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Conserved domains on  [gi|15227579|ref|NP_180520|]
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Galactose oxidase/kelch repeat superfamily protein [Arabidopsis thaliana]

Protein Classification

F-box/kelch-repeat protein( domain architecture ID 20253241)

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

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];
144-357 1.14e-20

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 90.99  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 144 TSLPPMfPGC-----TTVTIGHKIYVMGGLRSLNRRA---KTVFVIDCRFHTWRYLQEMQVARSYAASAVIDGMIYVVGG 215
Cdd:COG3055  51 SELAPL-PGPprhhaAAVAQDGKLYVFGGFTGANPSStplNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGG 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 216 STKRSD-DWVEVFNVETNTWENVPSVLSPygrsKAPFNVHFVLDNKIYILDGNNRVAYDLRgrrwedWGPAGNQLGYFWQ 294
Cdd:COG3055 130 WDDGGNvAWVEVYDPATGTWTQLAPLPTP----RDHLAAAVLPDGKILVIGGRNGSGFSNT------WTTLAPLPTARAG 199
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227579 295 VLYCVVDNLLYAVVPDHLHVTPIVVYDPREMGWRPvmgVDYLPNLVYSESRMTnFGGKLMILG 357
Cdd:COG3055 200 HAAAVLGGKILVFGGESGFSDEVEAYDPATNTWTA---LGELPTPRHGHAAVL-TDGKVYVIG 258
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
59-101 6.19e-07

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. 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. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


The actual alignment was detected with superfamily member cd22152:

Pssm-ID: 459239  Cd Length: 45  Bit Score: 45.64  E-value: 6.19e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15227579  59 PQMPLELIVSTIATLRRCHYPTLSLLSDSFRQVISSVDLFQTR 101
Cdd:cd22152   3 PGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
144-357 1.14e-20

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 90.99  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 144 TSLPPMfPGC-----TTVTIGHKIYVMGGLRSLNRRA---KTVFVIDCRFHTWRYLQEMQVARSYAASAVIDGMIYVVGG 215
Cdd:COG3055  51 SELAPL-PGPprhhaAAVAQDGKLYVFGGFTGANPSStplNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGG 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 216 STKRSD-DWVEVFNVETNTWENVPSVLSPygrsKAPFNVHFVLDNKIYILDGNNRVAYDLRgrrwedWGPAGNQLGYFWQ 294
Cdd:COG3055 130 WDDGGNvAWVEVYDPATGTWTQLAPLPTP----RDHLAAAVLPDGKILVIGGRNGSGFSNT------WTTLAPLPTARAG 199
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227579 295 VLYCVVDNLLYAVVPDHLHVTPIVVYDPREMGWRPvmgVDYLPNLVYSESRMTnFGGKLMILG 357
Cdd:COG3055 200 HAAAVLGGKILVFGGESGFSDEVEAYDPATNTWTA---LGELPTPRHGHAAVL-TDGKVYVIG 258
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
197-239 2.53e-10

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: 55.31  E-value: 2.53e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15227579   197 ARSYAASAVIDGMIYVVGGST-KRSDDWVEVFNVETNTWENVPS 239
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDgNQSLNSVEVYDPETNTWSKLPS 44
PRK14131 PRK14131
N-acetylneuraminate epimerase;
146-357 3.86e-09

