NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15235144|ref|NP_195667|]
View 

Galactose oxidase/kelch repeat superfamily protein [Arabidopsis thaliana]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 32-75 5.41e-16

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: 71.45  E-value: 5.41e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15235144  32 IPSLPDDLLVSIFARVSRLYYPILSLVSKSFRSLLRSPELYETR 75
Cdd:cd22152   2 IPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
NanM super family cl34543
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
132-269 6.63e-11

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


The actual alignment was detected with superfamily member COG3055:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 62.48  E-value: 6.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 132 PVPNPPLEHWSGH-ASVGSDIYFFGGYMEENVrSSRVVILDCRSHTLREAPSLQM-ERSDPAASVIDGKIYVAGGVDGDD 209
Cdd:COG3055   5 SLPDLPTPRSEAAaALLDGKVYVAGGLSGGSA-SNSFEVYDPATNTWSELAPLPGpPRHHAAAVAQDGKLYVFGGFTGAN 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 210 ADSLYP--IEVFDIKTQIW-DHRPIPYWEKDWGALSrsayVDGKFYLTIGM-------KVMAYDLEESRW 269
Cdd:COG3055  84 PSSTPLndVYVYDPATNTWtKLAPMPTPRGGATALL----LDGKIYVVGGWddggnvaWVEVYDPATGTW 149
 
Name Accession Description Interval E-value
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 32-75 5.41e-16

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: 71.45  E-value: 5.41e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15235144  32 IPSLPDDLLVSIFARVSRLYYPILSLVSKSFRSLLRSPELYETR 75
Cdd:cd22152   2 IPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
132-269 6.63e-11

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 62.48  E-value: 6.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 132 PVPNPPLEHWSGH-ASVGSDIYFFGGYMEENVrSSRVVILDCRSHTLREAPSLQM-ERSDPAASVIDGKIYVAGGVDGDD 209
Cdd:COG3055   5 SLPDLPTPRSEAAaALLDGKVYVAGGLSGGSA-SNSFEVYDPATNTWSELAPLPGpPRHHAAAVAQDGKLYVFGGFTGAN 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 210 ADSLYP--IEVFDIKTQIW-DHRPIPYWEKDWGALSrsayVDGKFYLTIGM-------KVMAYDLEESRW 269
Cdd:COG3055  84 PSSTPLndVYVYDPATNTWtKLAPMPTPRGGATALL----LDGKIYVVGGWddggnvaWVEVYDPATGTW 149
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 32-74 2.36e-08

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


Pssm-ID: 425796  Cd Length: 43  Bit Score: 49.46  E-value: 2.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15235144    32 IPSLPDDLLVSIFARVSRLYYPILSLVSKSFRSLLRSPELYET 74
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
PHA03098 PHA03098
kelch-like protein; Provisional
 151-328 3.05e-08

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 55.54  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144  151 IYFFGGyMEENVRSSRVVILDCRSHTLREAPSLQMERSDPAASVIDGKIYVAGGVDGDDaDSLYPIEVFDIKTQIWD-HR 229
Cdd:PHA03098 345 IYVIGG-IYNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNVNNLIYVIGGISKND-ELLKTVECFSLNTNKWSkGS 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144  230 PIPYWEKDWGAlsrsAYVDGKFYLTIGMK----------VMAYDLEESRWdFAGYQMGQSWFWSCNCVIENVLYCYGDAF 299
Cdd:PHA03098 423 PLPISHYGGCA----IYHDGKIYVIGGISyidnikvyniVESYNPVTNKW-TELSSLNFPRINASLCIFNNKIYVVGGDK 497

