NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15223715|ref|NP_172885|]
View 

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
167-409 1.46e-26

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 107.93  E-value: 1.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 167 WMNLPTMPSGVTFMCAdkesLAVGTDLLVLGKDDYSSHV--IYRYSLLTNSWSSGMRMNSPRcLFGSASL---GEIAIFa 241
Cdd:COG3055   3 WSSLPDLPTPRSEAAA----ALLDGKVYVAGGLSGGSASnsFEVYDPATNTWSELAPLPGPP-RHHAAAVaqdGKLYVF- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 242 GGFDSF---GKISDSAEMYNSELQTWTTLPKMNKPRKMCSGVFMDGKFYVIGGIggNDSKVLTCGEEFDLETKKWTEIPE 318
Cdd:COG3055  77 GGFTGAnpsSTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGW--DDGGNVAWVEVYDPATGTWTQLAP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 319 MspPRSREMPAAA-----------------------EAPPL--------VAVVNNELYAAD-----HADMEVrkYDKESK 362
Cdd:COG3055 155 L--PTPRDHLAAAvlpdgkilviggrngsgfsntwtTLAPLptaraghaAAVLGGKILVFGgesgfSDEVEA--YDPATN 230

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15223715 363 KWFTLGRLPeradsVNGWGLAFRACGERLIVIGGpRSSGGGYIELNS 409
Cdd:COG3055 231 TWTALGELP-----TPRHGHAAVLTDGKVYVIGG-ETKPGVRTPLVT 271
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 93-138 1.39e-05

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: 42.17  E-value: 1.39e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15223715  93 SLINDIgrdnSISCLIRCSRSGYGSIASLNRSFRSLVKTGEIYRLR 138
Cdd:cd22152   4 GLPDDI----ALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
167-409 1.46e-26

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 107.93  E-value: 1.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 167 WMNLPTMPSGVTFMCAdkesLAVGTDLLVLGKDDYSSHV--IYRYSLLTNSWSSGMRMNSPRcLFGSASL---GEIAIFa 241
Cdd:COG3055   3 WSSLPDLPTPRSEAAA----ALLDGKVYVAGGLSGGSASnsFEVYDPATNTWSELAPLPGPP-RHHAAAVaqdGKLYVF- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 242 GGFDSF---GKISDSAEMYNSELQTWTTLPKMNKPRKMCSGVFMDGKFYVIGGIggNDSKVLTCGEEFDLETKKWTEIPE 318
Cdd:COG3055  77 GGFTGAnpsSTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGW--DDGGNVAWVEVYDPATGTWTQLAP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 319 MspPRSREMPAAA-----------------------EAPPL--------VAVVNNELYAAD-----HADMEVrkYDKESK 362
Cdd:COG3055 155 L--PTPRDHLAAAvlpdgkilviggrngsgfsntwtTLAPLptaraghaAAVLGGKILVFGgesgfSDEVEA--YDPATN 230

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15223715 363 KWFTLGRLPeradsVNGWGLAFRACGERLIVIGGpRSSGGGYIELNS 409
Cdd:COG3055 231 TWTALGELP-----TPRHGHAAVLTDGKVYVIGG-ETKPGVRTPLVT 271
PHA03098 PHA03098
kelch-like protein; Provisional
 190-371 2.02e-16

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 81.35  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715  190 GTDLLVLGKDDYSSHVIYRYSLLTNSWSSgMRMNSPRCLFGSASLGEIAIFAGGFDSFGKISDSAEMYNSELQTWTTLPK 269
Cdd:PHA03098 250 GSIIYIHITMSIFTYNYITNYSPLSEINT-IIDIHYVYCFGSVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPE 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715  270 MNKPRKMCSGVFMDGKFYVIGGIGgnDSKVLTCGEEFDLETKKWTEIPEMSPPRSRempaaaeapPLVAVVNNELYAA-- 347
Cdd:PHA03098 329 LIYPRKNPGVTVFNNRIYVIGGIY--NSISLNTVESWKPGESKWREEPPLIFPRYN---------PCVVNVNNLIYVIgg 397