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 58.10  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  146 LPPMFPGCTTVTIGHKIYVmgGLRSLnrrAKTVFVIDCRFHT--WRYLQEMQ-VARSYAASAVIDGMIYVVGGSTKRSDD 222
Cdd:PRK14131  25 LPVPFKNGTGAIDNNTVYV--GLGSA---GTSWYKLDLNAPSkgWTKIAAFPgGPREQAVAAFIDGKLYVFGGIGKTNSE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  223 W-------VEVFNVETNTWENVPSVlSPYGRSKApfnVHFVLDN-KIYILDGNNRVAYDlrgRRWEDWGPAGNQlgyfwq 294
Cdd:PRK14131 100 GspqvfddVYKYDPKTNSWQKLDTR-SPVGLAGH---VAVSLHNgKAYITGGVNKNIFD---GYFEDLAAAGKD------ 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227579  295 vlycvvDNLLYAVVPDHLHVTP--------IVVYDPREMGWRPVMGVDYLPNlvySESRMTNFGGKLMILG 357
Cdd:PRK14131 167 ------KTPKDKINDAYFDKKPedyffnkeVLSYDPSTNQWKNAGESPFLGT---AGSAVVIKGNKLWLIN 228
Kelch smart00612
Kelch domain;
161-208 4.63e-07

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 46.01  E-value: 4.63e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 15227579    161 KIYVMGGLRSlNRRAKTVFVIDCRFHTWRYLQEMQVARSYAASAVIDG 208
Cdd:smart00612   1 KIYVVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
59-101 6.19e-07

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: 45.64  E-value: 6.19e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15227579  59 PQMPLELIVSTIATLRRCHYPTLSLLSDSFRQVISSVDLFQTR 101
Cdd:cd22152   3 PGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
144-357 1.14e-20

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 90.99  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 144 TSLPPMfPGC-----TTVTIGHKIYVMGGLRSLNRRA---KTVFVIDCRFHTWRYLQEMQVARSYAASAVIDGMIYVVGG 215
Cdd:COG3055  51 SELAPL-PGPprhhaAAVAQDGKLYVFGGFTGANPSStplNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGG 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 216 STKRSD-DWVEVFNVETNTWENVPSVLSPygrsKAPFNVHFVLDNKIYILDGNNRVAYDLRgrrwedWGPAGNQLGYFWQ 294
Cdd:COG3055 130 WDDGGNvAWVEVYDPATGTWTQLAPLPTP----RDHLAAAVLPDGKILVIGGRNGSGFSNT------WTTLAPLPTARAG 199
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227579 295 VLYCVVDNLLYAVVPDHLHVTPIVVYDPREMGWRPvmgVDYLPNLVYSESRMTnFGGKLMILG 357
Cdd:COG3055 200 HAAAVLGGKILVFGGESGFSDEVEAYDPATNTWTA---LGELPTPRHGHAAVL-TDGKVYVIG 258
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
144-280 7.72e-19

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 85.98  E-value: 7.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 144 TSLPPM-FPG--CTTVTIGHKIYVMGGLRSlNRRAKTVFVIDCRFHTWRYLQEM-QVARSYAASAVIDGMIYVVGGSTKR 219
Cdd:COG3055   4 SSLPDLpTPRseAAAALLDGKVYVAGGLSG-GSASNSFEVYDPATNTWSELAPLpGPPRHHAAAVAQDGKLYVFGGFTGA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227579 220 SDDW-----VEVFNVETNTWENVPSvlSPYGRSKApfnVHFVLDNKIYILDGNNRVA-------YDLRGRRWE 280
Cdd:COG3055  83 NPSStplndVYVYDPATNTWTKLAP--MPTPRGGA---TALLLDGKIYVVGGWDDGGnvawvevYDPATGTWT 150
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
187-357 5.92e-16

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 77.50  E-value: 5.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 187 TWRYLQEMQVARSYAASAVIDGMIYVVGGSTKRSDDW-VEVFNVETNTWENVPSVlsPYGRSKAPfnVHFVLDNKIYILD 265
Cdd:COG3055   2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNsFEVYDPATNTWSELAPL--PGPPRHHA--AAVAQDGKLYVFG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 266 GNNRVA-----------YDLRGRRWEDWGPAGNQLGYFWQVLYcvvDNLLYAV--VPDHLHVTPIVVYDPREMGWRPvmg 332
Cdd:COG3055  78 GFTGANpsstplndvyvYDPATNTWTKLAPMPTPRGGATALLL---DGKIYVVggWDDGGNVAWVEVYDPATGTWTQ--- 151
                       170       180
                ....*....|....*....|....*
gi 15227579 333 VDYLPNLVYSESRMTNFGGKLMILG 357
Cdd:COG3055 152 LAPLPTPRDHLAAAVLPDGKILVIG 176
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
143-284 2.70e-12

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 66.72  E-value: 2.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 143 VTSLPPMFPGCTTVTIGHKIYVMGGlRSLNRRAKTVFVIDCRFHTWRYLQEMQVARSYAASAVI-DGMIYVVGGSTkrsd 221
Cdd:COG3055 105 LAPMPTPRGGATALLLDGKIYVVGG-WDDGGNVAWVEVYDPATGTWTQLAPLPTPRDHLAAAVLpDGKILVIGGRN---- 179
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227579 222 dwvevFNVETNTWENVPSVLSPYGRSKAPfnvhfVLDNKIYILDGNNRV-----AYDLRGRRWEDWGP 284
Cdd:COG3055 180 -----GSGFSNTWTTLAPLPTARAGHAAA-----VLGGKILVFGGESGFsdeveAYDPATNTWTALGE 237
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
197-239 2.53e-10

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: 55.31  E-value: 2.53e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15227579   197 ARSYAASAVIDGMIYVVGGST-KRSDDWVEVFNVETNTWENVPS 239
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDgNQSLNSVEVYDPETNTWSKLPS 44
PRK14131 PRK14131
N-acetylneuraminate epimerase;
146-357 3.86e-09

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 58.10  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  146 LPPMFPGCTTVTIGHKIYVmgGLRSLnrrAKTVFVIDCRFHT--WRYLQEMQ-VARSYAASAVIDGMIYVVGGSTKRSDD 222
Cdd:PRK14131  25 LPVPFKNGTGAIDNNTVYV--GLGSA---GTSWYKLDLNAPSkgWTKIAAFPgGPREQAVAAFIDGKLYVFGGIGKTNSE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  223 W-------VEVFNVETNTWENVPSVlSPYGRSKApfnVHFVLDN-KIYILDGNNRVAYDlrgRRWEDWGPAGNQlgyfwq 294
Cdd:PRK14131 100 GspqvfddVYKYDPKTNSWQKLDTR-SPVGLAGH---VAVSLHNgKAYITGGVNKNIFD---GYFEDLAAAGKD------ 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227579  295 vlycvvDNLLYAVVPDHLHVTP--------IVVYDPREMGWRPVMGVDYLPNlvySESRMTNFGGKLMILG 357
Cdd:PRK14131 167 ------KTPKDKINDAYFDKKPedyffnkeVLSYDPSTNQWKNAGESPFLGT---AGSAVVIKGNKLWLIN 228
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
149-195 3.58e-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: 3.58e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15227579   149 MFPGCTTVTIGHKIYVMGGLRSlNRRAKTVFVIDCRFHTWRYLQEMQ 195
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDG-NQSLNSVEVYDPETNTWSKLPSMP 46
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
137-230 4.76e-08

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 54.01  E-value: 4.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579 137 SLQLSLVTSLPPMFPGCTTVTIGHKIYVMGGLRSLNrraKTVFVIDCRFHTWRYLQEMQVARSYAASAVIDGMIYVVGGS 216
Cdd:COG3055 184 SNTWTTLAPLPTARAGHAAAVLGGKILVFGGESGFS---DEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIGGE 260
                        90
                ....*....|....
gi 15227579 217 TKRSDDWVEVFNVE 230
Cdd:COG3055 261 TKPGVRTPLVTSAE 274
PHA03098 PHA03098
kelch-like protein; Provisional
137-243 1.86e-07

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 53.23  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  137 SLQLSLVTSLP-PMFPGCTTVTIGhKIYVMGGLRSLNR--RAKTVFVIDCRFHTWRYLQEMQVARSYAASAVIDGMIYVV 213
Cdd:PHA03098 415 TNKWSKGSPLPiSHYGGCAIYHDG-KIYVIGGISYIDNikVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVV 493
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15227579  214 GG-STKRSDDWVEVFNVETNTWE---NVPSVLSP 243
Cdd:PHA03098 494 GGdKYEYYINEIEVYDDKTNTWTlfcKFPKVIGS 527
PHA03098 PHA03098
kelch-like protein; Provisional
102-359 3.65e-07

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 52.08  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  102 SLIGSTEPVLYTLITFTSPNFEEPRWFILQRRNntslqlslvtslppmFPGC-TTVTIGHKIYVMGGLRSLNRRAKTVFV 180
Cdd:PHA03098 251 SIIYIHITMSIFTYNYITNYSPLSEINTIIDIH---------------YVYCfGSVVLNNVIYFIGGMNKNNLSVNSVVS 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  181 IDCRFHTWRYLQEMQVARSYAASAVIDGMIYVVGG-----STKRSDDWvevfNVETNTWENVPSVLSP-YGRSKAPfnvh 254
Cdd:PHA03098 316 YDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGiynsiSLNTVESW----KPGESKWREEPPLIFPrYNPCVVN---- 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  255 fvLDNKIYILDG--------NNRVAYDLRGRRWEdwgpAGNQLGYFWQVLYCVV-DNLLYAV----VPDHLHVTPIV-VY 320
Cdd:PHA03098 388 --VNNLIYVIGGiskndellKTVECFSLNTNKWS----KGSPLPISHYGGCAIYhDGKIYVIggisYIDNIKVYNIVeSY 461
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 15227579  321 DPREMGWRpvmgVDYLPNLVYSESRMTNFGGKLMILGCY 359
Cdd:PHA03098 462 NPVTNKWT----ELSSLNFPRINASLCIFNNKIYVVGGD 496
Kelch smart00612
Kelch domain;
161-208 4.63e-07

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 46.01  E-value: 4.63e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 15227579    161 KIYVMGGLRSlNRRAKTVFVIDCRFHTWRYLQEMQVARSYAASAVIDG 208
Cdd:smart00612   1 KIYVVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
59-101 6.19e-07

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: 45.64  E-value: 6.19e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15227579  59 PQMPLELIVSTIATLRRCHYPTLSLLSDSFRQVISSVDLFQTR 101
Cdd:cd22152   3 PGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
Kelch_6 pfam13964
Kelch motif;
197-239 8.11e-06

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 42.71  E-value: 8.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15227579   197 ARSYAASAVIDGMIYVVGGSTKRSD--DWVEVFNVETNTWENVPS 239
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNASPalNKLEVYNPLTKSWEELPP 45
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
198-240 9.38e-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: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 42.32  E-value: 9.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 15227579   198 RSYAASAVIDGMIYVVGGSTKRSDDW---VEVFNVETNTWENVPSV 240
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGSDGLGDLSssdVLVYDPETNVWTEVPRL 47
Kelch_6 pfam13964
Kelch motif;
152-198 4.27e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 40.78  E-value: 4.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15227579   152 GCTTVTIGHKIYVMGGLRSLNRRAKTVFVIDCRFHTWRYLQEMQVAR 198
Cdd:pfam13964   4 FHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPLPTPR 50
PHA02713 PHA02713
hypothetical protein; Provisional
134-266 5.15e-05

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 45.39  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  134 NNTSLQLSLVTSLPPMFPGCTTVTIGHKIYVMGGLRSLNRRAKTVFVIDCRFHTWRYLQEMQVARSYAASAVIDGMIYVV 213
Cdd:PHA02713 278 NINTMEYSVISTIPNHIINYASAIVDNEIIIAGGYNFNNPSLNKVYKINIENKIHVELPPMIKNRCRFSLAVIDDTIYAI 357
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15227579  214 GGSTKRS-DDWVEVFNVETNTWE---NVPSVLSPYGRSkapfnvhfVLDNKIYILDG 266
Cdd:PHA02713 358 GGQNGTNvERTIECYTMGDDKWKmlpDMPIALSSYGMC--------VLDQYIYIIGG 406
PHA02790 PHA02790
Kelch-like protein; Provisional
149-268 2.37e-04

