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Conserved domains on  [gi|2217263266|ref|XP_047290052|]
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influenza virus NS1A-binding protein isoform X2 [Homo sapiens]

Protein Classification

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];
260-538 7.62e-58

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 194.22  E-value: 7.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 260 KPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPM-RTPRARFQMAVLMGQLYVVGGSNGHS 338
Cdd:COG3055     4 SSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAPLpGPPRHHAAAVAQDGKLYVFGGFTGAN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 339 DDLSC---GEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDPYGqkGLKNCDVFDPVTKLWTSCAPL-NIRRH 414
Cdd:COG3055    84 PSSTPlndVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGG--NVAWVEVYDPATGTWTQLAPLpTPRDH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 415 QSAVCELGGYLYIIGGAeswnclntveRYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAIscVEMYDPTR 494
Cdd:COG3055   162 LAAAVLPDGKILVIGGR----------NGSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGGESGFSDE--VEAYDPAT 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2217263266 495 NEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGN----EFLNTVEVYN 538
Cdd:COG3055   230 NTWTALGELPTPRHGHAAVLTDGKVYVIGGETKPgvrtPLVTSAEVYD 277
BACK_NS1BP_IVNS1ABP cd18502
BACK (BTB and C-terminal Kelch) domain found in influenza virus NS1A-binding protein (NS1-BP); ...
 40-136 2.18e-44

BACK (BTB and C-terminal Kelch) domain found in influenza virus NS1A-binding protein (NS1-BP); NS1-BP, also called NS1-binding protein, or Aryl hydrocarbon receptor-associated protein 3, or IVNS1ABP, is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control.


:

Pssm-ID: 350577  Cd Length: 99  Bit Score: 152.39  E-value: 2.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPS--NGKLYTKVINWVQRSI 117
Cdd:cd18502     1 LTPENCIGIRSFAGRMNDSELLQKVDSYIQENIEEVAESKEFLKLPRLQIEVILESNQELESinERKLCQLVLEWVQRSI 80

                          90
                  ....*....|....*....
gi 2217263266 118 WENGDSLEELMEEVQTLYY 136
Cdd:cd18502    81 EEGGLDLDDLTEKVHMLYL 99
BTB_POZ super family cl38908
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 5-48 3.09e-18

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.


The actual alignment was detected with superfamily member cd18306:

Pssm-ID: 453885 [Multi-domain]  Cd Length: 124  Bit Score: 80.77  E-value: 3.09e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217263266   5 RLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISY 48
Cdd:cd18306    81 RLEVPADLVKSVYSAAKKLKMDRVKKACGDFLLEKLTPQNCIGI 124
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
260-538 7.62e-58

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 194.22  E-value: 7.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 260 KPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPM-RTPRARFQMAVLMGQLYVVGGSNGHS 338
Cdd:COG3055     4 SSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAPLpGPPRHHAAAVAQDGKLYVFGGFTGAN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 339 DDLSC---GEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDPYGqkGLKNCDVFDPVTKLWTSCAPL-NIRRH 414
Cdd:COG3055    84 PSSTPlndVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGG--NVAWVEVYDPATGTWTQLAPLpTPRDH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 415 QSAVCELGGYLYIIGGAeswnclntveRYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAIscVEMYDPTR 494
Cdd:COG3055   162 LAAAVLPDGKILVIGGR----------NGSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGGESGFSDE--VEAYDPAT 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2217263266 495 NEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGN----EFLNTVEVYN 538
Cdd:COG3055   230 NTWTALGELPTPRHGHAAVLTDGKVYVIGGETKPgvrtPLVTSAEVYD 277
BACK_NS1BP_IVNS1ABP cd18502
BACK (BTB and C-terminal Kelch) domain found in influenza virus NS1A-binding protein (NS1-BP); ...
 40-136 2.18e-44

BACK (BTB and C-terminal Kelch) domain found in influenza virus NS1A-binding protein (NS1-BP); NS1-BP, also called NS1-binding protein, or Aryl hydrocarbon receptor-associated protein 3, or IVNS1ABP, is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control.


Pssm-ID: 350577  Cd Length: 99  Bit Score: 152.39  E-value: 2.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPS--NGKLYTKVINWVQRSI 117
Cdd:cd18502     1 LTPENCIGIRSFAGRMNDSELLQKVDSYIQENIEEVAESKEFLKLPRLQIEVILESNQELESinERKLCQLVLEWVQRSI 80

                          90
                  ....*....|....*....
gi 2217263266 118 WENGDSLEELMEEVQTLYY 136
Cdd:cd18502    81 EEGGLDLDDLTEKVHMLYL 99
PHA03098 PHA03098
kelch-like protein; Provisional
 298-549 4.15e-39

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 149.92  E-value: 4.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 298 CYNPHTDHWSFLAPmRTPRARFQMAVLMGQLYVVGGSNGHSDDLSCGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLY 377
Cdd:PHA03098  268 TNYSPLSEINTIID-IHYVYCFGSVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIY 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 378 IVGGSdpYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIGGA-ESWNCLNTVERYNPENNTWTLIAPM 456
Cdd:PHA03098  347 VIGGI--YNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNVNNLIYVIGGIsKNDELLKTVECFSLNTNKWSKGSPL 424

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 457 NVARRGAGVAVLNGKLFVCGGF---DGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNT 533
Cdd:PHA03098  425 PISHYGGCAIYHDGKIYVIGGIsyiDNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEYYINE 504

                         250
                  ....*....|....*.
gi 2217263266 534 VEVYNLESNEWSPYTK 549
Cdd:PHA03098  505 IEVYDDKTNTWTLFCK 520
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
 45-140 3.07e-18

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: 80.08  E-value: 3.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266   45 CISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLE-DNVCLPSNGKLYTKVINWVQRSIWENGDS 123
Cdd:smart00875   1 CLGIRRFADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSsDDLNVSSEEEVFEAVLRWVKHDPEKRREH 80

                           90
                   ....*....|....*..
gi 2217263266  124 LEELMEEVQTLYYSADH 140
Cdd:smart00875  81 LPELLEHVRLPLLSPDY 97
BTB_POZ_NS1BP cd18306
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 5-48 3.09e-18

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP); NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349615 [Multi-domain]  Cd Length: 124  Bit Score: 80.77  E-value: 3.09e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217263266   5 RLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISY 48
Cdd:cd18306    81 RLEVPADLVKSVYSAAKKLKMDRVKKACGDFLLEKLTPQNCIGI 124
Kelch smart00612
Kelch domain;
425-470 1.31e-14

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 67.97  E-value: 1.31e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217263266  425 LYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNG 470
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 506-546 3.34e-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: 63.79  E-value: 3.34e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217263266 506 PRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSP 546
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSK 41
BACK pfam07707
BTB And C-terminal Kelch; This domain is found associated with pfam00651 and pfam01344. The ...
 45-131 2.35e-10

