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Conserved domains on  [gi|1775480896|pdb|6RYX|A]
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Chain A, Kelch domain-containing protein

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 589-689 1.34e-30

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


:

Pssm-ID: 199882  Cd Length: 103  Bit Score: 115.80  E-value: 1.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      589 GSRAARPVISAISADpIKAGATLTFTVEGVEGQGT-AALIRLGSVTHSVNSDQRRVPLNVTVSGNEYS--ATLPDDYGIL 665
Cdd:cd02851   1 GFGAPRPTITSAPKT-VGYGQTFTVTVSGPGGGIVrVTLVRPGFVTHSFNMGQRLVKLPVTGSGGDYTvtVTAPPNANVA 79

                        90       100
                ....*....|....*....|....
6RYX_A      666 LPGYYYLFVSTPQGTPSIAKTVHV 689
Cdd:cd02851  80 PPGYYMLFVVNADGVPSVAKWVRV 103
NanM super family cl34543
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
282-553 3.89e-17

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: 82.13  E-value: 3.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      282 DGRILIQGGSDADTVS----IYDPATNEFTRGPNMTLARGYQTSCTLSNGKVFTIGG---AWSGERVGKNGEVYDPVANA 354
Cdd:COG3055  22 DGKVYVAGGLSGGSASnsfeVYDPATNTWSELAPLPGPPRHHAAAVAQDGKLYVFGGftgANPSSTPLNDVYVYDPATNT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      355 WTYLPgadfrPMLTNdhegiwREDNHAWLFgwkNGSIFQAGpskdqhwyGIQGNGTVAKAatrDDDDAMCGVWvmydava 434
Cdd:COG3055 102 WTKLA-----PMPTP------RGGATALLL---DGKIYVVG--------GWDDGGNVAWV---EVYDPATGTW------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      435 gkifsaggspdytdspatqrahittigepntpaevERVADMGFPRGFANAVVLPDGQVLVTGGQRMSlVFTNT------- 507
Cdd:COG3055 150 -----------------------------------TQLAPLPTPRDHLAAAVLPDGKILVIGGRNGS-GFSNTwttlapl 193

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
6RYX_A      508 -------------DGILV----------AELFNPETREWKQMAPMAVPRnyHSVSILLPDATVFSGGGG 553
Cdd:COG3055 194 ptaraghaaavlgGKILVfggesgfsdeVEAYDPATNTWTALGELPTPR--HGHAAVLTDGKVYVIGGE 260
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 121-178 4.87e-04

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


:

Pssm-ID: 459635  Cd Length: 76  Bit Score: 39.07  E-value: 4.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
6RYX_A        121 EYRICPDTDYTGVNAKVVeGVTTIQACAELCSNTQDCRKSVFDHINNACAIKAAEPAT 178
Cdd:pfam00024   2 DFERVPGSSLSGVDVSTV-TVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGS 58
 
Name Accession Description Interval E-value
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 589-689 1.34e-30

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199882  Cd Length: 103  Bit Score: 115.80  E-value: 1.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      589 GSRAARPVISAISADpIKAGATLTFTVEGVEGQGT-AALIRLGSVTHSVNSDQRRVPLNVTVSGNEYS--ATLPDDYGIL 665
Cdd:cd02851   1 GFGAPRPTITSAPKT-VGYGQTFTVTVSGPGGGIVrVTLVRPGFVTHSFNMGQRLVKLPVTGSGGDYTvtVTAPPNANVA 79

                        90       100
                ....*....|....*....|....
6RYX_A      666 LPGYYYLFVSTPQGTPSIAKTVHV 689
Cdd:cd02851  80 PPGYYMLFVVNADGVPSVAKWVRV 103
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 600-689 1.04e-26

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


Pssm-ID: 462683  Cd Length: 91  Bit Score: 104.18  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A        600 ISADPIKAGATLTFTVeGVEGQGTAALIRLGSVTHSVNSDQRRVPLNVTV---SGNEYSATLPDDYGILLPGYYYLFVsT 676
Cdd:pfam09118   1 APPTTLSYGGTFTVTF-GVAGNVKVSLIRPGFVTHSVNMGQRLVFLDVTStggTGYTVTVTAPPNPNIAPPGYYMLFV-V 78

