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Conserved domains on  [gi|1002302799|ref|XP_015614781|]
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F-box/kelch-repeat protein At1g55270 [Oryza sativa Japonica Group]

Protein Classification

F-box/kelch-repeat protein( domain architecture ID 17778807)

F-box/kelch-repeat protein functions as the substrate-recognition component of an SCF (Skp1-Cullin-F-box protein) ubiquitin-protein ligase that is involved in ubiquitin-dependent degradation

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];
159-379 2.36e-23

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 159 WKSLPPVPaeysEALGFGCAVLSGCYLYLFGGKDPLRGSmRRVVFYNARTNKWHRAPDM-LRKRHFFGSCVINNCLYVAG 237
Cdd:COG3055     3 WSSLPDLP----TPRSEAAAALLDGKVYVAGGLSGGSAS-NSFEVYDPATNTWSELAPLpGPPRHHAAAVAQDGKLYVFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 238 G--ECEGIQRTLPSAEVYDPNRNRWACVAEMNNGMVPFIGVVYDGKWFLKG--LDSHRQVTSEVYLPSSNLWSTI----- 308
Cdd:COG3055    78 GftGANPSSTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGgwDDGGNVAWVEVYDPATGTWTQLaplpt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 309 -----------DDEM-VTGWRN---------------------PSITFNGKLYSSDCRDG--CKLRVYDPNTGTWakfmD 353
Cdd:COG3055   158 prdhlaaavlpDGKIlVIGGRNgsgfsntwttlaplptaraghAAAVLGGKILVFGGESGfsDEVEAYDPATNTW----T 233
                         250       260
                  ....*....|....*....|....*.
gi 1002302799 354 SKHHLGSSRAFEAAalVTLNGKLCIV 379
Cdd:COG3055   234 ALGELPTPRHGHAA--VLTDGKVYVI 257
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
82-126 4.59e-14

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: 66.05  E-value: 4.59e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002302799  82 LLPGLPDDLAIACLIRVPRVEHPNLRIVCKRWNRLLSGNYYYSLR 126
Cdd:cd22152     1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
159-379 2.36e-23

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 159 WKSLPPVPaeysEALGFGCAVLSGCYLYLFGGKDPLRGSmRRVVFYNARTNKWHRAPDM-LRKRHFFGSCVINNCLYVAG 237
Cdd:COG3055     3 WSSLPDLP----TPRSEAAAALLDGKVYVAGGLSGGSAS-NSFEVYDPATNTWSELAPLpGPPRHHAAAVAQDGKLYVFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 238 G--ECEGIQRTLPSAEVYDPNRNRWACVAEMNNGMVPFIGVVYDGKWFLKG--LDSHRQVTSEVYLPSSNLWSTI----- 308
Cdd:COG3055    78 GftGANPSSTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGgwDDGGNVAWVEVYDPATGTWTQLaplpt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 309 -----------DDEM-VTGWRN---------------------PSITFNGKLYSSDCRDG--CKLRVYDPNTGTWakfmD 353
Cdd:COG3055   158 prdhlaaavlpDGKIlVIGGRNgsgfsntwttlaplptaraghAAAVLGGKILVFGGESGfsDEVEAYDPATNTW----T 233
                         250       260
                  ....*....|....*....|....*.
gi 1002302799 354 SKHHLGSSRAFEAAalVTLNGKLCIV 379
Cdd:COG3055   234 ALGELPTPRHGHAA--VLTDGKVYVI 257
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
82-126 4.59e-14

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: 66.05  E-value: 4.59e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002302799  82 LLPGLPDDLAIACLIRVPRVEHPNLRIVCKRWNRLLSGNYYYSLR 126
Cdd:cd22152     1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
PHA03098 PHA03098
kelch-like protein; Provisional
175-348 9.06e-14