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: 57.56  E-value: 2.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  45 CISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLE-DNVCLPSNGKLYTKVINWVQRSIWENGDS 123
Cdd:pfam07707   1 CLGIYRFADAYGCTELAEAALRFILQNFLEVAKSEEFLELSLEQLLELLSsDDLNVPSEEEVFEAVIRWVKHDVERRKKH 80


                  ....*...
gi 2217263266 124 LEELMEEV 131
Cdd:pfam07707  81 LPELLSAV 88
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
260-538 7.62e-58

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 194.22  E-value: 7.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 260 KPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPM-RTPRARFQMAVLMGQLYVVGGSNGHS 338
Cdd:COG3055     4 SSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAPLpGPPRHHAAAVAQDGKLYVFGGFTGAN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 339 DDLSC---GEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDPYGqkGLKNCDVFDPVTKLWTSCAPL-NIRRH 414
Cdd:COG3055    84 PSSTPlndVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGG--NVAWVEVYDPATGTWTQLAPLpTPRDH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 415 QSAVCELGGYLYIIGGAeswnclntveRYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAIscVEMYDPTR 494
Cdd:COG3055   162 LAAAVLPDGKILVIGGR----------NGSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGGESGFSDE--VEAYDPAT 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2217263266 495 NEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGN----EFLNTVEVYN 538
Cdd:COG3055   230 NTWTALGELPTPRHGHAAVLTDGKVYVIGGETKPgvrtPLVTSAEVYD 277
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
353-545 5.65e-49

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 170.72  E-value: 5.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 353 DWIPVPELRTNRCNAGVCALNGKLYIVGGSDpyGQKGLKNCDVFDPVTKLWTSCAPLNI-RRHQSAVCELGGYLYIIGG- 430
Cdd:COG3055     2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLS--GGSASNSFEVYDPATNTWSELAPLPGpPRHHAAAVAQDGKLYVFGGf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 431 ---AESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMTSPR 507
Cdd:COG3055    80 tgaNPSSTPLNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTWTQLAPLPTPR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217263266 508 SNAGIATVGN-TIYAVGGFDG-----------------------------------NEFLNTVEVYNLESNEWS 545
Cdd:COG3055   160 DHLAAAVLPDgKILVIGGRNGsgfsntwttlaplptaraghaaavlggkilvfggeSGFSDEVEAYDPATNTWT 233
BACK_NS1BP_IVNS1ABP cd18502
BACK (BTB and C-terminal Kelch) domain found in influenza virus NS1A-binding protein (NS1-BP); ...
 40-136 2.18e-44

BACK (BTB and C-terminal Kelch) domain found in influenza virus NS1A-binding protein (NS1-BP); NS1-BP, also called NS1-binding protein, or Aryl hydrocarbon receptor-associated protein 3, or IVNS1ABP, is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control.


Pssm-ID: 350577  Cd Length: 99  Bit Score: 152.39  E-value: 2.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPS--NGKLYTKVINWVQRSI 117
Cdd:cd18502     1 LTPENCIGIRSFAGRMNDSELLQKVDSYIQENIEEVAESKEFLKLPRLQIEVILESNQELESinERKLCQLVLEWVQRSI 80

                          90
                  ....*....|....*....
gi 2217263266 118 WENGDSLEELMEEVQTLYY 136
Cdd:cd18502    81 EEGGLDLDDLTEKVHMLYL 99
PHA03098 PHA03098
kelch-like protein; Provisional
 298-549 4.15e-39

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 149.92  E-value: 4.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 298 CYNPHTDHWSFLAPmRTPRARFQMAVLMGQLYVVGGSNGHSDDLSCGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLY 377
Cdd:PHA03098  268 TNYSPLSEINTIID-IHYVYCFGSVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPELIYPRKNPGVTVFNNRIY 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 378 IVGGSdpYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIGGA-ESWNCLNTVERYNPENNTWTLIAPM 456
Cdd:PHA03098  347 VIGGI--YNSISLNTVESWKPGESKWREEPPLIFPRYNPCVVNVNNLIYVIGGIsKNDELLKTVECFSLNTNKWSKGSPL 424

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 457 NVARRGAGVAVLNGKLFVCGGF---DGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNT 533
Cdd:PHA03098  425 PISHYGGCAIYHDGKIYVIGGIsyiDNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEYYINE 504

                         250
                  ....*....|....*.
gi 2217263266 534 VEVYNLESNEWSPYTK 549
Cdd:PHA03098  505 IEVYDDKTNTWTLFCK 520
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
403-546 4.25e-38

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 141.45  E-value: 4.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 403 WTSCAPLNIRRHQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARR-GAGVAVLNGKLFVCGGFDGS 481
Cdd:COG3055     3 WSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAPLPGPPRhHAAAVAQDGKLYVFGGFTGA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217263266 482 HAISC----VEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSP 546
Cdd:COG3055    83 NPSSTplndVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEVYDPATGTWTQ 151
PHA03098 PHA03098
kelch-like protein; Provisional
 13-502 2.86e-34

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 136.05  E-value: 2.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  13 VKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVM 92
Cdd:PHA03098   78 VKDILSIANYLIIDFLINLCINYIIKIIDDNNCIDIYRFSFFYGCKKLYSAAYNYIRNNIELIYNDPDFIYLSKNELIKI 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  93 L---------EDNVCLpsngklytKVINWVQRSIWENGDSLEELMEEVQTLYYSAD--HKLLDGNLLDGQAEVFGSDDDH 161
Cdd:PHA03098  158 LsddklnvssEDVVLE--------IIIKWLTSKKNNKYKDICLILKVLRITFLSEEgiKKLKRWKLRIKKKKIVFNKRCI 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 162 ------IQFVQKKPPRENGHKQISSSSTGCLSSPNATVqSPKHEWKIVasEKTSNNTYLCL---AVLDGIFcvIFLHGRN 232
Cdd:PHA03098  230 kiiyskKYNLNKILPRSSTFGSIIYIHITMSIFTYNYI-TNYSPLSEI--NTIIDIHYVYCfgsVVLNNVI--YFIGGMN 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 233 spQSSPTStpklSKSLSFEMQQDELIEKPmsPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPM 312
Cdd:PHA03098  305 --KNNLSV----NSVVSYDTKTKSWNKVP--ELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTVESWKPGESKWREEPPL 376

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 313 RTPrarfqmavlmgqlyvvggsnghsddlscgemydsniddwipvpelrtnRCNAGVCALNGKLYIVGGSDPYGQKgLKN 392
Cdd:PHA03098  377 IFP------------------------------------------------RYNPCVVNVNNLIYVIGGISKNDEL-LKT 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 393 CDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIGG---AESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLN 469
Cdd:PHA03098  408 VECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGisyIDNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFN 487

                         490       500       510
                  ....*....|....*....|....*....|...
gi 2217263266 470 GKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGN 502
Cdd:PHA03098  488 NKIYVVGGDKYEYYINEIEVYDDKTNTWTLFCK 520
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
 45-140 3.07e-18

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: 80.08  E-value: 3.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266   45 CISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLE-DNVCLPSNGKLYTKVINWVQRSIWENGDS 123
Cdd:smart00875   1 CLGIRRFADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSsDDLNVSSEEEVFEAVLRWVKHDPEKRREH 80

                           90
                   ....*....|....*..
gi 2217263266  124 LEELMEEVQTLYYSADH 140
Cdd:smart00875  81 LPELLEHVRLPLLSPDY 97
BTB_POZ_NS1BP cd18306
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 5-48 3.09e-18

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP); NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349615 [Multi-domain]  Cd Length: 124  Bit Score: 80.77  E-value: 3.09e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217263266   5 RLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISY 48
Cdd:cd18306    81 RLEVPADLVKSVYSAAKKLKMDRVKKACGDFLLEKLTPQNCIGI 124
Kelch smart00612
Kelch domain;
425-470 1.31e-14

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 67.97  E-value: 1.31e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2217263266  425 LYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNG 470
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
Kelch smart00612
Kelch domain;
471-517 2.75e-14

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 66.81  E-value: 2.75e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217263266  471 KLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGN 517
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 506-546 3.34e-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: 63.79  E-value: 3.34e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217263266 506 PRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSP 546
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSK 41
PLN02153 PLN02153
epithiospecifier protein
 315-524 6.62e-13

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 70.02  E-value: 6.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 315 PRARFQMAVLMGQLYVVGGS---NGHSD-DLScgeMYDSNIDDWIPVPE----LRTNRCNAGVCALNGKLYIVGGSDPyg 386
Cdd:PLN02153   22 PRCSHGIAVVGDKLYSFGGElkpNEHIDkDLY---VFDFNTHTWSIAPAngdvPRISCLGVRMVAVGTKLYIFGGRDE-- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 387 QKGLKNCDVFDPVTKLWTSCAPLNIR-----RHQSAVCELGGYLYIIGGAESWNCLNTVER------YNPENNTWT-LIA 454
Cdd:PLN02153   97 KREFSDFYSYDTVKNEWTFLTKLDEEggpeaRTFHSMASDENHVYVFGGVSKGGLMKTPERfrtieaYNIADGKWVqLPD 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 455 P-MNVARRG-AGVAVLNGKLFVCGGFDGS--------HAISCVEMYDPTRNEW---KMMGNMTSPRSNAGIATVGNTIYA 521
Cdd:PLN02153  177 PgENFEKRGgAGFAVVQGKIWVVYGFATSilpggksdYESNAVQFFDPASGKWtevETTGAKPSARSVFAHAVVGKYIII 256


                  ...
gi 2217263266 522 VGG 524
Cdd:PLN02153  257 FGG 259
Kelch smart00612
Kelch domain;
280-326 1.01e-12

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 62.58  E-value: 1.01e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2217263266  280 KLIAAGGYNREECLRTVECYNPHTDHWSFLAPMRTPRARFQMAVLMG 326
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
PHA02790 PHA02790
Kelch-like protein; Provisional
 328-545 1.12e-12

Kelch-like protein; Provisional


Pssm-ID: 165153 [Multi-domain]  Cd Length: 480  Bit Score: 70.07  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 328 LYVVGG-----SNGHSDDLSCGEmydsniDDWIPVPELRTNRCNAGVCALNGKLYIVGG-SDPYGQKGLKNCDVFdpvtk 401
Cdd:PHA02790  274 VYLIGGwmnneIHNNAIAVNYIS------NNWIPIPPMNSPRLYASGVPANNKLYVVGGlPNPTSVERWFHGDAA----- 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 402 lWTSCAPLNIRRHQSAVCELGGYLYIIGGAESWNclNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGgfdgs 481
Cdd:PHA02790  343 -WVNMPSLLKPRCNPAVASINNVIYVIGGHSETD--TTTEYLLPNHDQWQFGPSTYYPHYKSCALVFGRRLFLVG----- 414

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217263266 482 haiSCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWS 545
Cdd:PHA02790  415 ---RNAEFYCESSNTWTLIDDPIYPRDNPELIIVDNKLLLIGGFYRGSYIDTIEVYNNRTYSWN 475
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 459-504 2.22e-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: 61.47  E-value: 2.22e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217263266 459 ARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMT 504
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPSMP 46
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 412-457 2.35e-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: 61.47  E-value: 2.35e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217263266 412 RRHQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMN 457
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 ...
 43-131 1.85e-11

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: 61.09  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  43 TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSIWENG 121
Cdd:cd18445     4 SNCLGIRAFADLHSCTDLLKYAQTYTEQHFSEVVKGEEFLLLSKEQVcELISSDDLTVPSEEKVFEAVMSWVNHDPENRK 83

                          90
                  ....*....|
gi 2217263266 122 DSLEELMEEV 131
Cdd:cd18445    84 EHLAELLEHV 93
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 268-313 4.97e-11

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: 57.62  E-value: 4.97e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217263266 268 ARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPMR 313
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPSMP 46
BACK pfam07707
BTB And C-terminal Kelch; This domain is found associated with pfam00651 and pfam01344. The ...
 45-131 2.35e-10

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: 57.56  E-value: 2.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  45 CISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLE-DNVCLPSNGKLYTKVINWVQRSIWENGDS 123
Cdd:pfam07707   1 CLGIYRFADAYGCTELAEAALRFILQNFLEVAKSEEFLELSLEQLLELLSsDDLNVPSEEEVFEAVIRWVKHDVERRKKH 80


                  ....*...
gi 2217263266 124 LEELMEEV 131
Cdd:pfam07707  81 LPELLSAV 88
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
496-546 2.56e-10

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 61.33  E-value: 2.56e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217263266 496 EWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSP 546
Cdd:COG3055     2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSE 52
Kelch smart00612
Kelch domain;
327-374 5.00e-10

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 54.87  E-value: 5.00e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2217263266  327 QLYVVGGSNGhSDDLSCGEMYDSNIDDWIPVPELRTNRCNAGVCALNG 374
Cdd:smart00612   1 KIYVVGGFDG-GQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
BACK_KLHL18 cd18457
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 18 (KLHL18); KLHL18 acts as ...
 43-131 6.22e-10

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: 56.55  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  43 TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLK-LEVMLEDNVCLPSNGKLYTKVINWVQRSIWENG 121
Cdd:cd18457     4 NNCLGIRQFAETMMCSSLVDAANKYIQQHFIEVSKSEEFLALSKEEvLEILSRDELNVKSEEQVFEAALAWVKYDRENRE 83

                          90
                  ....*....|
gi 2217263266 122 DSLEELMEEV 131
Cdd:cd18457    84 EYLPELLSKV 93
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 364-410 6.96e-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: 54.54  E-value: 6.96e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217263266 364 RCNAGVCALNGKLYIVGGSDpyGQKGLKNCDVFDPVTKLWTSCAPLN 410
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFD--GNQSLNSVEVYDPETNTWSKLPSMP 46
PHA02790 PHA02790
Kelch-like protein; Provisional
 285-499 1.33e-09

Kelch-like protein; Provisional


Pssm-ID: 165153 [Multi-domain]  Cd Length: 480  Bit Score: 60.44  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 285 GGYNREECLRTVECYNPHTDHWSFLAPMRTPRARFQMAVLMGQLYVVGGSnghsDDLSCGEMYDSNIDDWIPVPELRTNR 364
Cdd:PHA02790  278 GGWMNNEIHNNAIAVNYISNNWIPIPPMNSPRLYASGVPANNKLYVVGGL----PNPTSVERWFHGDAAWVNMPSLLKPR 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 365 CNAGVCALNGKLYIVGG---SDPYGQKGLKNCDV--FDPVTKL--WTSCAPLNIRRhqsavcelggyLYIIGgaeswncl 437
Cdd:PHA02790  354 CNPAVASINNVIYVIGGhseTDTTTEYLLPNHDQwqFGPSTYYphYKSCALVFGRR-----------LFLVG-------- 414

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217263266 438 NTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKM 499
Cdd:PHA02790  415 RNAEFYCESSNTWTLIDDPIYPRDNPELIIVDNKLLLIGGFYRGSYIDTIEVYNNRTYSWNI 476
PLN02193 PLN02193
nitrile-specifier protein
 368-524 1.38e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 60.35  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 368 GVC--ALNGKLYIVGGSDPYGQ-KGLKNcdvFDPVTKLWTSCAPL----NIRRHQSAVCELGGyLYIIGGAESWNCLNTV 440
Cdd:PLN02193  221 GVRmvSIGSTLYVFGGRDASRQyNGFYS---FDTTTNEWKLLTPVeegpTPRSFHSMAADEEN-VYVFGGVSATARLKTL 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 441 ERYNPENNTWTLIA-PMN--VARRGAGVAVLNGKLFVCGGFDGSHaISCVEMYDPTRNEW---KMMGNMTSPRSNAGIAT 514
Cdd:PLN02193  297 DSYNIVDKKWFHCStPGDsfSIRGGAGLEVVQGKVWVVYGFNGCE-VDDVHYYDPVQDKWtqvETFGVRPSERSVFASAA 375

                         170
                  ....*....|
gi 2217263266 515 VGNTIYAVGG 524
Cdd:PLN02193  376 VGKHIVIFGG 385
Kelch smart00612
Kelch domain;
519-546 1.41e-09

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 53.72  E-value: 1.41e-09
                           10        20
                   ....*....|....*....|....*...
gi 2217263266  519 IYAVGGFDGNEFLNTVEVYNLESNEWSP 546
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKWTP 29
PLN02193 PLN02193
nitrile-specifier protein
 364-545 1.78e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 59.97  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 364 RCNAGVCALNGKLYIVGGSDPYGQKGLKNCDVFDPVTKLWT-----------SCapLNIRrhqsaVCELGGYLYIIGGAE 432
Cdd:PLN02193  166 RCSHGIAQVGNKIYSFGGEFTPNQPIDKHLYVFDLETRTWSispatgdvphlSC--LGVR-----MVSIGSTLYVFGGRD 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 433 SWNCLNTVERYNPENNTWTLIAPMN---VARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEW---KMMGNMTSP 506
Cdd:PLN02193  239 ASRQYNGFYSFDTTTNEWKLLTPVEegpTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIVDKKWfhcSTPGDSFSI 318

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217263266 507 RSNAGIATVGNTIYAVGGFDGNEfLNTVEVYNLESNEWS 545
Cdd:PLN02193  319 RGGAGLEVVQGKVWVVYGFNGCE-VDDVHYYDPVQDKWT 356
PHA02713 PHA02713
hypothetical protein; Provisional
 240-393 3.37e-09

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 59.25  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 240 STPKLSKSLSFEMQQDELIEKPmsPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPMRTPRARF 319
Cdd:PHA02713  315 NNPSLNKVYKINIENKIHVELP--PMIKNRCRFSLAVIDDTIYAIGGQNGTNVERTIECYTMGDDKWKMLPDMPIALSSY 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 320 QMAVLMGQLYVVGGSNGHSDDLSCGEM-----------------YDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVggS 382
Cdd:PHA02713  393 GMCVLDQYIYIIGGRTEHIDYTSVHHMnsidmeedthssnkvirYDTVNNIWETLPNFWTGTIRPGVVSHKDDIYVV--C 470

                         170
                  ....*....|.
gi 2217263266 383 DPYGQKGLKNC 393
Cdd:PHA02713  471 DIKDEKNVKTC 481
BACK_KLHL12 cd18452
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 12 (KLHL12); KLHL12, also ...
 40-132 5.98e-09

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: 54.71  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLE-DNVCLPSNGKLYTKVINWVQRSIW 118
Cdd:cd18452     1 LDPSNCLGIRDFAETHNCVDLMQAAEVFSQKHFPEVVQHEEFMLLSQEEVEKLIKsDEIQVDSEEPVFEAVLNWVKHDKE 80

                          90
                  ....*....|....
gi 2217263266 119 ENGDSLEELMEEVQ 132
Cdd:cd18452    81 EREDYLPELLQYVR 94
PHA02790 PHA02790
Kelch-like protein; Provisional
 408-544 9.67e-09

Kelch-like protein; Provisional


Pssm-ID: 165153 [Multi-domain]  Cd Length: 480  Bit Score: 57.75  E-value: 9.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 408 PLNIRR-----HQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSh 482
Cdd:PHA02790  252 PMNMDQiidifHMCTSTHVGEVVYLIGGWMNNEIHNNAIAVNYISNNWIPIPPMNSPRLYASGVPANNKLYVVGGLPNP- 330

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217263266 483 aiSCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFdgNEFLNTVEVYNLESNEW 544
Cdd:PHA02790  331 --TSVERWFHGDAAWVNMPSLLKPRCNPAVASINNVIYVIGGH--SETDTTTEYLLPNHDQW 388
BACK_KLHL17 cd18456
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 17 (KLHL17); KLHL17, also ...
 40-139 1.14e-08

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: 52.70  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLP-RLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIW 118
Cdd:cd18456     1 LDPSNCLGIRGFADTHSCSDLLKSAHKYVLQHFVEVSKTEEFMLLPlKQVLDLISSDSLNVPSEEEVYRAVLSWVKHDVD 80

                          90       100
                  ....*....|....*....|.
gi 2217263266 119 ENGDSLEELMEEVQTLYYSAD 139
Cdd:cd18456    81 GRRQHVPRLMKCVRLPLLSRD 101
PHA03098 PHA03098
kelch-like protein; Provisional
 420-552 1.47e-08

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 57.47  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 420 ELGGYLYIIGGaeSWNCLNTVERYNPENNTWTLIAPMNVaRRGAGVAVLNGKLFVCGGFDGS-HAISCVEMYDPTRNEWK 498
Cdd:PHA03098  248 TFGSIIYIHIT--MSIFTYNYITNYSPLSEINTIIDIHY-VYCFGSVVLNNVIYFIGGMNKNnLSVNSVVSYDTKTKSWN 324

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217263266 499 MMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSPYTKIFQ 552
Cdd:PHA03098  325 KVPELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTVESWKPGESKWREEPPLIF 378
BACK_KLHL2_Mayven cd18512
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 2 (KLHL2); KLHL2, also ...
 43-132 3.61e-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: 52.34  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  43 TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSIWENG 121
Cdd:cd18512     4 TNCLGIRAFADMHACTELLNQANTYAEQHFSDVVLSEEFLNLGIEQVcSLIASDKLTISSEEKVFEAVIAWVNHDKEVRQ 83

                          90
                  ....*....|.
gi 2217263266 122 DSLEELMEEVQ 132
Cdd:cd18512    84 EHMAHLMEHVR 94
BACK_KLHL8 cd18448
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 8 (KLHL8); KLHL8 is a ...
 43-131 4.41e-08

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: 51.15  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  43 TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLED-NVCLPSNGKLYTKVINWVQRSIWENG 121
Cdd:cd18448     5 SNCLGVRTFAEQHNRVDLMKMADKYACDHFNEVVECEEFVSISAQHLEKLISSsDLNVESESQVYEAVMKWVKHDPQHRK 84

                          90
                  ....*....|
gi 2217263266 122 DSLEELMEEV 131
Cdd:cd18448    85 RHLDDLLSQV 94
Kelch_6 pfam13964
Kelch motif;
413-460 4.73e-08

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 49.26  E-value: 4.73e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217263266 413 RHQSAVCELGGYLYIIGGAE-SWNCLNTVERYNPENNTWTLIAPMNVAR 460
Cdd:pfam13964   2 RTFHSVVSVGGYIYVFGGYTnASPALNKLEVYNPLTKSWEELPPLPTPR 50
Kelch smart00612
Kelch domain;
375-423 4.79e-08

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 49.48  E-value: 4.79e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2217263266  375 KLYIVGGSDpyGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELGG 423
Cdd:smart00612   1 KIYVVGGFD--GGQRLKSVEVYDPETNKWTPLPSMPTPRSGHGVAVING 47
PRK14131 PRK14131
N-acetylneuraminate epimerase;
421-527 4.89e-08

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 55.02  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 421 LGGYLYI-IGGAE-SWNCLNTveryNPENNTWTLIAPM-NVARRGAGVAVLNGKLFVCGGF-----DGS-HAISCVEMYD 491
Cdd:PRK14131   37 DNNTVYVgLGSAGtSWYKLDL----NAPSKGWTKIAAFpGGPREQAVAAFIDGKLYVFGGIgktnsEGSpQVFDDVYKYD 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217263266 492 PTRNEWKMMgNMTSPRSNAGIATV---GNTIYAVGG-----FDG 527
Cdd:PRK14131  113 PKTNSWQKL-DTRSPVGLAGHVAVslhNGKAYITGGvnkniFDG 155
BACK_KLHL26 cd18465
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 26 (KLHL26); KLHL26 is a ...
 40-114 9.34e-08

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 26 (KLHL26); KLHL26 is a kelch family protein encoded by gene klhl26, which is regulated by p53 via fuzzy tandem repeats.


Pssm-ID: 350540  Cd Length: 97  Bit Score: 49.91  E-value: 9.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVcLPSNGK--LYTKVINWVQ 114
Cdd:cd18465     1 MSVETCLNIGQMATTFSLASLKESVDAFTFRHFLQIAEEEDFLHLPLERLVFFLQSNK-LKNCSEidLFRAAIRWLQ 76
PRK14131 PRK14131
N-acetylneuraminate epimerase;
413-540 1.26e-07

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 53.87  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 413 RHQSAVCELGGYLYIIGGAESWN------CLNTVERYNPENNTWT---LIAPMNVArRGAGVAVLNGKLFVCGG-----F 478
Cdd:PRK14131   75 REQAVAAFIDGKLYVFGGIGKTNsegspqVFDDVYKYDPKTNSWQkldTRSPVGLA-GHVAVSLHNGKAYITGGvnkniF 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 479 DG---------------------------------SHAIScvemYDPTRNEWKMMGnmTSPRS-NAGIATV--GNTIYAV 522
Cdd:PRK14131  154 DGyfedlaaagkdktpkdkindayfdkkpedyffnKEVLS----YDPSTNQWKNAG--ESPFLgTAGSAVVikGNKLWLI 227

                         170       180
                  ....*....|....*....|.
gi 2217263266 523 GGfdgnEF---LNTVEVYNLE 540
Cdd:PRK14131  228 NG----EIkpgLRTDAVKQGK 244
BACK_KLHL19_KEAP1 cd18458
BACK (BTB and C-terminal Kelch) domain found in Kelch-like ECH-associated protein 1 (KEAP1); ...
 40-114 1.97e-07

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: 48.83  E-value: 1.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQ 114
Cdd:cd18458     2 LDPSNCIGIANFAEQHGCTELHKKAREYIYMHFSEVSQSEEFFNLSPCQLvALISRDELNVRCESEVYNAVIRWVK 77
BACK cd14733
BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal ...
 41-95 2.05e-07

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.


Pssm-ID: 350515 [Multi-domain]  Cd Length: 55  Bit Score: 47.66  E-value: 2.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217263266  41 DVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLED 95
Cdd:cd14733     1 DPENCLGILELADLYNLEELKEKALKFILENFEEVSKSEEFLELSVELLLELLSS 55
Kelch_3 pfam13415
Galactose oxidase, central domain;
422-468 3.35e-07

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 46.90  E-value: 3.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217263266 422 GGYLYIIGGA--ESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVL 468
Cdd:pfam13415   1 GDKLYIFGGLgfDGQTRLNDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 49
BACK_KLHL4 cd18510
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 4 (KLHL4); KLHL4 shares ...
 43-117 3.78e-07

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: 48.76  E-value: 3.78e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217263266  43 TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVML-EDNVCLPSNGKLYTKVINWVQRSI 117
Cdd:cd18510     5 SNCLGIRSFGDAQGCTELLKVAHSYTMEHFLEVIKNQEFLLLPASEIVKLLaSDDINVPDEETIFQALMMWVRHDL 80
BACK_KLHL20 cd18459
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 20 (KLHL20); KLHL20, also ...
 39-132 6.73e-07

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: 47.81  E-value: 6.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  39 RMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSI 117
Cdd:cd18459     1 QLDPSNCLGIRAFADTHACRELLRIADKFTQHNFQEVMESEEFMLLPVNQLiDIISSDELNVRSEEQVFNAVMAWVKYNI 80

                          90
                  ....*....|....*
gi 2217263266 118 WENGDSLEELMEEVQ 132
Cdd:cd18459    81 QERRPHLPQVLQHVR 95
BACK_KLHL1 cd18509
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 1 (KLHL1); KLHL1 is a ...
 43-128 1.13e-06

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: 47.32  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  43 TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLK-LEVMLEDNVCLPSNGKLYTKVINWVQRSIWENG 121
Cdd:cd18509     5 SNCLGIRAFADAQGCIELMKVAHSYTMENIMEVIRNQEFLLLPAEElHKLLASDDVNVPDEETIFHALMMWVKYDMQRRC 84


                  ....*..
gi 2217263266 122 DSLEELM 128
Cdd:cd18509    85 SDLSMLL 91
PHA02713 PHA02713
hypothetical protein; Provisional
 405-524 1.53e-06

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 50.78  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 405 SCAPLNIRRHQSAVCElggYLYIIGGAESWN--CLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSH 482
Cdd:PHA02713  288 STIPNHIINYASAIVD---NEIIIAGGYNFNnpSLNKVYKINIENKIHVELPPMIKNRCRFSLAVIDDTIYAIGGQNGTN 364

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217263266 483 AISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGG 524
Cdd:PHA02713  365 VERTIECYTMGDDKWKMLPDMPIALSSYGMCVLDQYIYIIGG 406
BACK_KLHL5 cd18511
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 5 (KLHL5); KLHL5 shares ...
 43-132 2.18e-06

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: 46.60  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  43 TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVML-EDNVCLPSNGKLYTKVINWVQRSIWENG 121
Cdd:cd18511     5 SNCLGIRSFADAQGCTDLHKVAHNYTMEHFMEVIRNQEFLLLPASEIAKLLaSDDMNIPNEETILNALLSWVRHDVEQRR 84

                          90
                  ....*....|.
gi 2217263266 122 DSLEELMEEVQ 132
Cdd:cd18511    85 KDLSKLLAYIR 95
BACK_KBTBD3 cd18480
BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein ...
 40-117 2.20e-06

BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 3 (KBTBD3); KBTBD3, also termed BTB and kelch domain-containing protein 3 (BKLHD3), is a BTB-Kelch family protein. Its function remains unclear.


Pssm-ID: 350555 [Multi-domain]  Cd Length: 82  Bit Score: 45.78  E-value: 2.20e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLE-DNVCLPSNGKLYTKVINWVQRSI 117
Cdd:cd18480     1 LDLSNCLQLLSFAESYGSTRLLDHALEFVMQHFSLLSQSQEFLELNFEVLEKILEaDELNVPDEEAVLKAVLRWTKHDL 79
BACK_KLHL3 cd18513
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 3 (KLHL3); KLHL3 serves as ...
 43-140 3.76e-06

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: 46.60  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  43 TSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSIWENG 121
Cdd:cd18513     4 TNCLGIRAFADVHTCTELLQQANAYAEQHFPEVMLGEEFLSLSLDQVcSLISSDKLTVSSEEKVFEAVISWIKYDKEARL 83

                          90
                  ....*....|....*....
gi 2217263266 122 DSLEELMEEVQTLYYSADH 140
Cdd:cd18513    84 EHMAKLMEHVRLPLLPRDY 102
BACK_KEL_like cd18508
BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster ring canal kelch ...
 41-114 6.81e-06

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: 44.32  E-value: 6.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217263266  41 DVTSCISYRNFA---SCMgdsRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQ 114
Cdd:cd18508     1 DATNCLGIHEFAdahSCV---ELEEAAQNYIYQHFNEVIQGEEFLSLDHESLtELISSDRLNVPSEERVYEAAVAWLK 75
Kelch_3 pfam13415
Galactose oxidase, central domain;
373-419 1.07e-05

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 42.66  E-value: 1.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217263266 373 NGKLYIVGGSDPYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVC 419
Cdd:pfam13415   1 GDKLYIFGGLGFDGQTRLNDLYVYDLDTNTWTQIGDLPPPRSGHSAT 47
Kelch_6 pfam13964
Kelch motif;
364-413 1.69e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 42.32  E-value: 1.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217263266 364 RCNAGVCALNGKLYIVGGSDPYGqKGLKNCDVFDPVTKLWTSCAPLNIRR 413
Cdd:pfam13964   2 RTFHSVVSVGGYIYVFGGYTNAS-PALNKLEVYNPLTKSWEELPPLPTPR 50
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 315-361 1.86e-05

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


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 41.83  E-value: 1.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217263266 315 PRARFQMAVLMGQLYVVGGSNGHSdDLSCGEMYDSNIDDWIPVPELR 361
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQ-SLNSVEVYDPETNTWSKLPSMP 46
PHA02713 PHA02713
hypothetical protein; Provisional
 343-522 2.14e-05

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 47.31  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 343 CGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDpYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELG 422
Cdd:PHA02713  273 CILVYNINTMEYSVISTIPNHIINYASAIVDNEIIIAGGYN-FNNPSLNKVYKINIENKIHVELPPMIKNRCRFSLAVID 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 423 GYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGG------FDGSHAISCVEM------- 489
Cdd:PHA02713  352 DTIYAIGGQNGTNVERTIECYTMGDDKWKMLPDMPIALSSYGMCVLDQYIYIIGGrtehidYTSVHHMNSIDMeedthss 431

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217263266 490 -----YDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAV 522
Cdd:PHA02713  432 nkvirYDTVNNIWETLPNFWTGTIRPGVVSHKDDIYVV 469
PLN02153 PLN02153
epithiospecifier protein
 364-544 4.52e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 45.75  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 364 RCNAGVCALNGKLYIVGGSDPYGQKGLKNCDVFDPVTKLWtSCAPLNirrhqsavcelggylyiiGGAESWNCLntvery 443
Cdd:PLN02153   23 RCSHGIAVVGDKLYSFGGELKPNEHIDKDLYVFDFNTHTW-SIAPAN------------------GDVPRISCL------ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 444 npenntwtliapmnvarrGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMT-----SPRSNAGIATVGNT 518
Cdd:PLN02153   78 ------------------GVRMVAVGTKLYIFGGRDEKREFSDFYSYDTVKNEWTFLTKLDeeggpEARTFHSMASDENH 139

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2217263266 519 IYAVGGFDGNEFLN------TVEVYNLESNEW 544
Cdd:PLN02153  140 VYVFGGVSKGGLMKtperfrTIEAYNIADGKW 171
PLN02193 PLN02193
nitrile-specifier protein
 299-430 6.56e-05

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 45.72  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266 299 YNPHTDHWSFLAPMR---TPRARFQMAVLMGQLYVVGGSnGHSDDLSCGEMYdsNIDD--WI----PVPELrTNRCNAGV 369
Cdd:PLN02193  249 FDTTTNEWKLLTPVEegpTPRSFHSMAADEENVYVFGGV-SATARLKTLDSY--NIVDkkWFhcstPGDSF-SIRGGAGL 324

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217263266 370 CALNGKLYIVggsdpYGQKGLKNCDV--FDPVTKLWTSCAPLNIR---RHQSAVCELGGYLYIIGG 430
Cdd:PLN02193  325 EVVQGKVWVV-----YGFNGCEVDDVhyYDPVQDKWTQVETFGVRpseRSVFASAAVGKHIVIFGG 385
BACK_KLHL1_like cd18444
BACK (BTB and C-terminal Kelch) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5; ...
 45-131 8.01e-05

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: 41.93  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  45 CISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDS 123
Cdd:cd18444     7 CLGIRSFADAQGCTDLLKVAHNYTMEHFMEVIQNQEFLLLPAEEVaKLLASDDLNVPSEETIFHALLLWVKHDLPERKKH 86


                  ....*...
gi 2217263266 124 LEELMEEV 131
Cdd:cd18444    87 LAKLLALI 94
Kelch_6 pfam13964
Kelch motif;
506-545 1.50e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 39.63  E-value: 1.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217263266 506 PRSNAGIATVGNTIYAVGGF-DGNEFLNTVEVYNLESNEWS 545
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYtNASPALNKLEVYNPLTKSWE 41
BACK_KLHL21 cd18460
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 21 (KLHL21); KLHL21 is a ...
 40-132 1.53e-04

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 21 (KLHL21); KLHL21 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of aurora B. KLHL21 targets IkappaB kinase-beta to regulate nuclear factor kappa-light chain enhancer of activated B cells (NF-kappaB) signaling negatively.


Pssm-ID: 350535 [Multi-domain]  Cd Length: 101  Bit Score: 40.94  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLK-LEVMLEDNVCLPSNGKLYTKVINWVQRSIW 118
Cdd:cd18460     1 LDVSNCLEMQDFAEAFACRGLAEAAKRFILRHIVELAKGEQFERLPLKRlLEYLSDDGLCVDKEETAYQIALRWVKADPK 80

                          90
                  ....*....|....
gi 2217263266 119 ENGDSLEELMEEVQ 132
Cdd:cd18460    81 HRQHFWPELLQHVR 94
BACK_KLHL16_gigaxonin cd18455
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 16 (KLHL16); Gigaxonin, ...
 45-128 2.42e-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: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  45 CISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDS 123
Cdd:cd18455     5 CIGIRDFAERFSCPHVHYVATEYLETHFRDVSSTEEFLELSPEKLkELLSRDKLNVGNEEYIFEAVLRWVRHDPEERKVH 84


                  ....*
gi 2217263266 124 LEELM 128
Cdd:cd18455    85 LKDLM 89
Kelch_3 pfam13415
Galactose oxidase, central domain;
516-547 2.77e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 38.81  E-value: 2.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217263266 516 GNTIYAVGG--FDGNEFLNTVEVYNLESNEWSPY 547
Cdd:pfam13415   1 GDKLYIFGGlgFDGQTRLNDLYVYDLDTNTWTQI 34
BACK_KLHL7 cd18447
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a ...
 39-114 3.87e-04

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: 40.03  E-value: 3.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217263266  39 RMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVML-EDNVCLPSNGKLYTKVINWVQ 114
Cdd:cd18447     1 QVDASNCLGISVLAECLDCPELKATADDFIHQHFTEVYKTDEFLQLDVKRVTHLLnQDTLTVRAEDQVYDAAVRWLK 77
Kelch_6 pfam13964
Kelch motif;
268-316 5.27e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.09  E-value: 5.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217263266 268 ARSGLGTAEMNGKLIAAGGY-NREECLRTVECYNPHTDHWSFLAPMRTPR 316
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYtNASPALNKLEVYNPLTKSWEELPPLPTPR 50
BACK_KBTBD8 cd18483
BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein ...
 40-127 6.63e-04

BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing protein 8 (KBTBD8); KBTBD8, also called T-cell activation kelch repeat protein (TA-KRP), is a BTB-kelch family protein that is located in the Golgi apparatus and translocates to the spindle apparatus during mitosis. It acts as a substrate-specific adaptor for a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex monoubiquitylates NOLC1 and its paralogue TCOF1, the mutation of which underlies the neurocristopathy Treacher Collins syndrome.


Pssm-ID: 350558 [Multi-domain]  Cd Length: 97  Bit Score: 39.07  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLE-DNVCLPSNGKLYTKVINWVQRSIW 118
Cdd:cd18483     1 LDPQNSIGVFIFADHYGHQELKERSQDYIRKKFLSVTKEQEFLHLTKDQLISILNsDDLNVEKEEHVYESIIHWFEHEQS 80


                  ....*....
gi 2217263266 119 ENGDSLEEL 127
Cdd:cd18483    81 KREMHLPEI 89
BACK_KLHL29_KBTBD9 cd18468
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 29 (KLHL29); KLHL29, also ...
 41-131 6.76e-04

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: 39.32  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  41 DVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSIWE 119
Cdd:cd18468     1 TPSNCLGIWALAEALQCTELHNMAKAYALQNFPDVARQEEILSISKDDIvEYLSHDSLNTKAEELVFETAIKWLKKDPKN 80

                          90
                  ....*....|..
gi 2217263266 120 NGDSLEELMEEV 131
Cdd:cd18468    81 RKQHIAELLAVV 92
Kelch_4 pfam13418
Galactose oxidase, central domain;
412-456 8.40e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 37.21  E-value: 8.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217263266 412 RRHQSAVCELGGYLYIIGGaESWNC--LNTVERYNPENNTWTLIAPM 456
Cdd:pfam13418   2 RAYHTSTSIPDDTIYLFGG-EGEDGtlLSDLWVFDLSTNEWTRLGSL 47
Kelch_6 pfam13964
Kelch motif;
459-507 1.03e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 37.31  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217263266 459 ARRGAGVAVLNGKLFVCGGFDGSH-AISCVEMYDPTRNEWKMMGNMTSPR 507
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNASpALNKLEVYNPLTKSWEELPPLPTPR 50
BACK_KLHL30 cd18469
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 30 (KLHL30); KLHL30 belongs ...
 39-132 1.19e-03

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 30 (KLHL30); KLHL30 belongs to the KLHL family. Its function remains unclear. Differential expression of the KLHL30 gene has been observed in glioblastoma multiforme versus normal brain.


Pssm-ID: 350544 [Multi-domain]  Cd Length: 104  Bit Score: 38.58  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  39 RMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVC----LPSNGKlytKVINWVQ 114
Cdd:cd18469     2 QIDATNCLGICEFGETHGCPEVAAKAWSFLLENFEAVSQEEEFLQLEKERLVACLGDDLLqvrdEQSRLE---AVLRWVG 78

                          90
                  ....*....|....*...
gi 2217263266 115 RSIWENGDSLEELMEEVQ 132
Cdd:cd18469    79 HDPQARAAHLPELLSLVH 96
Kelch_4 pfam13418
Galactose oxidase, central domain;
506-546 1.26e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.82  E-value: 1.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217263266 506 PRSN-AGIATVGNTIYAVGGFDGN-EFLNTVEVYNLESNEWSP 546
Cdd:pfam13418   1 PRAYhTSTSIPDDTIYLFGGEGEDgTLLSDLWVFDLSTNEWTR 43
BACK_KLHL27_IPP cd18466
BACK (BTB and C-terminal Kelch) domain found in intracisternal A particle-promoted polypeptide ...
 40-132 1.46e-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: 38.23  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSIW 118
Cdd:cd18466     1 IDPANCIGIFQFSEQIACHDLLEFTENYIHVHFLEVQSGEEFLGLTKDQLvKILRSEELSIEDEYQVFTAAMEWILKDVG 80

                          90
                  ....*....|....
gi 2217263266 119 ENGDSLEELMEEVQ 132
Cdd:cd18466    81 KRKKHVVEVLEPVR 94
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 506-546 2.05e-03

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


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 36.16  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217263266 506 PRSNAGIATVGNTIYAVGGFDGN--EFLNTVEVYNLESNEWSP 546
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDGLgdLSSSDVLVYDPETNVWTE 43
BACK_KLHL24 cd18463
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 24 (KLHL24); KLHL24, also ...
 39-115 2.23e-03

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 24 (KLHL24); KLHL24, also called kainate receptor-interacting protein for GluR6 (KRIP6), or protein DRE1, is necessary to maintain the balance between intermediate filament stability and degradation, a process that is essential for skin integrity. KLHL24 is a component of the BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates ubiquitination of KRT14 and controls its levels during keratinocyte differentiation.


Pssm-ID: 350538 [Multi-domain]  Cd Length: 78  Bit Score: 36.99  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217263266  39 RMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVML-EDNVCLPSNGKLYTKVINWVQR 115
Cdd:cd18463     1 QLDPCNCLGIQKFADTHSLKQLFEKCKKFALENFVEVSQHEEFLELCKDELIEYIsNDELVVPKEEEVFEAVMRWVYH 78
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 412-456 2.33e-03

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


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 36.16  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217263266 412 RRHQSAVCELGGYLYIIGGA-ESWNC-LNTVERYNPENNTWTLIAPM 456
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSdGLGDLsSSDVLVYDPETNVWTEVPRL 47
Kelch_4 pfam13418
Galactose oxidase, central domain;
364-409 2.66e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217263266 364 RCNAGVCAL-NGKLYIVGGSDPYGqKGLKNCDVFDPVTKLWTSCAPL 409
Cdd:pfam13418   2 RAYHTSTSIpDDTIYLFGGEGEDG-TLLSDLWVFDLSTNEWTRLGSL 47
BACK_KLHL31_KBTBD1 cd18470
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 31 (KLHL31); KLHL31, also ...
 40-114 3.44e-03

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 31 (KLHL31); KLHL31, also termed BTB and kelch domain-containing protein 6, or Kelch repeat and BTB domain-containing protein 1, or Kelch-like protein KLHL, is a transcriptional repressor in MAPK/JNK signaling pathway that regulates cellular functions. Overexpression inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE).


Pssm-ID: 350545  Cd Length: 98  Bit Score: 37.16  E-value: 3.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQ 114
Cdd:cd18470     1 INVENCMYVVNIAETYGLKNTKEAAQKFIRDNFIEFSETDQFLKLTFEQInEFLIDDDLQLPSEITAFQIAMKWLD 76
BACK_KLHL28_BTBD5 cd18467
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 28 (KLHL28); KLHL28, also ...
 40-132 3.45e-03

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: 37.23  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSIW 118
Cdd:cd18467     1 LDPGNCIGISRFAETYGCHDLYLAANKYICQNFEDVCQTEEFFELTHAELdEIVSNDCLNVVTEETVFYALESWIKYDVQ 80

                          90
                  ....*....|....
gi 2217263266 119 ENGDSLEELMEEVQ 132
Cdd:cd18467    81 ERQKYLAQLLHCVR 94
Kelch_3 pfam13415
Galactose oxidase, central domain;
469-513 6.37e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 34.96  E-value: 6.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217263266 469 NGKLFVCGG--FDGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIA 513
Cdd:pfam13415   1 GDKLYIFGGlgFDGQTRLNDLYVYDLDTNTWTQIGDLPPPRSGHSAT 47
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 460-498 6.95e-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: 34.62  E-value: 6.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217263266 460 RRGAGVAVLNGKLFVCGGFDGSHAISCVEM--YDPTRNEWK 498
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGSDGLGDLSSSDVlvYDPETNVWT 42
BACK_KBTBD6_7 cd18482
BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing ...
 40-132 8.76e-03

BACK (BTB and C-terminal Kelch) domain found in Kelch repeat and BTB domain-containing proteins, KBTBD6 and KBTBD7; KBTBD6 and KBTBD7 are substrate adaptors of a cullin-3 RING ubiquitin ligase complex that mediates ubiquitylation and proteasomal degradation of T-lymphoma and metastasis gene 1 (TIAM1), a RAC1-specific guanine exchange factor (GEF), by cooperating with gamma-aminobutyric acid receptor-associated proteins (GABARAP). KBTBD7 may also act as a new transcriptional activator in mitogen-activated protein kinase (MAPK) signaling.


Pssm-ID: 350557 [Multi-domain]  Cd Length: 99  Bit Score: 35.94  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217263266  40 MDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQIS-EEEEFLKLPRLKL-EVMLEDNVCLPSNGKLYTKVINWVQRSI 117
Cdd:cd18482     1 LDLSNCAGILKFADAFDNRELKSKALAFIARNFQQLLaKEEELCELSLAQLkEVLMLDSLDVDSERKVCSVAVQWIEANL 80

                          90
                  ....*....|....*
gi 2217263266 118 WENGDSLEELMEEVQ 132
Cdd:cd18482    81 KERAASAAEVLKCVR 95
BACK_KLHL6 cd18446
BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 6 (KLHL6); KLHL6 is a ...
 60-132 9.28e-03

BACK (BTB and C-terminal Kelch) domain found in Kelch-like protein 6 (KLHL6); KLHL6 is a BTB-kelch protein with a lymphoid tissue-restricted expression pattern. It belongs to the KLHL gene family, which is composed of an N-terminal BTB-POZ domain and four to six Kelch motifs in tandem. It is involved in B-lymphocyte antigen receptor signaling and germinal center formation.


Pssm-ID: 350521 [Multi-domain]  Cd Length: 108  Bit Score: 36.29  E-value: 9.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217263266  60 LLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLE-DNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQ 132
Cdd:cd18446    21 LKKQVQNYIIQNFSQVLNHEEFLELPVDILCHILKsDDLYVTEEEQVFETVMRWVRYKESERLPLLPRVLENVR 94
 
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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