                        170       180
                 ....*....|....*....|....*...
gi 15223715  348 ----DHADMEVRKYDKESKKWFTLGRLP 371
Cdd:PHA03098 398 isknDELLKTVECFSLNTNKWSKGSPLP 425
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 273-320 4.21e-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: 51.84  E-value: 4.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15223715   273 PRKMCSGVFMDGKFYVIGGIGGNDSkvLTCGEEFDLETKKWTEIPEMS 320
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQS--LNSVEVYDPETNTWSKLPSMP 46
Kelch smart00612
Kelch domain;
239-284 7.29e-07

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 45.63  E-value: 7.29e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 15223715    239 IFA-GGFDsFGKISDSAEMYNSELQTWTTLPKMNKPRKMCSGVFMDG 284
Cdd:smart00612   2 IYVvGGFD-GGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 93-138 1.39e-05

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: 42.17  E-value: 1.39e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15223715  93 SLINDIgrdnSISCLIRCSRSGYGSIASLNRSFRSLVKTGEIYRLR 138
Cdd:cd22152   4 GLPDDI----ALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
167-409 1.46e-26

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 107.93  E-value: 1.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 167 WMNLPTMPSGVTFMCAdkesLAVGTDLLVLGKDDYSSHV--IYRYSLLTNSWSSGMRMNSPRcLFGSASL---GEIAIFa 241
Cdd:COG3055   3 WSSLPDLPTPRSEAAA----ALLDGKVYVAGGLSGGSASnsFEVYDPATNTWSELAPLPGPP-RHHAAAVaqdGKLYVF- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 242 GGFDSF---GKISDSAEMYNSELQTWTTLPKMNKPRKMCSGVFMDGKFYVIGGIggNDSKVLTCGEEFDLETKKWTEIPE 318
Cdd:COG3055  77 GGFTGAnpsSTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGW--DDGGNVAWVEVYDPATGTWTQLAP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 319 MspPRSREMPAAA-----------------------EAPPL--------VAVVNNELYAAD-----HADMEVrkYDKESK 362
Cdd:COG3055 155 L--PTPRDHLAAAvlpdgkilviggrngsgfsntwtTLAPLptaraghaAAVLGGKILVFGgesgfSDEVEA--YDPATN 230

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15223715 363 KWFTLGRLPeradsVNGWGLAFRACGERLIVIGGpRSSGGGYIELNS 409
Cdd:COG3055 231 TWTALGELP-----TPRHGHAAVLTDGKVYVIGG-ETKPGVRTPLVT 271
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
159-347 6.21e-19

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 86.36  E-value: 6.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 159 AFNPFERRWMNLPTMPSGVtfmcADKESLAVGTDLLVLGKDDYSSHV--IYRYSLLTNSWSSGMRMNSPRCLFGSASL-- 234
Cdd:COG3055  94 VYDPATNTWTKLAPMPTPR----GGATALLLDGKIYVVGGWDDGGNVawVEVYDPATGTWTQLAPLPTPRDHLAAAVLpd 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 235 GEIaIFAGGFDSFGKIsdsaemynselQTWTTLPKMNKPRKMCSGVFMDGKFYVIGGIGGNDSKVltcgEEFDLETKKWT 314
Cdd:COG3055 170 GKI-LVIGGRNGSGFS-----------NTWTTLAPLPTARAGHAAAVLGGKILVFGGESGFSDEV----EAYDPATNTWT 233

                       170       180       190
                ....*....|....*....|....*....|...
gi 15223715 315 EIPEMspPRSREMPAAaeapplvAVVNNELYAA 347
Cdd:COG3055 234 ALGEL--PTPRHGHAA-------VLTDGKVYVI 257
PHA03098 PHA03098
kelch-like protein; Provisional
 190-371 2.02e-16