                          90
                  ....*....|...
6RYX_A        677 PQGTPSIAKTVHV 689
Cdd:pfam09118  79 DNGVPSVGKWVRV 91
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
282-553 3.89e-17

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 82.13  E-value: 3.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      282 DGRILIQGGSDADTVS----IYDPATNEFTRGPNMTLARGYQTSCTLSNGKVFTIGG---AWSGERVGKNGEVYDPVANA 354
Cdd:COG3055  22 DGKVYVAGGLSGGSASnsfeVYDPATNTWSELAPLPGPPRHHAAAVAQDGKLYVFGGftgANPSSTPLNDVYVYDPATNT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      355 WTYLPgadfrPMLTNdhegiwREDNHAWLFgwkNGSIFQAGpskdqhwyGIQGNGTVAKAatrDDDDAMCGVWvmydava 434
Cdd:COG3055 102 WTKLA-----PMPTP------RGGATALLL---DGKIYVVG--------GWDDGGNVAWV---EVYDPATGTW------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      435 gkifsaggspdytdspatqrahittigepntpaevERVADMGFPRGFANAVVLPDGQVLVTGGQRMSlVFTNT------- 507
Cdd:COG3055 150 -----------------------------------TQLAPLPTPRDHLAAAVLPDGKILVIGGRNGS-GFSNTwttlapl 193

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
6RYX_A      508 -------------DGILV----------AELFNPETREWKQMAPMAVPRnyHSVSILLPDATVFSGGGG 553
Cdd:COG3055 194 ptaraghaaavlgGKILVfggesgfsdeVEAYDPATNTWTALGELPTPR--HGHAAVLTDGKVYVIGGE 260
Kelch smart00612
Kelch domain;
491-541 7.62e-05

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 40.62  E-value: 7.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
6RYX_A         491 QVLVTGGQrMSLVFTNTdgilvAELFNPETREWKQMAPMAVPRNYHSVSIL 541
Cdd:smart00612   1 KIYVVGGF-DGGQRLKS-----VEVYDPETNKWTPLPSMPTPRSGHGVAVI 45
Kelch_6 pfam13964
Kelch motif;
482-533 2.31e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 39.24  E-value: 2.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
6RYX_A        482 ANAVVLPDGQVLVTGGQRMSLVFTNtdgilVAELFNPETREWKQMAPMAVPR 533
Cdd:pfam13964   4 FHSVVSVGGYIYVFGGYTNASPALN-----KLEVYNPLTKSWEELPPLPTPR 50
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 121-178 4.87e-04

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 39.07  E-value: 4.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
6RYX_A        121 EYRICPDTDYTGVNAKVVeGVTTIQACAELCSNTQDCRKSVFDHINNACAIKAAEPAT 178
Cdd:pfam00024   2 DFERVPGSSLSGVDVSTV-TVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGS 58
PHA03098 PHA03098
kelch-like protein; Provisional
 264-355 5.23e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 40.14  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A       264 TVTNTHHDMFCPGISQLeDGRILIQGGSDAD----TVSIYDPATNEFTRGPNMTLARGYQTSCTLsNGKVFTIGGAWSGE 339
Cdd:PHA03098 325 KVPELIYPRKNPGVTVF-NNRIYVIGGIYNSislnTVESWKPGESKWREEPPLIFPRYNPCVVNV-NNLIYVIGGISKND 402

                         90
                 ....*....|....*.
6RYX_A       340 RVGKNGEVYDPVANAW 355
Cdd:PHA03098 403 ELLKTVECFSLNTNKW 418
 
Name Accession Description Interval E-value
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 589-689 1.34e-30

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199882  Cd Length: 103  Bit Score: 115.80  E-value: 1.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      589 GSRAARPVISAISADpIKAGATLTFTVEGVEGQGT-AALIRLGSVTHSVNSDQRRVPLNVTVSGNEYS--ATLPDDYGIL 665
Cdd:cd02851   1 GFGAPRPTITSAPKT-VGYGQTFTVTVSGPGGGIVrVTLVRPGFVTHSFNMGQRLVKLPVTGSGGDYTvtVTAPPNANVA 79

