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Conserved domains on  [gi|74200263|dbj|BAE22931|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

kelch repeat domain-containing protein( domain architecture ID 1000219)

kelch repeat domain-containing protein such as human kelch-like protein 1 that may play a role in organizing the actin cytoskeleton of the brain cells

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];
119-378 1.14e-58

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 192.29  E-value: 1.14e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 119 GSWLRLADLQVPRSGLAGCVVGGLLYAVGGRnnspDGNTDSSALDCYNPMTNQWSPCASMS-VPRNRIGVGVIDGHIYAV 197
Cdd:COG3055   1 ATWSSLPDLPTPRSEAAAALLDGKVYVAGGL----SGGSASNSFEVYDPATNTWSELAPLPgPPRHHAAAVAQDGKLYVF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 198 GGSHGCIHHS----SVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITPMN 273
Cdd:COG3055  77 GGFTGANPSStplnDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTWTQLAPLP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 274 TIRSG-AGVCVLHNCIYAAGGYDGQDQLNsverydveteTWTFVAPMRHHRSALGITVHQGKIYVLGGYDGhtFLDSVEC 352
Cdd:COG3055 157 TPRDHlAAAVLPDGKILVIGGRNGSGFSN----------TWTTLAPLPTARAGHAAAVLGGKILVFGGESG--FSDEVEA 224

                       250       260
                ....*....|....*....|....*.
gi 74200263 353 YDPDSDTWSEVTRMTSGRSGVGVAVT 378
Cdd:COG3055 225 YDPATNTWTALGELPTPRHGHAAVLT 250
BACK super family cl28903
BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal ...
 1-37 1.96e-18

BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal to a BTB domain, in a diverse set of architectures together with Kelch, MATH, and/or TAZ domains. It is involved in interactions with the Cullin3 (Cul3) ubiquitin ligase complex, as well as in homo-oligomerization. Most proteins containing the BACK domain are understood to function as adaptor proteins that play a role in ubiquitination of various substrates.


The actual alignment was detected with superfamily member cd18458:

Pssm-ID: 475122 [Multi-domain]  Cd Length: 91  Bit Score: 79.65  E-value: 1.96e-18
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALL 37
Cdd:cd18458  55 ISRDELNVRCESEVYNAVIRWVKYDEENRRQYLEALL 91
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 93-128 2.13e-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: 35.67  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 74200263    93 VGRLIYTAGGY-FRQSLSYLEAYNPSNGSWLRLADLQ 128
Cdd:pfam01344  10 VGGKIYVIGGFdGNQSLNSVEVYDPETNTWSKLPSMP 46
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
119-378 1.14e-58

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 192.29  E-value: 1.14e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 119 GSWLRLADLQVPRSGLAGCVVGGLLYAVGGRnnspDGNTDSSALDCYNPMTNQWSPCASMS-VPRNRIGVGVIDGHIYAV 197
Cdd:COG3055   1 ATWSSLPDLPTPRSEAAAALLDGKVYVAGGL----SGGSASNSFEVYDPATNTWSELAPLPgPPRHHAAAVAQDGKLYVF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 198 GGSHGCIHHS----SVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITPMN 273
Cdd:COG3055  77 GGFTGANPSStplnDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTWTQLAPLP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 274 TIRSG-AGVCVLHNCIYAAGGYDGQDQLNsverydveteTWTFVAPMRHHRSALGITVHQGKIYVLGGYDGhtFLDSVEC 352
Cdd:COG3055 157 TPRDHlAAAVLPDGKILVIGGRNGSGFSN----------TWTTLAPLPTARAGHAAAVLGGKILVFGGESG--FSDEVEA 224

                       250       260
                ....*....|....*....|....*.
gi 74200263 353 YDPDSDTWSEVTRMTSGRSGVGVAVT 378
Cdd:COG3055 225 YDPATNTWTALGELPTPRHGHAAVLT 250
PHA03098 PHA03098
kelch-like protein; Provisional
 2-365 2.37e-43

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 158.39  E-value: 2.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263    2 SRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLqTQLQKCEilqadARCKDYLVqIFQE----- 76
Cdd:PHA03098 159 SDDKLNVSSEDVVLEIIIKWLTSKKNNKYKDICLILKVLRITFLSEEGI-KKLKRWK-----LRIKKKKI-VFNKrciki 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263   77 -LTLHKPTQAVPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSNgSWLRLADlqVPRSGLAGCVV-GGLLYAVGGRNNSPD 154
Cdd:PHA03098 232 iYSKKYNLNKILPRSSTFGSIIYIHITMSIFTYNYITNYSPLS-EINTIID--IHYVYCFGSVVlNNVIYFIGGMNKNNL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  155 GNTDSSAldcYNPMTNQWSPCASMSVPRNRIGVGVIDGHIYAVGGSHGCIHHSSVERYEPERDEWHLVAPMLTRRIGVGV 234
Cdd:PHA03098 309 SVNSVVS---YDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTVESWKPGESKWREEPPLIFPRYNPCV 385

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  235 AVLNRLLYAVGG-FDGTNRLNSAECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGGY---DGQDQLNSVERYDVET 310
Cdd:PHA03098 386 VNVNNLIYVIGGiSKNDELLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGIsyiDNIKVYNIVESYNPVT 465

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74200263  311 ETWTFVAPMRHHRSALGITVHQGKIYVLGGYDGHTFLDSVECYDPDSDTWSEVTR 365
Cdd:PHA03098 466 NKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTWTLFCK 520
BACK_KLHL19_KEAP1 cd18458
BACK (BTB and C-terminal Kelch) domain found in Kelch-like ECH-associated protein 1 (KEAP1); ...
 1-37 1.96e-18

BACK (BTB and C-terminal Kelch) domain found in Kelch-like ECH-associated protein 1 (KEAP1); KEAP1, also termed cytosolic inhibitor of Nrf2 (INrf2), or Kelch-like protein 19 (KLHL19), is a redox-regulated substrate adaptor protein for a Cullin3-dependent ubiquitin ligase complex that targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression.


Pssm-ID: 350533 [Multi-domain]  Cd Length: 91  Bit Score: 79.65  E-value: 1.96e-18
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALL 37
Cdd:cd18458  55 ISRDELNVRCESEVYNAVIRWVKYDEENRRQYLEALL 91
BACK pfam07707
BTB And C-terminal Kelch; This domain is found associated with pfam00651 and pfam01344. The ...
 1-55 2.42e-17

BTB And C-terminal Kelch; This domain is found associated with pfam00651 and pfam01344. The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues. This family appears to be closely related to the BTB domain (Finn RD, personal observation).


Pssm-ID: 462237 [Multi-domain]  Cd Length: 103  Bit Score: 76.82  E-value: 2.42e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74200263     1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLQTQLQ 55
Cdd:pfam07707  49 LSSDDLNVPSEEEVFEAVIRWVKHDVERRKKHLPELLSAVRLPLLSPQYLLNLVE 103
Kelch smart00612
Kelch domain;
240-286 1.42e-16

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 72.98  E-value: 1.42e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 74200263    240 LLYAVGGFDGTNRLNSAECYYPERNEWRMITPMNTIRSGAGVCVLHN 286
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
 1-53 5.41e-15

BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues.


Pssm-ID: 197943 [Multi-domain]  Cd Length: 101  Bit Score: 70.06  E-value: 5.41e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 74200263      1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLQTQ 53
Cdd:smart00875  49 LSSDDLNVSSEEEVFEAVLRWVKHDPEKRREHLPELLEHVRLPLLSPDYLLEV 101
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 276-320 3.24e-14

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: 66.48  E-value: 3.24e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 74200263   276 RSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMR 320
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPSMP 46
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 93-128 2.13e-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: 35.67  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 74200263    93 VGRLIYTAGGY-FRQSLSYLEAYNPSNGSWLRLADLQ 128
Cdd:pfam01344  10 VGGKIYVIGGFdGNQSLNSVEVYDPETNTWSKLPSMP 46
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
119-378 1.14e-58

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 192.29  E-value: 1.14e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 119 GSWLRLADLQVPRSGLAGCVVGGLLYAVGGRnnspDGNTDSSALDCYNPMTNQWSPCASMS-VPRNRIGVGVIDGHIYAV 197
Cdd:COG3055   1 ATWSSLPDLPTPRSEAAAALLDGKVYVAGGL----SGGSASNSFEVYDPATNTWSELAPLPgPPRHHAAAVAQDGKLYVF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 198 GGSHGCIHHS----SVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITPMN 273
Cdd:COG3055  77 GGFTGANPSStplnDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTWTQLAPLP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 274 TIRSG-AGVCVLHNCIYAAGGYDGQDQLNsverydveteTWTFVAPMRHHRSALGITVHQGKIYVLGGYDGhtFLDSVEC 352
Cdd:COG3055 157 TPRDHlAAAVLPDGKILVIGGRNGSGFSN----------TWTTLAPLPTARAGHAAAVLGGKILVFGGESG--FSDEVEA 224

                       250       260
                ....*....|....*....|....*.
gi 74200263 353 YDPDSDTWSEVTRMTSGRSGVGVAVT 378
Cdd:COG3055 225 YDPATNTWTALGELPTPRHGHAAVLT 250
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
97-354 7.09e-50

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 169.18  E-value: 7.09e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  97 IYTAGGYFRQS-LSYLEAYNPSNGSWLRLADLQVPRSGLAGCVV-GGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSP 174
Cdd:COG3055  25 VYVAGGLSGGSaSNSFEVYDPATNTWSELAPLPGPPRHHAAAVAqDGKLYVFGGFTGANPSSTPLNDVYVYDPATNTWTK 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 175 CASMSVPRNRIGVGVIDGHIYAVGGSHGCIHHSSVERYEPERDEWHLVAPMLTRRIGVGVAVL-NRLLYAVGGFDGTNRL 253
Cdd:COG3055 105 LAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTWTQLAPLPTPRDHLAAAVLpDGKILVIGGRNGSGFS 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263 254 NSaecyyperneWRMITPMNTIRSGAGVCVLHNCIYAAGGYDGqdQLNSVERYDVETETWTFVAPMRHHRSALGITVHQG 333
Cdd:COG3055 185 NT----------WTTLAPLPTARAGHAAAVLGGKILVFGGESG--FSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDG 252

                       250       260
                ....*....|....*....|....*
gi 74200263 334 KIYVLGGYD----GHTFLDSVECYD 354
Cdd:COG3055 253 KVYVIGGETkpgvRTPLVTSAEVYD 277
PHA03098 PHA03098
kelch-like protein; Provisional
 2-365 2.37e-43

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 158.39  E-value: 2.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263    2 SRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLqTQLQKCEilqadARCKDYLVqIFQE----- 76
Cdd:PHA03098 159 SDDKLNVSSEDVVLEIIIKWLTSKKNNKYKDICLILKVLRITFLSEEGI-KKLKRWK-----LRIKKKKI-VFNKrciki 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263   77 -LTLHKPTQAVPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSNgSWLRLADlqVPRSGLAGCVV-GGLLYAVGGRNNSPD 154
Cdd:PHA03098 232 iYSKKYNLNKILPRSSTFGSIIYIHITMSIFTYNYITNYSPLS-EINTIID--IHYVYCFGSVVlNNVIYFIGGMNKNNL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  155 GNTDSSAldcYNPMTNQWSPCASMSVPRNRIGVGVIDGHIYAVGGSHGCIHHSSVERYEPERDEWHLVAPMLTRRIGVGV 234
Cdd:PHA03098 309 SVNSVVS---YDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTVESWKPGESKWREEPPLIFPRYNPCV 385

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  235 AVLNRLLYAVGG-FDGTNRLNSAECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGGY---DGQDQLNSVERYDVET 310
Cdd:PHA03098 386 VNVNNLIYVIGGiSKNDELLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGIsyiDNIKVYNIVESYNPVT 465

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74200263  311 ETWTFVAPMRHHRSALGITVHQGKIYVLGGYDGHTFLDSVECYDPDSDTWSEVTR 365
Cdd:PHA03098 466 NKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTWTLFCK 520
PHA03098 PHA03098
kelch-like protein; Provisional
 96-326 7.25e-34

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 131.81  E-value: 7.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263   96 LIYTAGGYFRQSLSY--LEAYNPSNGSWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSaldcYNPMTNQWS 173
Cdd:PHA03098 296 VIYFIGGMNKNNLSVnsVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTVES----WKPGESKWR 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  174 PCASMSVPRNRIGVGVIDGHIYAVGG-SHGCIHHSSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGF---DG 249
Cdd:PHA03098 372 EEPPLIFPRYNPCVVNVNNLIYVIGGiSKNDELLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGIsyiDN 451

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74200263  250 TNRLNSAECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMRHHRSAL 326
Cdd:PHA03098 452 IKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTWTLFCKFPKVIGSL 528
PHA03098 PHA03098
kelch-like protein; Provisional
 233-378 5.85e-21

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 94.45  E-value: 5.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  233 GVAVLNRLLYAVGGFDGTN-RLNSAECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETE 311
Cdd:PHA03098 289 GSVVLNNVIYFIGGMNKNNlSVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTVESWKPGES 368

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74200263  312 TWTFVAPMRHHRSALGITVHQGKIYVLGG-YDGHTFLDSVECYDPDSDTWSEVTRMTSGRSGVGVAVT 378
Cdd:PHA03098 369 KWREEPPLIFPRYNPCVVNVNNLIYVIGGiSKNDELLKTVECFSLNTNKWSKGSPLPISHYGGCAIYH 436
BACK_KLHL19_KEAP1 cd18458
BACK (BTB and C-terminal Kelch) domain found in Kelch-like ECH-associated protein 1 (KEAP1); ...
 1-37 1.96e-18

BACK (BTB and C-terminal Kelch) domain found in Kelch-like ECH-associated protein 1 (KEAP1); KEAP1, also termed cytosolic inhibitor of Nrf2 (INrf2), or Kelch-like protein 19 (KLHL19), is a redox-regulated substrate adaptor protein for a Cullin3-dependent ubiquitin ligase complex that targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression.


Pssm-ID: 350533 [Multi-domain]  Cd Length: 91  Bit Score: 79.65  E-value: 1.96e-18
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALL 37
Cdd:cd18458  55 ISRDELNVRCESEVYNAVIRWVKYDEENRRQYLEALL 91
BACK pfam07707
BTB And C-terminal Kelch; This domain is found associated with pfam00651 and pfam01344. The ...
 1-55 2.42e-17

BTB And C-terminal Kelch; This domain is found associated with pfam00651 and pfam01344. The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues. This family appears to be closely related to the BTB domain (Finn RD, personal observation).


Pssm-ID: 462237 [Multi-domain]  Cd Length: 103  Bit Score: 76.82  E-value: 2.42e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74200263     1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLQTQLQ 55
Cdd:pfam07707  49 LSSDDLNVPSEEEVFEAVIRWVKHDVERRKKHLPELLSAVRLPLLSPQYLLNLVE 103
Kelch smart00612
Kelch domain;
240-286 1.42e-16

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 72.98  E-value: 1.42e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 74200263    240 LLYAVGGFDGTNRLNSAECYYPERNEWRMITPMNTIRSGAGVCVLHN 286
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
Kelch smart00612
Kelch domain;
334-380 5.36e-16

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 71.44  E-value: 5.36e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 74200263    334 KIYVLGGYDGHTFLDSVECYDPDSDTWSEVTRMTSGRSGVGVAVTME 380
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
Kelch smart00612
Kelch domain;
287-333 3.62e-15

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 69.12  E-value: 3.62e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 74200263    287 CIYAAGGYDGQDQLNSVERYDVETETWTFVAPMRHHRSALGITVHQG 333
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
 1-53 5.41e-15

BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues.


Pssm-ID: 197943 [Multi-domain]  Cd Length: 101  Bit Score: 70.06  E-value: 5.41e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 74200263      1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLQTQ 53
Cdd:smart00875  49 LSSDDLNVSSEEEVFEAVLRWVKHDPEKRREHLPELLEHVRLPLLSPDYLLEV 101
PLN02193 PLN02193
nitrile-specifier protein
 230-363 2.68e-14

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 74.22  E-value: 2.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  230 IGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITPMN---TIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERY 306
Cdd:PLN02193 220 LGVRMVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVEegpTPRSFHSMAADEENVYVFGGVSATARLKTLDSY 299

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74200263  307 DVETETW--------TFVApmrhhRSALGITVHQGKIYVLGGYDGHTfLDSVECYDPDSDTWSEV 363
Cdd:PLN02193 300 NIVDKKWfhcstpgdSFSI-----RGGAGLEVVQGKVWVVYGFNGCE-VDDVHYYDPVQDKWTQV 358
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 276-320 3.24e-14

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: 66.48  E-value: 3.24e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 74200263   276 RSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMR 320
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPSMP 46
PHA03098 PHA03098
kelch-like protein; Provisional
 253-378 3.99e-14

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 73.65  E-value: 3.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  253 LNSAECYYPERNEWRMITPmNTIRSGAGVCVLHNCIYAAGGYDGQDQ-LNSVERYDVETETWTFVAPMRHHRSALGITVH 331
Cdd:PHA03098 263 TYNYITNYSPLSEINTIID-IHYVYCFGSVVLNNVIYFIGGMNKNNLsVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVF 341

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 74200263  332 QGKIYVLGGYDGHTFLDSVECYDPDSDTWSEVTRMTSGRSGVGVAVT 378
Cdd:PHA03098 342 NNRIYVIGGIYNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNV 388
Kelch smart00612
Kelch domain;
193-238 8.27e-14

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 65.27  E-value: 8.27e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 74200263    193 HIYAVGGSHGCIHHSSVERYEPERDEWHLVAPMLTRRIGVGVAVLN 238
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVIN 46
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 322-367 1.96e-13

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: 64.17  E-value: 1.96e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 74200263   322 HRSALGITVHQGKIYVLGGYDGHTFLDSVECYDPDSDTWSEVTRMT 367
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPSMP 46
BACK_KLHL18 cd18457
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 18 (KLHL18); KLHL18 acts as ...
 1-50 1.17e-12

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 18 (KLHL18); KLHL18 acts as a substrate-specific adaptor for the Cullin3 E3 ubiquitin-protein ligase complex that regulates mitotic entry and ubiquitylates Aurora-A.


Pssm-ID: 350532 [Multi-domain]  Cd Length: 107  Bit Score: 63.87  E-value: 1.17e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFL 50
Cdd:cd18457  54 LSRDELNVKSEEQVFEAALAWVKYDRENREEYLPELLSKVRLPLLRPQFL 103
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 228-273 4.73e-12

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: 60.32  E-value: 4.73e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 74200263   228 RRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITPMN 273
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPSMP 46
BACK_KLHL2_like cd18445
BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL2 and KLHL3; This ...
 1-61 8.09e-12

BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL2 and KLHL3; This subfamily includes Kelch-like proteins, KLHL2 and KLHL3. KLHL2 is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. Both KLHL2 and KLHL3 function as a component of an E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins.


Pssm-ID: 350520 [Multi-domain]  Cd Length: 114  Bit Score: 61.48  E-value: 8.09e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLQTQLQKCEILQ 61
Cdd:cd18445  54 ISSDDLTVPSEEKVFEAVMSWVNHDPENRKEHLAELLEHVRLPLLSPEYLVQRVEEEELIK 114
Kelch smart00612
Kelch domain;
142-192 3.43e-11

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 57.95  E-value: 3.43e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 74200263    142 LLYAVGGRNnspdGNTDSSALDCYNPMTNQWSPCASMSVPRNRIGVGVIDG 192
Cdd:smart00612   1 KIYVVGGFD----GGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
PHA02790 PHA02790
Kelch-like protein; Provisional
 1-313 6.17e-11

Kelch-like protein; Provisional


Pssm-ID: 165153 [Multi-domain]  Cd Length: 480  Bit Score: 63.91  E-value: 6.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263    1 ISRDDLNVRCESEVFHACIDWVKydcpQRRFYVQALL----RAVRCHALTPRFLQTQ---LQKCEILQADARCKDYLVQI 73
Cdd:PHA02790 172 LESDELNVPDEDYVVDFVIKWYM----KRRNRLGNLLllikNVIRSNYLSPRGINNVkwiLDCTKIFHCDKQPRKSYKYP 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263   74 FQELTLHKpTQAVP----CRAPKVGRLIYTAGGYFRQSL-SYLEAYNPSNGSWLRLADLQVPRSGLAGCVVGGLLYAVGG 148
Cdd:PHA02790 248 FIEYPMNM-DQIIDifhmCTSTHVGEVVYLIGGWMNNEIhNNAIAVNYISNNWIPIPPMNSPRLYASGVPANNKLYVVGG 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  149 RNNspdgntdSSALDCYNPMTNQWSPCASMSVPRNRIGVGVIDGHIYAVGGSHGCihHSSVERYEPERDEWHLVAPMLTR 228
Cdd:PHA02790 327 LPN-------PTSVERWFHGDAAWVNMPSLLKPRCNPAVASINNVIYVIGGHSET--DTTTEYLLPNHDQWQFGPSTYYP 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  229 RIGVGVAVLNRLLYAVGgfdgtnrlNSAECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDV 308
Cdd:PHA02790 398 HYKSCALVFGRRLFLVG--------RNAEFYCESSNTWTLIDDPIYPRDNPELIIVDNKLLLIGGFYRGSYIDTIEVYNN 469


                 ....*
gi 74200263  309 ETETW 313
Cdd:PHA02790 470 RTYSW 474
PHA02713 PHA02713
hypothetical protein; Provisional
 224-338 2.83e-10

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 61.95  E-value: 2.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  224 PMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGG------YDGQ 297
Cdd:PHA02713 337 PMIKNRCRFSLAVIDDTIYAIGGQNGTNVERTIECYTMGDDKWKMLPDMPIALSSYGMCVLDQYIYIIGGrtehidYTSV 416

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74200263  298 DQLNSVE------------RYDVETETWTFVAPMRHHRSALGITVHQGKIYVL 338
Cdd:PHA02713 417 HHMNSIDmeedthssnkviRYDTVNNIWETLPNFWTGTIRPGVVSHKDDIYVV 469
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 181-225 3.08e-10

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


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 54.93  E-value: 3.08e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 74200263   181 PRNRIGVGVIDGHIYAVGGSHGCIHHSSVERYEPERDEWHLVAPM 225
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPSM 45
PHA02790 PHA02790
Kelch-like protein; Provisional
 139-361 4.19e-10

Kelch-like protein; Provisional


Pssm-ID: 165153 [Multi-domain]  Cd Length: 480  Bit Score: 61.21  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  139 VGGLLYAVGGRNNSPDGNtDSSALDCynpMTNQWSPCASMSVPRNRIGVGVIDGHIYAVGGshgCIHHSSVERYEPERDE 218
Cdd:PHA02790 270 VGEVVYLIGGWMNNEIHN-NAIAVNY---ISNNWIPIPPMNSPRLYASGVPANNKLYVVGG---LPNPTSVERWFHGDAA 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  219 WHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNrlNSAECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGgydgqd 298
Cdd:PHA02790 343 WVNMPSLLKPRCNPAVASINNVIYVIGGHSETD--TTTEYLLPNHDQWQFGPSTYYPHYKSCALVFGRRLFLVG------ 414

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74200263  299 qlNSVERYDVETETWTFVAPMRHHRSALGITVHQGKIYVLGGYDGHTFLDSVECYDPDSDTWS 361
Cdd:PHA02790 415 --RNAEFYCESSNTWTLIDDPIYPRDNPELIIVDNKLLLIGGFYRGSYIDTIEVYNNRTYSWN 475
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 130-179 6.94e-10

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


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 54.16  E-value: 6.94e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 74200263   130 PRSGLAGCVVGGLLYAVGGRnnspDGNTDSSALDCYNPMTNQWSPCASMS 179
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGF----DGNQSLNSVEVYDPETNTWSKLPSMP 46
BACK_KLHL1_like cd18444
BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5; ...
 1-50 1.92e-09

BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5; This subfamily contains Kelch-like proteins: KLHL1, KLHL4 and KLHL5, all of which share high identity and similarity with the Drosophila kelch protein, a component of ring canals. Members of this subfamily contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels.


Pssm-ID: 350519 [Multi-domain]  Cd Length: 106  Bit Score: 54.64  E-value: 1.92e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFL 50
Cdd:cd18444  55 LASDDLNVPSEETIFHALLLWVKHDLPERKKHLAKLLALIRLPLLTPQFL 104
Kelch smart00612
Kelch domain;
96-141 1.02e-08

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 50.63  E-value: 1.02e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 74200263     96 LIYTAGGY-FRQSLSYLEAYNPSNGSWLRLADLQVPRSGLAGCVVGG 141
Cdd:smart00612   1 KIYVVGGFdGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
BACK_KLHL12 cd18452
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 12 (KLHL12); KLHL12, also ...
 1-68 1.37e-08

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 12 (KLHL12); KLHL12, also termed CUL3-interacting protein 1 (C3IP1), or DKIR, is a substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport.


Pssm-ID: 350527 [Multi-domain]  Cd Length: 136  Bit Score: 53.17  E-value: 1.37e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLQTQLQKCEILQADARCKD 68
Cdd:cd18452  54 IKSDEIQVDSEEPVFEAVLNWVKHDKEEREDYLPELLQYVRLPLLSPRYITDVVDAEPLIRCSLECRD 121
BACK_KLHL2_Mayven cd18512
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 2 (KLHL2); KLHL2, also ...
 1-72 5.64e-08

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 2 (KLHL2); KLHL2, also called actin-binding protein Mayven, is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation.


Pssm-ID: 350587 [Multi-domain]  Cd Length: 130  Bit Score: 51.18  E-value: 5.64e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLQTQLQKCEILQADARCKDYLVQ 72
Cdd:cd18512  54 IASDKLTISSEEKVFEAVIAWVNHDKEVRQEHMAHLMEHVRLPLLSREYLVQRVEEETLVKNSSACKDYLIE 125
BACK_KLHL20 cd18459
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 20 (KLHL20); KLHL20, also ...
 1-41 6.43e-08

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 20 (KLHL20); KLHL20, also termed Kelch-like ECT2-interacting protein (KLEIP), or Kelch-like protein X, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. KLHL20 plays a role in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells. It also controls endothelial migration and sprouting angiogenesis.


Pssm-ID: 350534 [Multi-domain]  Cd Length: 100  Bit Score: 50.12  E-value: 6.43e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVR 41
Cdd:cd18459  55 ISSDELNVRSEEQVFNAVMAWVKYNIQERRPHLPQVLQHVR 95
BACK_KLHL3 cd18513
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 3 (KLHL3); KLHL3 serves as ...
 1-72 7.43e-08

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 3 (KLHL3); KLHL3 serves as a substrate adapter in Cullin3 (Cul3) E3 ubiquitin ligase complexes. It is a component of an E3 ubiquitin ligase complex that regulates blood pressure by targeting With-No-Lysine (WNK) kinases for degradation.


Pssm-ID: 350588 [Multi-domain]  Cd Length: 130  Bit Score: 50.84  E-value: 7.43e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFLQTQLQKCEILQADARCKDYLVQ 72
Cdd:cd18513  54 ISSDKLTVSSEEKVFEAVISWIKYDKEARLEHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIE 125
BACK_KLHL1 cd18509
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 1 (KLHL1); KLHL1 is a ...
 1-50 1.28e-07

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 1 (KLHL1); KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. It may play a role in organizing the actin cytoskeleton in brain cells. KLHL1 contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein.


Pssm-ID: 350584 [Multi-domain]  Cd Length: 106  Bit Score: 49.63  E-value: 1.28e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFL 50
Cdd:cd18509  55 LASDDVNVPDEETIFHALMMWVKYDMQRRCSDLSMLLAYIRLPLLPPQLL 104
BACK_KLHL29_KBTBD9 cd18468
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 29 (KLHL29); KLHL29, also ...
 1-50 4.92e-07

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 29 (KLHL29); KLHL29, also termed Kelch repeat and BTB domain-containing protein 9 (KBTBD9), belongs to the KLHL family. Its function remains unclear. A nuclear receptor subfamily 5, group A, member 2 (NR5A2)-Kelch-like family member 29 (KLHL29) fusion transcript may participate in the origin or progression of some colon cancers.


Pssm-ID: 350543 [Multi-domain]  Cd Length: 102  Bit Score: 47.79  E-value: 4.92e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFL 50
Cdd:cd18468  53 LSHDSLNTKAEELVFETAIKWLKKDPKNRKQHIAELLAVVRLPFIHPSYL 102
PHA02713 PHA02713
hypothetical protein; Provisional
 283-377 5.02e-07

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 51.55  E-value: 5.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  283 VLHNCIYAAGGYDGQD-QLNSVERYDVETETWTFVAPMRHHRSALGITVHQGKIYVLGGYDGHTFLDSVECYDPDSDTWS 361
Cdd:PHA02713 301 IVDNEIIIAGGYNFNNpSLNKVYKINIENKIHVELPPMIKNRCRFSLAVIDDTIYAIGGQNGTNVERTIECYTMGDDKWK 380

                         90
                 ....*....|....*.
gi 74200263  362 EVTRMTSGRSGVGVAV 377
Cdd:PHA02713 381 MLPDMPIALSSYGMCV 396
PLN02193 PLN02193
nitrile-specifier protein
 92-269 1.07e-06

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 50.34  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263   92 KVGRLIYTAGGYF--RQSL-SYLEAYNPSNGSW-LRLADLQVPR-SGLAGCVV--GGLLYAVGGRNNSPDGNTDSSaldc 164
Cdd:PLN02193 173 QVGNKIYSFGGEFtpNQPIdKHLYVFDLETRTWsISPATGDVPHlSCLGVRMVsiGSTLYVFGGRDASRQYNGFYS---- 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  165 YNPMTNQW---SPCASMSVPRNRIGVGVIDGHIYAVGGSHGCIHHSSVERYEPERDEW-HLVAPM--LTRRIGVGVAVLN 238
Cdd:PLN02193 249 FDTTTNEWkllTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIVDKKWfHCSTPGdsFSIRGGAGLEVVQ 328

                        170       180       190
                 ....*....|....*....|....*....|.
gi 74200263  239 RLLYAVGGFDGTnRLNSAECYYPERNEWRMI 269
Cdd:PLN02193 329 GKVWVVYGFNGC-EVDDVHYYDPVQDKWTQV 358
BACK_KLHL25_ENC2 cd18514
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 25 (KLHL25); KLHL25, also ...
 1-47 1.65e-06

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 25 (KLHL25); KLHL25, also called ectoderm-neural cortex protein 2 (ENC-2), is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1).


Pssm-ID: 350589 [Multi-domain]  Cd Length: 99  Bit Score: 45.99  E-value: 1.65e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRChALTP 47
Cdd:cd18514  54 ISSDELEIEDEQVVFNAVLQWVKYDLEKRKDYLPELLRNVRL-ALLP 99
BACK_KLHL25_like cd18464
BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL25 and KLHL37; The ...
 1-47 2.78e-06

BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins, KLHL25 and KLHL37; The family includes KLHL25 and KLHL37. KLHL25, also called ectoderm-neural cortex protein 2 (ENC-2), is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1). KLHL37, also called ectoderm-neural cortex protein 1 (ENC-1), or nuclear matrix protein NRP/B, or p53-induced gene 10 protein, is an actin-binding nuclear matrix protein that associates with p110(RB), and is involved in the regulation of neuronal process formation and in differentiation of neural crest cells.


Pssm-ID: 350539 [Multi-domain]  Cd Length: 98  Bit Score: 45.57  E-value: 2.78e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRChALTP 47
Cdd:cd18464  53 VSSEELEVEDERLVYEAVIGWIRYDLPRRHEVLPELLRSVRL-ALLP 98
BACK_KLHL8 cd18448
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 8 (KLHL8); KLHL8 is a ...
 1-41 4.53e-06

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 8 (KLHL8); KLHL8 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex. The BCR(KLHL8) ubiquitin ligase complex mediates ubiquitination and degradation of RAPSN.


Pssm-ID: 350523 [Multi-domain]  Cd Length: 97  Bit Score: 44.60  E-value: 4.53e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVR 41
Cdd:cd18448  55 ISSSDLNVESESQVYEAVMKWVKHDPQHRKRHLDDLLSQVR 95
Kelch_3 pfam13415
Galactose oxidase, central domain;
333-377 5.02e-06

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 43.43  E-value: 5.02e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 74200263   333 GKIYVLGGYD--GHTFLDSVECYDPDSDTWSEVTRMTSGRSGVGVAV 377
Cdd:pfam13415   2 DKLYIFGGLGfdGQTRLNDLYVYDLDTNTWTQIGDLPPPRSGHSATY 48
Kelch_6 pfam13964
Kelch motif;
322-370 5.55e-06

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 43.09  E-value: 5.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 74200263   322 HRSALGITVHQGKIYVLGGY-DGHTFLDSVECYDPDSDTWSEVTRMTSGR 370
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYtNASPALNKLEVYNPLTKSWEELPPLPTPR 50
PLN02153 PLN02153
epithiospecifier protein
 181-363 8.89e-06

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 47.29  E-value: 8.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  181 PRNRIGVGVIDGHIYAVGGSHGCIHHSSVERY--EPERDEWHLV-----APMLTRrIGVGVAVLNRLLYAVGGFDGTNRL 253
Cdd:PLN02153  22 PRCSHGIAVVGDKLYSFGGELKPNEHIDKDLYvfDFNTHTWSIApangdVPRISC-LGVRMVAVGTKLYIFGGRDEKREF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  254 NSAECYYPERNEWRMITPMNTI-----RSGAGVCVLHNCIYAAGG------YDGQDQLNSVERYDVETETWTFVA-PMRH 321
Cdd:PLN02153 101 SDFYSYDTVKNEWTFLTKLDEEggpeaRTFHSMASDENHVYVFGGvskgglMKTPERFRTIEAYNIADGKWVQLPdPGEN 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74200263  322 --HRSALGITVHQGKIYVL---------GGYDGHTFlDSVECYDPDSDTWSEV 363
Cdd:PLN02153 181 feKRGGAGFAVVQGKIWVVygfatsilpGGKSDYES-NAVQFFDPASGKWTEV 232
BACK_KLHL28_BTBD5 cd18467
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 28 (KLHL28); KLHL28, also ...
 1-41 1.01e-05

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 28 (KLHL28); KLHL28, also termed BTB/POZ domain-containing protein 5 (BTBD5), belongs to the KLHL family. Its function remains unclear.


Pssm-ID: 350542 [Multi-domain]  Cd Length: 99  Bit Score: 43.78  E-value: 1.01e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVR 41
Cdd:cd18467  54 VSNDCLNVVTEETVFYALESWIKYDVQERQKYLAQLLHCVR 94
BACK_KLHL5 cd18511
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 5 (KLHL5); KLHL5 shares ...
 1-50 1.05e-05

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 5 (KLHL5); KLHL5 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. It is abundantly expressed in ovary, adrenal gland, and thymus.


Pssm-ID: 350586 [Multi-domain]  Cd Length: 106  Bit Score: 43.90  E-value: 1.05e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFL 50
Cdd:cd18511  55 LASDDMNIPNEETILNALLSWVRHDVEQRRKDLSKLLAYIRLPLLAPQFL 104
Kelch_6 pfam13964
Kelch motif;
275-321 1.06e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 42.32  E-value: 1.06e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 74200263   275 IRSGAGVCVLHNCIYAAGGYDGQDQ-LNSVERYDVETETWTFVAPMRH 321
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNASPaLNKLEVYNPLTKSWEELPPLPT 48
PHA02713 PHA02713
hypothetical protein; Provisional
 97-324 1.64e-05

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 46.93  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263   97 IYTAGGYFRQSLSYLEAY--NPSNGSWLRLADLQVPRSGLAGCVVGGLLYAVGGRNnspdGNTDSSALDCYNPMTNQWSP 174
Cdd:PHA02713 306 IIIAGGYNFNNPSLNKVYkiNIENKIHVELPPMIKNRCRFSLAVIDDTIYAIGGQN----GTNVERTIECYTMGDDKWKM 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  175 CASMSVPRNRIGVGVIDGHIYAVGGSHGCIHHSSVE------------------RYEPERDEWHLVAPMLTRRIGVGVAV 236
Cdd:PHA02713 382 LPDMPIALSSYGMCVLDQYIYIIGGRTEHIDYTSVHhmnsidmeedthssnkviRYDTVNNIWETLPNFWTGTIRPGVVS 461

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  237 LNRLLYAVggFDGTNRLNSAECYY----PERNEWRMITPMNTiRSGAGVCVLH-NCIYAAGGYDG---QDQLNsverydV 308
Cdd:PHA02713 462 HKDDIYVV--CDIKDEKNVKTCIFryntNTYNGWELITTTES-RLSALHTILHdNTIMMLHCYESymlQDTFN------V 532

                        250
                 ....*....|....*.
gi 74200263  309 ETETWTFVApmrHHRS 324
Cdd:PHA02713 533 YTYEWNHIC---HQHS 545
BACK_KLHL7 cd18447
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a ...
 1-41 1.73e-05

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a BTB-Kelch protein that constitutes a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 cause autosomal-dominant retinitis pigmentosa.


Pssm-ID: 350522 [Multi-domain]  Cd Length: 98  Bit Score: 43.12  E-value: 1.73e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVR 41
Cdd:cd18447  55 LNQDTLTVRAEDQVYDAAVRWLKYDEPNRQPYMVDILAKVR 95
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 323-366 4.81e-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: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 40.40  E-value: 4.81e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 74200263   323 RSALGITVHQGKIYVLGGYDGH--TFLDSVECYDPDSDTWSEVTRM 366
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGSDGLgdLSSSDVLVYDPETNVWTEVPRL 47
BACK_KLHL17 cd18456
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 17 (KLHL17); KLHL17, also ...
 1-49 5.99e-05

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 17 (KLHL17); KLHL17, also termed actinfilin, is a substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes. It acts as a Cullin 3 (Cul3) substrate adaptor that links GluR6 to the E3 ubiquitin-ligase complex, and mediates the ubiquitination and subsequent degradation of GLUR6. It may play a role in the actin-based neuronal function.


Pssm-ID: 350531 [Multi-domain]  Cd Length: 102  Bit Score: 41.91  E-value: 5.99e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRF 49
Cdd:cd18456  54 ISSDSLNVPSEEEVYRAVLSWVKHDVDGRRQHVPRLMKCVRLPLLSRDF 102
Kelch_6 pfam13964
Kelch motif;
130-182 6.60e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 40.01  E-value: 6.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 74200263   130 PRSGLAGCVVGGLLYAVGGRNNspdGNTDSSALDCYNPMTNQWSPCASMSVPR 182
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTN---ASPALNKLEVYNPLTKSWEELPPLPTPR 50
PHA02713 PHA02713
hypothetical protein; Provisional
 218-365 7.14e-05

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 45.00  E-value: 7.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  218 EWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTN-RLNSAECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGGYDG 296
Cdd:PHA02713 283 EYSVISTIPNHIINYASAIVDNEIIIAGGYNFNNpSLNKVYKINIENKIHVELPPMIKNRCRFSLAVIDDTIYAIGGQNG 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74200263  297 QDQLNSVERYDVETETWTFVAPMRHHRSALGITVHQGKIYVLGGYDGHTFLDSVEC-----YDPDSDTWSEVTR 365
Cdd:PHA02713 363 TNVERTIECYTMGDDKWKMLPDMPIALSSYGMCVLDQYIYIIGGRTEHIDYTSVHHmnsidMEEDTHSSNKVIR 436
PRK14131 PRK14131
N-acetylneuraminate epimerase;
92-200 1.20e-04

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 43.85  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263   92 KVGRLIYTAGGYFRQSLSYLEAYNPSNGsWLRLADLQ-VPRSGLAGCVVGGLLYAVGGRNNSPDgNTDSSALD---CYNP 167
Cdd:PRK14131  36 IDNNTVYVGLGSAGTSWYKLDLNAPSKG-WTKIAAFPgGPREQAVAAFIDGKLYVFGGIGKTNS-EGSPQVFDdvyKYDP 113

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 74200263  168 MTNQWSPCASMSvPRNRIG-VGVI--DGHIYAVGGS 200
Cdd:PRK14131 114 KTNSWQKLDTRS-PVGLAGhVAVSlhNGKAYITGGV 148
BACK_KLHL16_gigaxonin cd18455
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 16 (KLHL16); Gigaxonin, ...
 1-45 1.48e-04

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 16 (KLHL16); Gigaxonin, also termed Kelch-like protein 16 (KLHL16), may be a cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. It may also act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as tubulin folding cofactor B (TBCB), microtubule-associated protein MAP1B and glial fibrillary acidic protein (GFAP). Gigaxonin is mutated in giant axonal neuropathy.


Pssm-ID: 350530 [Multi-domain]  Cd Length: 97  Bit Score: 40.38  E-value: 1.48e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHAL 45
Cdd:cd18455  53 LSRDKLNVGNEEYIFEAVLRWVRHDPEERKVHLKDLMSSCWRSGL 97
BACK_KLHL4 cd18510
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 4 (KLHL4); KLHL4 shares ...
 1-50 1.66e-04

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 4 (KLHL4); KLHL4 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein.


Pssm-ID: 350585 [Multi-domain]  Cd Length: 106  Bit Score: 40.67  E-value: 1.66e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFL 50
Cdd:cd18510  55 LASDDINVPDEETIFQALMMWVRHDLQNRQKDLGMLLSYIRLPLLPPQLL 104
PRK14131 PRK14131
N-acetylneuraminate epimerase;
276-346 2.37e-04

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 42.69  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74200263  276 RSGAGVCVLHNCIYAAGGY-----DGQDQL-NSVERYDVETETWTFVaPMRHHRSALG---ITVHQGKIYVLGGYDGHTF 346
Cdd:PRK14131  75 REQAVAAFIDGKLYVFGGIgktnsEGSPQVfDDVYKYDPKTNSWQKL-DTRSPVGLAGhvaVSLHNGKAYITGGVNKNIF 153
Kelch_6 pfam13964
Kelch motif;
189-229 4.07e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.09  E-value: 4.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 74200263   189 VIDGHIYAVGG-SHGCIHHSSVERYEPERDEWHLVAPMLTRR 229
Cdd:pfam13964   9 SVGGYIYVFGGyTNASPALNKLEVYNPLTKSWEELPPLPTPR 50
Kelch_3 pfam13415
Galactose oxidase, central domain;
238-284 4.62e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 37.65  E-value: 4.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 74200263   238 NRLLYAVGG--FDGTNRLNSAECYYPERNEWRMITPMNTIRSGAGVCVL 284
Cdd:pfam13415   1 GDKLYIFGGlgFDGQTRLNDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 49
BACK_KEL_like cd18508
BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster ring canal kelch ...
 1-25 6.82e-04

BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster ring canal kelch protein (KEL) and similar proteins; KEL, also termed kelch short protein, is a component of ring canals that regulates the flow of cytoplasm between cells. It binds actin and may be involved in the regulation of cytoplasm flow from nurse cells to the oocyte during oogenesis.


Pssm-ID: 350583 [Multi-domain]  Cd Length: 77  Bit Score: 38.16  E-value: 6.82e-04
                        10        20
                ....*....|....*....|....*
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYD 25
Cdd:cd18508  53 ISSDRLNVPSEERVYEAAVAWLKHD 77
BACK_KLHL37_ENC1 cd18515
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 37 (KLHL37); KLHL37, also ...
 1-47 8.32e-04

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 37 (KLHL37); KLHL37, also called ectoderm-neural cortex protein 1 (ENC-1), or nuclear matrix protein NRP/B, or p53-induced gene 10 protein, is an actin-binding nuclear matrix protein that associates with p110(RB), and is involved in the regulation of neuronal process formation and in differentiation of neural crest cells.


Pssm-ID: 350590 [Multi-domain]  Cd Length: 98  Bit Score: 38.42  E-value: 8.32e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRChALTP 47
Cdd:cd18515  53 LSSEELETEDERLVYEAAINWVNYDLKKRHCYLSELLQTVRL-ALLP 98
Kelch_3 pfam13415
Galactose oxidase, central domain;
140-182 1.35e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 36.50  E-value: 1.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 74200263   140 GGLLYAVGGRNnsPDGNTDSSALDCYNPMTNQWSPCASMSVPR 182
Cdd:pfam13415   1 GDKLYIFGGLG--FDGQTRLNDLYVYDLDTNTWTQIGDLPPPR 41
BACK_KLHL40_KBTBD5 cd18516
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 40 (KLHL40); KLHL40, also ...
 1-42 1.52e-03

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 40 (KLHL40); KLHL40, also called Kelch repeat and BTB domain-containing protein 5, or sarcosynapsin, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. Mutations in KLHL40 may cause severe autosomal-recessive nemaline myopathy.


Pssm-ID: 350591 [Multi-domain]  Cd Length: 99  Bit Score: 37.81  E-value: 1.52e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRC 42
Cdd:cd18516  54 ISSDSLNVEKEEDVFEAVMKWVGKDQEERTKALPVLLESIRF 95
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 93-128 2.13e-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: 35.67  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 74200263    93 VGRLIYTAGGY-FRQSLSYLEAYNPSNGSWLRLADLQ 128
Cdd:pfam01344  10 VGGKIYVIGGFdGNQSLNSVEVYDPETNTWSKLPSMP 46
BACK_KLHL27_IPP cd18466
BACK (BTB and C-terminal Kelch) domain found in intracisternal A particle-promoted polypeptide ...
 4-50 2.14e-03

BACK (BTB and C-terminal Kelch) domain found in intracisternal A particle-promoted polypeptide (IPP); IPP, also termed Kelch-like protein 27 (KLHL27), is an actin-binding protein that may play a role in organizing the actin cytoskeleton.


Pssm-ID: 350541 [Multi-domain]  Cd Length: 103  Bit Score: 37.46  E-value: 2.14e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 74200263   4 DDLNVRCESEVFHACIDWVKYDCPQRRFYVQALLRAVRCHALTPRFL 50
Cdd:cd18466  57 EELSIEDEYQVFTAAMEWILKDVGKRKKHVVEVLEPVRFPLLPPQRL 103
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 130-178 2.70e-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: 35.39  E-value: 2.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 74200263   130 PRSGLAGCVVGGLLYAVGGRNNSPDgnTDSSALDCYNPMTNQWSPCASM 178
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDGLGD--LSSSDVLVYDPETNVWTEVPRL 47
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 276-319 2.95e-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: 35.39  E-value: 2.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 74200263   276 RSGAGVCVLHNCIYAAGGYDGQDQL--NSVERYDVETETWTFVAPM 319
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGSDGLGDLssSDVLVYDPETNVWTEVPRL 47
Kelch_6 pfam13964
Kelch motif;
93-131 5.08e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 35.00  E-value: 5.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 74200263    93 VGRLIYTAGGYFRQS--LSYLEAYNPSNGSWLRLADLQVPR 131
Cdd:pfam13964  10 VGGYIYVFGGYTNASpaLNKLEVYNPLTKSWEELPPLPTPR 50
BACK_KLHL10 cd18450
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 10 (KLHL10); KLHL10 may be ...
 1-25 6.70e-03

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 10 (KLHL10); KLHL10 may be a substrate-specific adapter of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins during spermatogenesis.


Pssm-ID: 350525 [Multi-domain]  Cd Length: 80  Bit Score: 35.28  E-value: 6.70e-03
                        10        20
                ....*....|....*....|....*
gi 74200263   1 ISRDDLNVRCESEVFHACIDWVKYD 25
Cdd:cd18450  55 IEDDELNVKEEEVVFEAIVKWIDHD 79
Kelch_3 pfam13415
Galactose oxidase, central domain;
94-139 7.08e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 34.19  E-value: 7.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 74200263    94 GRLIYTAGGYFRQS---LSYLEAYNPSNGSWLRLADLQVPRSGLAGCVV 139
Cdd:pfam13415   1 GDKLYIFGGLGFDGqtrLNDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 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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