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 81.35  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715  190 GTDLLVLGKDDYSSHVIYRYSLLTNSWSSgMRMNSPRCLFGSASLGEIAIFAGGFDSFGKISDSAEMYNSELQTWTTLPK 269
Cdd:PHA03098 250 GSIIYIHITMSIFTYNYITNYSPLSEINT-IIDIHYVYCFGSVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPE 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715  270 MNKPRKMCSGVFMDGKFYVIGGIGgnDSKVLTCGEEFDLETKKWTEIPEMSPPRSRempaaaeapPLVAVVNNELYAA-- 347
Cdd:PHA03098 329 LIYPRKNPGVTVFNNRIYVIGGIY--NSISLNTVESWKPGESKWREEPPLIFPRYN---------PCVVNVNNLIYVIgg 397

                        170       180
                 ....*....|....*....|....*...
gi 15223715  348 ----DHADMEVRKYDKESKKWFTLGRLP 371
Cdd:PHA03098 398 isknDELLKTVECFSLNTNKWSKGSPLP 425
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
160-307 1.54e-15

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 76.35  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 160 FNPFERRWMNLPTMPSGVTFMCAdkeSLAVGTDLLVLGKDDYSSHviyrysllTNSWSSGMRMNSPRCLFGSASLGEIAI 239
Cdd:COG3055 142 YDPATGTWTQLAPLPTPRDHLAA---AVLPDGKILVIGGRNGSGF--------SNTWTTLAPLPTARAGHAAAVLGGKIL 210

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 240 FAGGFDSFgkiSDSAEMYNSELQTWTTLPKMNKPRKMCSGVFMDGKFYVIGGI--GGNDSKVLTCGEEFD 307
Cdd:COG3055 211 VFGGESGF---SDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIGGEtkPGVRTPLVTSAEVYD 277
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
263-425 3.28e-13

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 69.80  E-value: 3.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 263 TWTTLPKMNKPRKMCSGVFMDGKFYVIGGI-GGNDSKVLtcgEEFDLETKKWTEIPEMSPPRsREMPAAaeapplvAVVN 341
Cdd:COG3055   2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLsGGSASNSF---EVYDPATNTWSELAPLPGPP-RHHAAA-------VAQD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715 342 NELYAA-----------DHADMEVrkYDKESKKWFTLGRLPERADSvngwGLAFRACGeRLIVIGGPRSSGGgyielNSW 410
Cdd:COG3055  71 GKLYVFggftganpsstPLNDVYV--YDPATNTWTKLAPMPTPRGG----ATALLLDG-KIYVVGGWDDGGN-----VAW 138

                       170
                ....*....|....*
gi 15223715 411 IPSSDRSPPLWTLLG 425
Cdd:COG3055 139 VEVYDPATGTWTQLA 153
PHA03098 PHA03098
kelch-like protein; Provisional
 198-371 6.39e-11

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 64.02  E-value: 6.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715  198 KDDYSSHVIYRYSLLTNSWSSGMRMNSPRCLFGSASLGEIAIFAGGFDSFGKISDSAEMYNSELQTWTTLPKMNKPRKMC 277
Cdd:PHA03098 352 YNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPLPISHYGG 431

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715  278 SGVFMDGKFYVIGGIG-GNDSKVLTCGEEFDLETKKWTEIPEMSPPRSRempaaaeapPLVAVVNNELY--AADHADM-- 352
Cdd:PHA03098 432 CAIYHDGKIYVIGGISyIDNIKVYNIVESYNPVTNKWTELSSLNFPRIN---------ASLCIFNNKIYvvGGDKYEYyi 502

                        170       180
                 ....*....|....*....|
gi 15223715  353 -EVRKYDKESKKWFTLGRLP 371
Cdd:PHA03098 503 nEIEVYDDKTNTWTLFCKFP 522
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 273-320 4.21e-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: 51.84  E-value: 4.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15223715   273 PRKMCSGVFMDGKFYVIGGIGGNDSkvLTCGEEFDLETKKWTEIPEMS 320
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQS--LNSVEVYDPETNTWSKLPSMP 46
Kelch smart00612
Kelch domain;
239-284 7.29e-07

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 45.63  E-value: 7.29e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 15223715    239 IFA-GGFDsFGKISDSAEMYNSELQTWTTLPKMNKPRKMCSGVFMDG 284
Cdd:smart00612   2 IYVvGGFD-GGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
PHA02790 PHA02790
Kelch-like protein; Provisional
 231-345 7.53e-06