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 73.26  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 175 FGCAVLSGCyLYLFGGKDPLRGSMRRVVFYNARTNKWHRAPDMLRKRHFFGSCVINNCLYVAGGECEGIqrTLPSAEVYD 254
Cdd:PHA03098  288 FGSVVLNNV-IYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSI--SLNTVESWK 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 255 PNRNRW------------ACVAeMNNGMVPFIGVVYDGKWFLKgldshrqvTSEVYLPSSNLWSTIDDEMVTGWRNPSIT 322
Cdd:PHA03098  365 PGESKWreepplifprynPCVV-NVNNLIYVIGGISKNDELLK--------TVECFSLNTNKWSKGSPLPISHYGGCAIY 435
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1002302799 323 FNGKLY-------SSDCRDGCKLRVYDPNTGTW 348
Cdd:PHA03098  436 HDGKIYviggisyIDNIKVYNIVESYNPVTNKW 468
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
221-267 7.15e-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: 48.38  E-value: 7.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002302799 221 RHFFGSCVINNCLYVAGGECEgiQRTLPSAEVYDPNRNRWACVAEMN 267
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFDG--NQSLNSVEVYDPETNTWSKLPSMP 46
Kelch smart00612
Kelch domain;
185-231 5.36e-06

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 43.32  E-value: 5.36e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1002302799  185 LYLFGGKDPlRGSMRRVVFYNARTNKWHRAPDMLRKRHFFGSCVINN 231
Cdd:smart00612   2 IYVVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
83-118 1.65e-04

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: 39.06  E-value: 1.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002302799  83 LPGLPDDLAIACLIRVPRVEHPNLRIVCKRWNRLLS 118
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVD 36
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
159-379 2.36e-23

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 159 WKSLPPVPaeysEALGFGCAVLSGCYLYLFGGKDPLRGSmRRVVFYNARTNKWHRAPDM-LRKRHFFGSCVINNCLYVAG 237
Cdd:COG3055     3 WSSLPDLP----TPRSEAAAALLDGKVYVAGGLSGGSAS-NSFEVYDPATNTWSELAPLpGPPRHHAAAVAQDGKLYVFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 238 G--ECEGIQRTLPSAEVYDPNRNRWACVAEMNNGMVPFIGVVYDGKWFLKG--LDSHRQVTSEVYLPSSNLWSTI----- 308
Cdd:COG3055    78 GftGANPSSTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGgwDDGGNVAWVEVYDPATGTWTQLaplpt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 309 -----------DDEM-VTGWRN---------------------PSITFNGKLYSSDCRDG--CKLRVYDPNTGTWakfmD 353
Cdd:COG3055   158 prdhlaaavlpDGKIlVIGGRNgsgfsntwttlaplptaraghAAAVLGGKILVFGGESGfsDEVEAYDPATNTW----T 233
                         250       260
                  ....*....|....*....|....*.
gi 1002302799 354 SKHHLGSSRAFEAAalVTLNGKLCIV 379
Cdd:COG3055   234 ALGELPTPRHGHAA--VLTDGKVYVI 257
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
136-284 6.32e-16

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 77.50  E-value: 6.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 136 VYVFK-RDREGKISWH-AFDPLHQLWKSLPPVPAEYSealGFGCAVLSGCYLYLFGGKDplrgsmrrvvfYNARTNKWHR 213
Cdd:COG3055   124 IYVVGgWDDGGNVAWVeVYDPATGTWTQLAPLPTPRD---HLAAAVLPDGKILVIGGRN-----------GSGFSNTWTT 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002302799 214 APDMLRKRHFFGSCVINNCLYVAGGEcegiQRTLPSAEVYDPNRNRWACVAEMNNGMVPFIGVVYDGKWFL 284
Cdd:COG3055   190 LAPLPTARAGHAAAVLGGKILVFGGE----SGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYV 256
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
82-126 4.59e-14

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: 66.05  E-value: 4.59e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002302799  82 LLPGLPDDLAIACLIRVPRVEHPNLRIVCKRWNRLLSGNYYYSLR 126
Cdd:cd22152     1 LIPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
PHA03098 PHA03098
kelch-like protein; Provisional
175-348 9.06e-14

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 73.26  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 175 FGCAVLSGCyLYLFGGKDPLRGSMRRVVFYNARTNKWHRAPDMLRKRHFFGSCVINNCLYVAGGECEGIqrTLPSAEVYD 254
Cdd:PHA03098  288 FGSVVLNNV-IYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSI--SLNTVESWK 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 255 PNRNRW------------ACVAeMNNGMVPFIGVVYDGKWFLKgldshrqvTSEVYLPSSNLWSTIDDEMVTGWRNPSIT 322
Cdd:PHA03098  365 PGESKWreepplifprynPCVV-NVNNLIYVIGGISKNDELLK--------TVECFSLNTNKWSKGSPLPISHYGGCAIY 435
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1002302799 323 FNGKLY-------SSDCRDGCKLRVYDPNTGTW 348
Cdd:PHA03098  436 HDGKIYviggisyIDNIKVYNIVESYNPVTNKW 468
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
159-254 6.15e-09

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 56.70  E-value: 6.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 159 WKSLPPVPaeySEALGFGCAVLSGcYLYLFGGKDplrGSMRRVVFYNARTNKWHRAPDMLRKRHFFGSCVINNCLYVAGG 238
Cdd:COG3055   187 WTTLAPLP---TARAGHAAAVLGG-KILVFGGES---GFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIGG 259
                          90
                  ....*....|....*...
gi 1002302799 239 ECEGIQRT--LPSAEVYD 254
Cdd:COG3055   260 ETKPGVRTplVTSAEVYD 277
PHA03098 PHA03098
kelch-like protein; Provisional
152-275 2.60e-08

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 55.93  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 152 FDPLHQLWKSLPPVPaeYSeaLGFGCAVLSGCYLYLFGG----KDPLRGSMrrVVFYNARTNKWHRAPDMLRKRHFFGSC 227
Cdd:PHA03098  411 FSLNTNKWSKGSPLP--IS--HYGGCAIYHDGKIYVIGGisyiDNIKVYNI--VESYNPVTNKWTELSSLNFPRINASLC 484
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1002302799 228 VINNCLYVAGGECegIQRTLPSAEVYDPNRNRWacvaEMNNGMVPFIG 275
Cdd:PHA03098  485 IFNNKIYVVGGDK--YEYYINEIEVYDDKTNTW----TLFCKFPKVIG 526
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
221-267 7.15e-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: 48.38  E-value: 7.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002302799 221 RHFFGSCVINNCLYVAGGECEgiQRTLPSAEVYDPNRNRWACVAEMN 267
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFDG--NQSLNSVEVYDPETNTWSKLPSMP 46
Kelch smart00612
Kelch domain;
185-231 5.36e-06

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 43.32  E-value: 5.36e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1002302799  185 LYLFGGKDPlRGSMRRVVFYNARTNKWHRAPDMLRKRHFFGSCVINN 231
Cdd:smart00612   2 IYVVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
PHA03098 PHA03098
kelch-like protein; Provisional
191-364 6.35e-05

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 45.14  E-value: 6.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 191 KDPLRGSMRRVVFYNARTNKWhrapDMLRKRHF---FGSCVINNCLYVAGGEcegIQRTLPSAEV--YDPNRNRWACVAE 265
Cdd:PHA03098  256 HITMSIFTYNYITNYSPLSEI----NTIIDIHYvycFGSVVLNNVIYFIGGM---NKNNLSVNSVvsYDTKTKSWNKVPE 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 266 MNNGMVPFIGVVYDGKWFLKG--LDSHRQVTSEVYLPSSNLWsTIDDEMVTGWRNPSITF-NGKLY-----SSDCRDGCK 337
Cdd:PHA03098  329 LIYPRKNPGVTVFNNRIYVIGgiYNSISLNTVESWKPGESKW-REEPPLIFPRYNPCVVNvNNLIYviggiSKNDELLKT 407
                         170       180
                  ....*....|....*....|....*...
gi 1002302799 338 LRVYDPNTGTWAKFMDSK-HHLGSSRAF 364
Cdd:PHA03098  408 VECFSLNTNKWSKGSPLPiSHYGGCAIY 435
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
83-118 1.65e-04