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15235144  300 RW--------FDTKLRLWKVmkVKGLPKLSRNVDVKI 328
Cdd:PHA03098 498 YEyyineievYDDKTNTWTL--FCKFPKVIGSLEKNI 532
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 187-226 3.45e-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: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 43.75  E-value: 3.45e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 15235144   187 RSDPAASVIDGKIYVAGGVDGDdaDSLYPIEVFDIKTQIW 226
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFDGN--QSLNSVEVYDPETNTW 39
FBOX smart00256
A Receptor for Ubiquitination Targets;
35-75 1.49e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 41.65  E-value: 1.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 15235144     35 LPDDLLVSIFARVSRLYYPILSLVSKSFRSLLRSPELYETR 75
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
Kelch smart00612
Kelch domain;
151-197 3.31e-03

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 35.23  E-value: 3.31e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 15235144    151 IYFFGGYMEeNVRSSRVVILDCRSHTLREAPSLQMERSDPAASVIDG 197
Cdd:smart00612   2 IYVVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
 
Name Accession Description Interval E-value
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
 32-75 5.41e-16

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: 71.45  E-value: 5.41e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15235144  32 IPSLPDDLLVSIFARVSRLYYPILSLVSKSFRSLLRSPELYETR 75
Cdd:cd22152   2 IPGLPDDIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
132-269 6.63e-11

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 62.48  E-value: 6.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 132 PVPNPPLEHWSGH-ASVGSDIYFFGGYMEENVrSSRVVILDCRSHTLREAPSLQM-ERSDPAASVIDGKIYVAGGVDGDD 209
Cdd:COG3055   5 SLPDLPTPRSEAAaALLDGKVYVAGGLSGGSA-SNSFEVYDPATNTWSELAPLPGpPRHHAAAVAQDGKLYVFGGFTGAN 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 210 ADSLYP--IEVFDIKTQIW-DHRPIPYWEKDWGALSrsayVDGKFYLTIGM-------KVMAYDLEESRW 269
Cdd:COG3055  84 PSSTPLndVYVYDPATNTWtKLAPMPTPRGGATALL----LDGKIYVVGGWddggnvaWVEVYDPATGTW 149
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 32-74 2.36e-08

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


Pssm-ID: 425796  Cd Length: 43  Bit Score: 49.46  E-value: 2.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15235144    32 IPSLPDDLLVSIFARVSRLYYPILSLVSKSFRSLLRSPELYET 74
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
PHA03098 PHA03098
kelch-like protein; Provisional
 151-328 3.05e-08

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 55.54  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144  151 IYFFGGyMEENVRSSRVVILDCRSHTLREAPSLQMERSDPAASVIDGKIYVAGGVDGDDaDSLYPIEVFDIKTQIWD-HR 229
Cdd:PHA03098 345 IYVIGG-IYNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNVNNLIYVIGGISKND-ELLKTVECFSLNTNKWSkGS 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144  230 PIPYWEKDWGAlsrsAYVDGKFYLTIGMK----------VMAYDLEESRWdFAGYQMGQSWFWSCNCVIENVLYCYGDAF 299
Cdd:PHA03098 423 PLPISHYGGCA----IYHDGKIYVIGGISyidnikvyniVESYNPVTNKW-TELSSLNFPRINASLCIFNNKIYVVGGDK 497

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15235144  300 RW--------FDTKLRLWKVmkVKGLPKLSRNVDVKI 328
Cdd:PHA03098 498 YEyyineievYDDKTNTWTL--FCKFPKVIGSLEKNI 532
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
132-269 2.66e-07

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 51.70  E-value: 2.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 132 PVPNPPLEHWSGHASVGSD-IYFFGGYMEENVRSSrVVILDCRSHTLREAPSLQMERSDPAASVI-DGKIYVAGGVDGDD 209
Cdd:COG3055 104 KLAPMPTPRGGATALLLDGkIYVVGGWDDGGNVAW-VEVYDPATGTWTQLAPLPTPRDHLAAAVLpDGKILVIGGRNGSG 182