                        90       100
                ....*....|....*....|....
6RYX_A      666 LPGYYYLFVSTPQGTPSIAKTVHV 689
Cdd:cd02851  80 PPGYYMLFVVNADGVPSVAKWVRV 103
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 600-689 1.04e-26

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


Pssm-ID: 462683  Cd Length: 91  Bit Score: 104.18  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A        600 ISADPIKAGATLTFTVeGVEGQGTAALIRLGSVTHSVNSDQRRVPLNVTV---SGNEYSATLPDDYGILLPGYYYLFVsT 676
Cdd:pfam09118   1 APPTTLSYGGTFTVTF-GVAGNVKVSLIRPGFVTHSVNMGQRLVFLDVTStggTGYTVTVTAPPNPNIAPPGYYMLFV-V 78

                          90
                  ....*....|...
6RYX_A        677 PQGTPSIAKTVHV 689
Cdd:pfam09118  79 DNGVPSVGKWVRV 91
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
282-553 3.89e-17

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 82.13  E-value: 3.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      282 DGRILIQGGSDADTVS----IYDPATNEFTRGPNMTLARGYQTSCTLSNGKVFTIGG---AWSGERVGKNGEVYDPVANA 354
Cdd:COG3055  22 DGKVYVAGGLSGGSASnsfeVYDPATNTWSELAPLPGPPRHHAAAVAQDGKLYVFGGftgANPSSTPLNDVYVYDPATNT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      355 WTYLPgadfrPMLTNdhegiwREDNHAWLFgwkNGSIFQAGpskdqhwyGIQGNGTVAKAatrDDDDAMCGVWvmydava 434
Cdd:COG3055 102 WTKLA-----PMPTP------RGGATALLL---DGKIYVVG--------GWDDGGNVAWV---EVYDPATGTW------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      435 gkifsaggspdytdspatqrahittigepntpaevERVADMGFPRGFANAVVLPDGQVLVTGGQRMSlVFTNT------- 507
Cdd:COG3055 150 -----------------------------------TQLAPLPTPRDHLAAAVLPDGKILVIGGRNGS-GFSNTwttlapl 193

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
6RYX_A      508 -------------DGILV----------AELFNPETREWKQMAPMAVPRnyHSVSILLPDATVFSGGGG 553
Cdd:COG3055 194 ptaraghaaavlgGKILVfggesgfsdeVEAYDPATNTWTALGELPTPR--HGHAAVLTDGKVYVIGGE 260
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
305-552 1.10e-11

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 65.95  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      305 EFTRGPNMTLARGYqTSCTLSNGKVFTIGGaWSGERVGKNGEVYDPVANAWTYLPGADFRPMltndhegiwredNHAWLF 384
Cdd:COG3055   2 TWSSLPDLPTPRSE-AAAALLDGKVYVAGG-LSGGSASNSFEVYDPATNTWSELAPLPGPPR------------HHAAAV 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      385 GwKNGSIFQAGpskdqhwygiqGNGTVAKAATRDDDdamcgVWVmYDavagkifsaggspdytdsPATQRAhittigepn 464
Cdd:COG3055  68 A-QDGKLYVFG-----------GFTGANPSSTPLND-----VYV-YD------------------PATNTW--------- 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      465 tpaevERVADMGFPRGFANAVVlPDGQVLVTGGQRMSLVFTNtdgilvAELFNPETREWKQMAPMAVPRNYHSVsILLPD 544
Cdd:COG3055 103 -----TKLAPMPTPRGGATALL-LDGKIYVVGGWDDGGNVAW------VEVYDPATGTWTQLAPLPTPRDHLAA-AVLPD 169


                ....*...
6RYX_A      545 ATVFSGGG 552
Cdd:COG3055 170 GKILVIGG 177
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
253-359 3.34e-07

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 52.47  E-value: 3.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      253 YDFATGAISQRT---VTNTHHDMFcpgisqLEDGRILIQGGSDAD----TVSIYDPATNEFTRGPNMTLARGYQTSCTLS 325
Cdd:COG3055  95 YDPATNTWTKLApmpTPRGGATAL------LLDGKIYVVGGWDDGgnvaWVEVYDPATGTWTQLAPLPTPRDHLAAAVLP 168

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
6RYX_A      326 NGKVFTIGGA--------WS------GERVG--------------------KNGEVYDPVANAWTYLP 359
Cdd:COG3055 169 DGKILVIGGRngsgfsntWTtlaplpTARAGhaaavlggkilvfggesgfsDEVEAYDPATNTWTALG 236
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
467-552 9.45e-07

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 50.92  E-value: 9.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A      467 AEVERVADMGFPRGFAnAVVLPDGQVLVTGGQRMSLVfTNTdgilvAELFNPETREWKQMAPMAVPRNYHSVSiLLPDAT 546
Cdd:COG3055   1 ATWSSLPDLPTPRSEA-AAALLDGKVYVAGGLSGGSA-SNS-----FEVYDPATNTWSELAPLPGPPRHHAAA-VAQDGK 72


                ....*.
6RYX_A      547 VFSGGG 552
Cdd:COG3055  73 LYVFGG 78
Kelch smart00612
Kelch domain;
491-541 7.62e-05

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 40.62  E-value: 7.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
6RYX_A         491 QVLVTGGQrMSLVFTNTdgilvAELFNPETREWKQMAPMAVPRNYHSVSIL 541
Cdd:smart00612   1 KIYVVGGF-DGGQRLKS-----VEVYDPETNKWTPLPSMPTPRSGHGVAVI 45
Kelch smart00612
Kelch domain;
284-326 1.46e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 39.85  E-value: 1.46e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
6RYX_A         284 RILIQGGSDA----DTVSIYDPATNEFTRGPNMTLARGYQTSCTLSN 326
Cdd:smart00612   1 KIYVVGGFDGgqrlKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
Kelch_6 pfam13964
Kelch motif;
482-533 2.31e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 39.24  E-value: 2.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
6RYX_A        482 ANAVVLPDGQVLVTGGQRMSLVFTNtdgilVAELFNPETREWKQMAPMAVPR 533
Cdd:pfam13964   4 FHSVVSVGGYIYVFGGYTNASPALN-----KLEVYNPLTKSWEELPPLPTPR 50
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 316-359 4.21e-04

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


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 38.36  E-value: 4.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
6RYX_A        316 RGYQTSCTLSNGKVFTIGGaWSGERVGKNGEVYDPVANAWTYLP 359
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGG-FDGNQSLNSVEVYDPETNTWSKLP 43
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 121-178 4.87e-04

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 39.07  E-value: 4.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
6RYX_A        121 EYRICPDTDYTGVNAKVVeGVTTIQACAELCSNTQDCRKSVFDHINNACAIKAAEPAT 178
Cdd:pfam00024   2 DFERVPGSSLSGVDVSTV-TVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGS 58
Kelch_4 pfam13418
Galactose oxidase, central domain;
478-529 1.58e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.82  E-value: 1.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
6RYX_A        478 PRGFANAVVLPDGQVLVTGGQrmslvftNTDGILVAEL--FNPETREWKQMAPM 529
Cdd:pfam13418   1 PRAYHTSTSIPDDTIYLFGGE-------GEDGTLLSDLwvFDLSTNEWTRLGSL 47
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 478-529 1.99e-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: 36.44  E-value: 1.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
6RYX_A        478 PRGFANAVVLpDGQVLVTGGQRMSlVFTNTdgilvAELFNPETREWKQMAPM 529
Cdd:pfam01344   1 RRSGAGVVVV-GGKIYVIGGFDGN-QSLNS-----VEVYDPETNTWSKLPSM 45
PHA03098 PHA03098
kelch-like protein; Provisional
 264-355 5.23e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 40.14  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6RYX_A       264 TVTNTHHDMFCPGISQLeDGRILIQGGSDAD----TVSIYDPATNEFTRGPNMTLARGYQTSCTLsNGKVFTIGGAWSGE 339
Cdd:PHA03098 325 KVPELIYPRKNPGVTVF-NNRIYVIGGIYNSislnTVESWKPGESKWREEPPLIFPRYNPCVVNV-NNLIYVIGGISKND 402

                         90
                 ....*....|....*.
6RYX_A       340 RVGKNGEVYDPVANAW 355
Cdd:PHA03098 403 ELLKTVECFSLNTNKW 418
 
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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