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: 39.06  E-value: 1.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002302799  83 LPGLPDDLAIACLIRVPRVEHPNLRIVCKRWNRLLS 118
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVD 36
Kelch_6 pfam13964
Kelch motif;
175-221 2.15e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.86  E-value: 2.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002302799 175 FGCAVLSGCYLYLFGGKDPLRGSMRRVVFYNARTNKWHRAPDMLRKR 221
Cdd:pfam13964   4 FHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPLPTPR 50
F-box_AtFBW1-like cd22157
F-box domain found in Arabidopsis thaliana F-box/WD-40 repeat-containing protein 1 (AtFBW1) ...
84-118 4.54e-04

F-box domain found in Arabidopsis thaliana F-box/WD-40 repeat-containing protein 1 (AtFBW1) and similar proteins; AtFBW1, also called WD-40-associated F-box protein 1, is an F-box protein that contains four WD-40 repeats, which are separated from each other by a spacer region. Like other F-box proteins, AtFBW1 may be a component of SCF (Skp1 Cdc53 F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. This subfamily also contains many F-box only proteins that do not have any WD repeat. 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: 438928  Cd Length: 39  Bit Score: 37.44  E-value: 4.54e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1002302799  84 PGLPDDLAIACLIRVPRVEHPNLRIVCKRWNRLLS 118
Cdd:cd22157     1 SSLPDDLVEEILSRLPAKSLLRFRCVCKQWNSLIS 35
Kelch smart00612
Kelch domain;
232-280 5.83e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 37.54  E-value: 5.83e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1002302799  232 CLYVAGGeCEGIQRtLPSAEVYDPNRNRWACVAEMNNGMVPFIGVVYDG 280
Cdd:smart00612   1 KIYVVGG-FDGGQR-LKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
Kelch_3 pfam13415
Galactose oxidase, central domain;
182-229 9.97e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 36.88  E-value: 9.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002302799 182 GCYLYLFGGKDPLRGSMRRVVF-YNARTNKWHRAPDMLRKRHFFGSCVI 229
Cdd:pfam13415   1 GDKLYIFGGLGFDGQTRLNDLYvYDLDTNTWTQIGDLPPPRSGHSATYI 49
PHA02790 PHA02790
Kelch-like protein; Provisional
159-312 4.51e-03

Kelch-like protein; Provisional


Pssm-ID: 165153 [Multi-domain]  Cd Length: 480  Bit Score: 39.26  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002302799 159 WKSLPPVPAEYSEALGfgcaVLSGCYLYLFGGKdPLRGSMRRvvFYNARTNkWHRAPDMLRKRHFFGSCVINNCLYVAGG 238
Cdd:PHA02790  299 WIPIPPMNSPRLYASG----VPANNKLYVVGGL-PNPTSVER--WFHGDAA-WVNMPSLLKPRCNPAVASINNVIYVIGG 370
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002302799 239 ECEgiqrTLPSAEVYDPNRNRWACVAEMNNGMVPFIGVVYDGKWFLKGLDshrqvtSEVYLPSSNLWSTIDDEM 312
Cdd:PHA02790  371 HSE----TDTTTEYLLPNHDQWQFGPSTYYPHYKSCALVFGRRLFLVGRN------AEFYCESSNTWTLIDDPI 434
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
174-217 5.14e-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: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 34.90  E-value: 5.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002302799 174 GFGCAVLSGCyLYLFGGKDPLRgSMRRVVFYNARTNKWHRAPDM 217
Cdd:pfam01344   4 GAGVVVVGGK-IYVIGGFDGNQ-SLNSVEVYDPETNTWSKLPSM 45
Kelch_6 pfam13964
Kelch motif;
221-269 9.28e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 34.23  E-value: 9.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002302799 221 RHFFGSCVINNCLYVAGGECEGIQRtLPSAEVYDPNRNRWACVAEMNNG 269
Cdd:pfam13964   2 RTFHSVVSVGGYIYVFGGYTNASPA-LNKLEVYNPLTKSWEELPPLPTP 49
 
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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