Kelch-like protein; Provisional


Pssm-ID: 165153 [Multi-domain]  Cd Length: 480  Bit Score: 48.12  E-value: 7.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715  231 SASLGEIAIFAGGFDSfGKISDSAEMYNSELQTWTTLPKMNKPRKMCSGVFMDGKFYVIGGIgGNDSKVltcgEEFDLET 310
Cdd:PHA02790 267 STHVGEVVYLIGGWMN-NEIHNNAIAVNYISNNWIPIPPMNSPRLYASGVPANNKLYVVGGL-PNPTSV----ERWFHGD 340

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15223715  311 KKWTEIPEMSPPRSRempaaaeapPLVAVVNNELY 345
Cdd:PHA02790 341 AAWVNMPSLLKPRCN---------PAVASINNVIY 366
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 93-138 1.39e-05

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: 42.17  E-value: 1.39e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15223715  93 SLINDIgrdnSISCLIRCSRSGYGSIASLNRSFRSLVKTGEIYRLR 138
Cdd:cd22152   4 GLPDDI----ALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
Kelch smart00612
Kelch domain;
287-325 2.20e-05

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 41.39  E-value: 2.20e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 15223715    287 YVIGGIGGNDSkvLTCGEEFDLETKKWTEIPEMSPPRSR 325
Cdd:smart00612   3 YVVGGFDGGQR--LKSVEVYDPETNKWTPLPSMPTPRSG 39
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 225-271 3.01e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 41.06  E-value: 3.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15223715   225 PRCLFGSASLGEIaIFA-GGFDSfGKISDSAEMYNSELQTWTTLPKMN 271
Cdd:pfam01344   1 RRSGAGVVVVGGK-IYViGGFDG-NQSLNSVEVYDPETNTWSKLPSMP 46
Kelch_6 pfam13964
Kelch motif;
273-323 3.45e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 41.17  E-value: 3.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15223715   273 PRKMCSGVFMDGKFYVIGGIGgNDSKVLTCGEEFDLETKKWTEIPEMSPPR 323
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYT-NASPALNKLEVYNPLTKSWEELPPLPTPR 50
Kelch_3 pfam13415
Galactose oxidase, central domain;
283-324 1.19e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 39.58  E-value: 1.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15223715   283 DGKFYVIGGIGGNDSKVLTCGEEFDLETKKWTEIPEMSPPRS 324
Cdd:pfam13415   1 GDKLYIFGGLGFDGQTRLNDLYVYDLDTNTWTQIGDLPPPRS 42
PHA03098 PHA03098
kelch-like protein; Provisional
 160-278 3.51e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 42.83  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223715  160 FNPFERRWMNLPTMPSGVTFMCADKEslavGTDLLVLGKDDYSSHV-----IYRYSLLTNSWSSGMRMNSPRclfGSASL 234
Cdd:PHA03098 411 FSLNTNKWSKGSPLPISHYGGCAIYH----DGKIYVIGGISYIDNIkvyniVESYNPVTNKWTELSSLNFPR---INASL 483

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15223715  235 GEI--AIFAGGFDSFGKISDSAEMYNSELQTWT---TLPKMNKPRKMCS 278
Cdd:PHA03098 484 CIFnnKIYVVGGDKYEYYINEIEVYDDKTNTWTlfcKFPKVIGSLEKNI 532
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 280-319 1.22e-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: 36.55  E-value: 1.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 15223715   280 VFMDGKFYVIGGIGGNDSKVLTCGEEFDLETKKWTEIPEM 319
Cdd:pfam07646   8 SVPGGKLYVVGGSDGLGDLSSSDVLVYDPETNVWTEVPRL 47
Kelch_6 pfam13964
Kelch motif;
225-274 1.70e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 36.16  E-value: 1.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15223715   225 PRCLFGSASLGE-IAIFaGGFDSFGKISDSAEMYNSELQTWTTLPKMNKPR 274
Cdd:pfam13964   1 PRTFHSVVSVGGyIYVF-GGYTNASPALNKLEVYNPLTKSWEELPPLPTPR 50
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH