVVVEDVLYVMSHGLVFKQEGDTWKmVASASEFKRRiGMAMTSLSDEVLIVGGVIG 298
Cdd:COG3055 185 NTWTTLAPLPTARAGHAAAVLGGKILVFGGESGFSDEVEAYDPATNTWT-ALGELPTPRH-GHAAVLTDGKVYVIGGETK 262


                .
gi 15229392 299 P 299
Cdd:COG3055 263 P 263
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
79-331 2.21e-20

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 89.44  E-value: 2.21e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392  79 WLTLPLLPSrirHLAHFGAVTTAGMLFVLGGgsdavspvtgdHDGTFATDQVWSYDFVQRQWTPRASM-LVPRAMFACCV 157
Cdd:COG3055   3 WSSLPDLPT---PRSEAAAALLDGKVYVAGG-----------LSGGSASNSFEVYDPATNTWSELAPLpGPPRHHAAAVA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 158 LQGKIVVAGGFTTC---RKSISGAEMYDPENDVWTSIPDLHQTHNSAcSGLVVNGKVHVL-----HKGLSTVQVLESVKL 229
Cdd:COG3055  69 QDGKLYVFGGFTGAnpsSTPLNDVYVYDPATNTWTKLAPMPTPRGGA-TALLLDGKIYVVggwddGGNVAWVEVYDPATG 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 230 GWDVKdygwpqGPM----------VVVEDVLYVMShGLVFKQEGDTWKMVASASEFkrRIGMAMTSLSDEVLIVGGVIGp 299
Cdd:COG3055 148 TWTQL------APLptprdhlaaaVLPDGKILVIG-GRNGSGFSNTWTTLAPLPTA--RAGHAAAVLGGKILVFGGESG- 217

                       250       260       270
                ....*....|....*....|....*....|..
gi 15229392 300 drlnwdikPLSDVDALTVGNDRpaWRSVAPMT 331
Cdd:COG3055 218 --------FSDEVEAYDPATNT--WTALGELP 239
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
139-334 5.32e-14

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 71.34  E-value: 5.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 139 QWTPRASMLVPRAMFACCVLQGKIVVAGGFTTCRkSISGAEMYDPENDVWTSIPDLHQTHNSACSGLVVNGKVHVLhkGl 218
Cdd:COG3055   2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGS-ASNSFEVYDPATNTWSELAPLPGPPRHHAAAVAQDGKLYVF--G- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392 219 stvqvlesvklGWDVKDYGWPqgpmvvvedvlyVMSHGLVFKQEGDTWKMVASASEfkRRIGMAMTSLSDEVLIVGGVIG 298
Cdd:COG3055  78 -----------GFTGANPSST------------PLNDVYVYDPATNTWTKLAPMPT--PRGGATALLLDGKIYVVGGWDD 132

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15229392 299 PDRLNWdikplsdVDALTVGNDRpaWRSVAPMTRCR 334
Cdd:COG3055 133 GGNVAW-------VEVYDPATGT--WTQLAPLPTPR 159
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 4-48 7.31e-13

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: 62.20  E-value: 7.31e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15229392   4 LLDGIPEAVALRCLAHVPLHLHPNLELVSRSWRAAIRSHELFRVR 48
Cdd:cd22152   1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
PHA03098 PHA03098
kelch-like protein; Provisional
 17-295 5.16e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 57.47  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392   17 LAHVPLHLHPNLELVSRSWRAAIRSHELFRVRKELRSSEH-----LLCVCAFDPENIWQVYSPNcDRWLTLpllpSRIRH 91
Cdd:PHA03098 210 LKRWKLRIKKKKIVFNKRCIKIIYSKKYNLNKILPRSSTFgsiiyIHITMSIFTYNYITNYSPL-SEINTI----IDIHY 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392   92 LAHFGAVTTAGMLFVLGGGSDAVSPVtgdhdgtfatDQVWSYDFVQRQWTPRASMLVPRAMFACCVLQGKIVVAGGFTTc 171
Cdd:PHA03098 285 VYCFGSVVLNNVIYFIGGMNKNNLSV----------NSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYN- 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229392  172 RKSISGAEMYDPENDVWTSIPDLHQTHNSACSgLVVNGKVHVL------HKGLSTVQVLESVKLGWDVKD---YGWPQGP 242
Cdd:PHA03098 354 SISLNTVESWKPGESKWREEPPLIFPRYNPCV-VNVNNLIYVIggisknDELLKTVECFSLNTNKWSKGSplpISHYGGC 432

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229392  243 MVVVEDVLYV---MSH-------GLVFKQ--EGDTWKMVASAseFKRRIGMAMTSLSDEVLIVGG 295
Cdd:PHA03098 433 AIYHDGKIYViggISYidnikvyNIVESYnpVTNKWTELSSL--NFPRINASLCIFNNKIYVVGG 495
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 149-194 3.53e-08

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: 49.15  E-value: 3.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 15229392   149 PRAMFACCVLQGKIVVAGGFTTCRkSISGAEMYDPENDVWTSIPDL 194
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQ-SLNSVEVYDPETNTWSKLPSM 45
Kelch smart00612
Kelch domain;
117-160 9.10e-07

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 45.24  E-value: 9.10e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 15229392    117 VTGDHDGTFATDQVWSYDFVQRQWTPRASMLVPRAMFACCVLQG 160
Cdd:smart00612   4 VVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
Kelch smart00612
Kelch domain;
161-209 3.56e-06

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 43.32  E-value: 3.56e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 15229392    161 KIVVAGGFTTCRkSISGAEMYDPENDVWTSIPDLHQTHnSACSGLVVNG 209
Cdd:smart00612   1 KIYVVGGFDGGQ-RLKSVEVYDPETNKWTPLPSMPTPR-SGHGVAVING 47
Kelch_6 pfam13964
Kelch motif;
149-194 7.91e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 39.63  E-value: 7.91e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 15229392   149 PRAMFACCVLQGKIVVAGGFTTCRKSISGAEMYDPENDVWTSIPDL 194
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPL 46
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 93-146 4.62e-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: 37.59  E-value: 4.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15229392    93 AHFGAVTTAGMLFVLGGgsdavspvtgdHDGTFATDQVWSYDFVQRQWTPRASM 146
Cdd:pfam01344   3 SGAGVVVVGGKIYVIGG-----------FDGNQSLNSVEVYDPETNTWSKLPSM 45
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 5-46 2.70e-03

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: 35.21  E-value: 2.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15229392     5 LDGIPEAVALRCLAHVPLHLHPNLELVSRSWRAAIRSHELFR 46
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42
Kelch_3 pfam13415
Galactose oxidase, central domain;
102-158 4.43e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 34.96  E-value: 4.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15229392   102 GMLFVLGGGSDavspvtgdHDGTFATDQVWSYDFVQRQWTPRASMLVPRAMFACCVL 158
Cdd:pfam13415   1 GDKLYIFGGLG--------FDGQTRLNDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 49
FBOX smart00256
A Receptor for Ubiquitination Targets;
8-46 5.43e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 34.33  E-value: 5.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 15229392      8 IPEAVALRCLAHVPLHLHPNLELVSRSWRAAIRSHELFR 46
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
 
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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