Kelch-like protein; Provisional


Pssm-ID: 165153 [Multi-domain]  Cd Length: 480  Bit Score: 43.11  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  149 MFPGCTTVTIGHKIYVMGGLRSlNRRAKTVFVIDCRFHTWRYLQEMQVARSYAASAVIDGMIYVVGGSTKRSDdwVEVFN 228
Cdd:PHA02790 261 IFHMCTSTHVGEVVYLIGGWMN-NEIHNNAIAVNYISNNWIPIPPMNSPRLYASGVPANNKLYVVGGLPNPTS--VERWF 337
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15227579  229 VETNTWENVPSVLSPYGRSKAPfnvhfVLDNKIYILDGNN 268
Cdd:PHA02790 338 HGDAAWVNMPSLLKPRCNPAVA-----SINNVIYVIGGHS 372
Kelch smart00612
Kelch domain;
210-249 2.77e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 38.31  E-value: 2.77e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 15227579    210 IYVVGG-STKRSDDWVEVFNVETNTWENVPSVlsPYGRSKA 249
Cdd:smart00612   2 IYVVGGfDGGQRLKSVEVYDPETNKWTPLPSM--PTPRSGH 40
Kelch_4 pfam13418
Galactose oxidase, central domain;
197-240 2.94e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 38.36  E-value: 2.94e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15227579   197 ARSYAASAVI-DGMIYVVGG---STKRSDDwVEVFNVETNTWENVPSV 240
Cdd:pfam13418   1 PRAYHTSTSIpDDTIYLFGGegeDGTLLSD-LWVFDLSTNEWTRLGSL 47
PLN02153 PLN02153
epithiospecifier protein
152-238 5.89e-04

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 41.51  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  152 GCTTVTIGHKIYVMGGlRSLNRRAKTVFVIDCRFHTWRYLQEMQV-----ARSYAASAVIDGMIYVVGGSTK-------- 218
Cdd:PLN02153  78 GVRMVAVGTKLYIFGG-RDEKREFSDFYSYDTVKNEWTFLTKLDEeggpeARTFHSMASDENHVYVFGGVSKgglmktpe 156
                         90       100
                 ....*....|....*....|..
gi 15227579  219 --RSddwVEVFNVETNTWENVP 238
Cdd:PLN02153 157 rfRT---IEAYNIADGKWVQLP 175
Kelch_3 pfam13415
Galactose oxidase, central domain;
207-243 8.10e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 34.19  E-value: 8.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 15227579   207 DGMIYVVGG----STKRSDDwVEVFNVETNTWENVPSVLSP 243
Cdd:pfam13415   1 GDKLYIFGGlgfdGQTRLND-LYVYDLDTNTWTQIGDLPPP 40
PHA02713 PHA02713
hypothetical protein; Provisional
121-242 9.05e-03

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 38.07  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227579  121 NFEEPRwfiLQRRNNTSLQLSLVTSLPPMFPG-C--TTVTIGHKIYVMGGLRSLNRRaKTVFVIDCRFHTWRYLQEMQVA 197
Cdd:PHA02713 313 NFNNPS---LNKVYKINIENKIHVELPPMIKNrCrfSLAVIDDTIYAIGGQNGTNVE-RTIECYTMGDDKWKMLPDMPIA 388
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227579  198 RSYAASAVIDGMIYVVGGSTKRSD-------------------DWVEVFNVETNTWENVPSVLS 242
Cdd:PHA02713 389 LSSYGMCVLDQYIYIIGGRTEHIDytsvhhmnsidmeedthssNKVIRYDTVNNIWETLPNFWT 452
 
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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