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15235144 210 AdslypievfdikTQIWDHRPiPYWEKDWGAlsRSAYVDGKFYLTIGM-----KVMAYDLEESRW 269
Cdd:COG3055 183 F------------SNTWTTLA-PLPTARAGH--AAAVLGGKILVFGGEsgfsdEVEAYDPATNTW 232
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
176-269 4.51e-07

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 50.92  E-value: 4.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 176 TLREAPSLQMERSDPAASVIDGKIYVAGGVDGDDADSlyPIEVFDIKTQIWdhRPIPywekDWGALSRS----AYVDGKF 251
Cdd:COG3055   2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASN--SFEVYDPATNTW--SELA----PLPGPPRHhaaaVAQDGKL 73

                        90       100
                ....*....|....*....|....*....
gi 15235144 252 YLTIGM-----------KVMAYDLEESRW 269
Cdd:COG3055  74 YVFGGFtganpsstplnDVYVYDPATNTW 102
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 187-226 3.45e-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: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 43.75  E-value: 3.45e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 15235144   187 RSDPAASVIDGKIYVAGGVDGDdaDSLYPIEVFDIKTQIW 226
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFDGN--QSLNSVEVYDPETNTW 39
F-box_ScMDM30-like cd22143
F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology ...
 31-72 5.19e-06

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


Pssm-ID: 438915  Cd Length: 44  Bit Score: 42.98  E-value: 5.19e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15235144  31 PIPSLPDDLLVSIFARVSRLYYPILSLVSKSFRSLLrSPELY 72
Cdd:cd22143   1 AFDSLPDEILSIIFSHLPQSDLYNLLFVNKHFYSLA-LPELW 41
FBOX smart00256
A Receptor for Ubiquitination Targets;
35-75 1.49e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 41.65  E-value: 1.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 15235144     35 LPDDLLVSIFARVSRLYYPILSLVSKSFRSLLRSPELYETR 75
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
132-220 2.32e-05

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 45.53  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235144 132 PVPNPPLEHWSGHASVGSD-IYFFGGymeENVRSSRVVILDCRSHTLREAPSLQMERSDPAASVIDGKIYVAGG--VDGD 208
Cdd:COG3055 189 TLAPLPTARAGHAAAVLGGkILVFGG---ESGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIGGetKPGV 265

                        90
                ....*....|..
gi 15235144 209 DADSLYPIEVFD 220
Cdd:COG3055 266 RTPLVTSAEVYD 277
F-box_AtFBW1-like cd22157
F-box domain found in Arabidopsis thaliana F-box/WD-40 repeat-containing protein 1 (AtFBW1) ...
 33-70 1.13e-03

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: 36.29  E-value: 1.13e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15235144  33 PSLPDDLLVSIFARVsrlyyPILSL-----VSKSFRSLLRSPE 70
Cdd:cd22157   1 SSLPDDLVEEILSRL-----PAKSLlrfrcVCKQWNSLISSPS 38
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 187-227 1.77e-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: 36.16  E-value: 1.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 15235144   187 RSDPAASVIDGKIYVAGGVDGDDADSLYPIEVFDIKTQIWD 227
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGSDGLGDLSSSDVLVYDPETNVWT 42
Kelch_6 pfam13964
Kelch motif;
145-184 2.41e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 35.77  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 15235144   145 ASVGSDIYFFGGYMEENVRSSRVVILDCRSHTLREAPSLQ 184
Cdd:pfam13964   8 VSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPLP 47
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 32-72 2.91e-03

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 35.15  E-value: 2.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15235144    32 IPSLPDDLLVSIFARVSR--LYypILSLVSKSFRSLLRSPELY 72
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPkdLL--RLALVCRRWRELASDDSLW 41
Kelch smart00612
Kelch domain;
151-197 3.31e-03

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 35.23  E-value: 3.31e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 15235144    151 IYFFGGYMEeNVRSSRVVILDCRSHTLREAPSLQMERSDPAASVIDG 197
Cdd:smart00612   2 IYVVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH