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Conserved domains on  [gi|568996059|ref|XP_006522540|]
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leucine-zipper-like transcriptional regulator 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BTB1_POZ_LZTR1 cd18308
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 417-568 1.85e-86

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas. LZTR-1 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


:

Pssm-ID: 349617 [Multi-domain]  Cd Length: 156  Bit Score: 268.47  E-value: 1.85e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 417 QFSCYPKCTLHEDYGRLWEGRQFCDVEFVLGEKEECVQGHVAIVTARSRWLRRKIVQAQEWLAQKLEEDGALAPKEAPGP 496
Cdd:cd18308    1 QFSSYPKCTLHDDFGRLLESRQFCDVEFIVGEEEERIPAHIAFVAARSKWLRNKILQARERQKQKAEQEVEDEGSEADSS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568996059 497 AVGRARPPLLRVAIREAEARPFEVLMQFLYTDKIKYPRKG----HVEDVLLIMDVYKLALSFQLCRLEQLCRQYIE 568
Cdd:cd18308   81 SASKNDSPMLEVRLPEADPEAFELILSFIYTDKIDPTRKGqdpgSNEVVLLMMDVYRLALQFQMSRLEQLCVQYLE 156
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
51-417 2.80e-32

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 126.42  E-value: 2.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  51 WRRLPPcdeFVGARRSkHTVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWcraFTTGTPPAPRYHHSA-VVYGSSMFV 129
Cdd:COG3055    3 WSSLPD---LPTPRSE-AAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTW---SELAPLPGPPRHHAAaVAQDGKLYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 130 FGGYTGDIYSNSNLknkNDLFEYKFATGQWTEwkiEGRLPVARSAHGATVYSDKLWIFAGYDGNARLNDMWtigLQDREL 209
Cdd:COG3055   76 FGGFTGANPSSTPL---NDVYVYDPATNTWTK---LAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVE---VYDPAT 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 210 TCWEEVAqsgEIPPSCCNFPVAVCRD-KMFVFSGQSGakitnnlfqfEFKDKTWTRIptehllrgsPPPPQRRYGHTMVA 288
Cdd:COG3055  147 GTWTQLA---PLPTPRDHLAAAVLPDgKILVIGGRNG----------SGFSNTWTTL---------APLPTARAGHAAAV 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 289 FDRHLYVFGGaaDNTLPNELHCYDVDFQTWEVVqpssdsevggaemperasssedastltseerssfkksrdvfgldfgt 368
Cdd:COG3055  205 LGGKILVFGG--ESGFSDEVEAYDPATNTWTAL----------------------------------------------- 235

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568996059 369 tsakqpvhlaSELPSGRLFHAAAVISDAMYIFGGTVDNNIRSGEMYRFQ 417
Cdd:COG3055  236 ----------GELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLVTSAE 274
BACK1_LZTR1 cd18505
first BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional ...
 572-630 3.38e-32

first BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a Golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas.


:

Pssm-ID: 350580  Cd Length: 59  Bit Score: 118.54  E-value: 3.38e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568996059 572 DLQNVLVVCESAARLQLGQLKEHCLNFIVKESHFNQVIMMKEFERLSSPLIVEIVRRKQ 630
Cdd:cd18505    1 NVRNVLVALENASKLNLDQLKEHCLNFIVKESNYNQIVMSKEFEHLDQPLMVEIVRRRQ 59
BTB_POZ super family cl38908
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 644-686 6.03e-20

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 cd18309:

Pssm-ID: 453885 [Multi-domain]  Cd Length: 126  Bit Score: 85.90  E-value: 6.03e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568996059 644 IGTSLIQDMKAYLEGAGSEFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18309    1 IGTTLEQDMEAFLESVGGDFCDITLLLDGHPIPAHKAILAARC 43
 
Name Accession Description Interval E-value
BTB1_POZ_LZTR1 cd18308
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 417-568 1.85e-86

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas. LZTR-1 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349617 [Multi-domain]  Cd Length: 156  Bit Score: 268.47  E-value: 1.85e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 417 QFSCYPKCTLHEDYGRLWEGRQFCDVEFVLGEKEECVQGHVAIVTARSRWLRRKIVQAQEWLAQKLEEDGALAPKEAPGP 496
Cdd:cd18308    1 QFSSYPKCTLHDDFGRLLESRQFCDVEFIVGEEEERIPAHIAFVAARSKWLRNKILQARERQKQKAEQEVEDEGSEADSS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568996059 497 AVGRARPPLLRVAIREAEARPFEVLMQFLYTDKIKYPRKG----HVEDVLLIMDVYKLALSFQLCRLEQLCRQYIE 568
Cdd:cd18308   81 SASKNDSPMLEVRLPEADPEAFELILSFIYTDKIDPTRKGqdpgSNEVVLLMMDVYRLALQFQMSRLEQLCVQYLE 156
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
51-417 2.80e-32

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 126.42  E-value: 2.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  51 WRRLPPcdeFVGARRSkHTVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWcraFTTGTPPAPRYHHSA-VVYGSSMFV 129
Cdd:COG3055    3 WSSLPD---LPTPRSE-AAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTW---SELAPLPGPPRHHAAaVAQDGKLYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 130 FGGYTGDIYSNSNLknkNDLFEYKFATGQWTEwkiEGRLPVARSAHGATVYSDKLWIFAGYDGNARLNDMWtigLQDREL 209
Cdd:COG3055   76 FGGFTGANPSSTPL---NDVYVYDPATNTWTK---LAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVE---VYDPAT 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 210 TCWEEVAqsgEIPPSCCNFPVAVCRD-KMFVFSGQSGakitnnlfqfEFKDKTWTRIptehllrgsPPPPQRRYGHTMVA 288
Cdd:COG3055  147 GTWTQLA---PLPTPRDHLAAAVLPDgKILVIGGRNG----------SGFSNTWTTL---------APLPTARAGHAAAV 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 289 FDRHLYVFGGaaDNTLPNELHCYDVDFQTWEVVqpssdsevggaemperasssedastltseerssfkksrdvfgldfgt 368
Cdd:COG3055  205 LGGKILVFGG--ESGFSDEVEAYDPATNTWTAL----------------------------------------------- 235

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568996059 369 tsakqpvhlaSELPSGRLFHAAAVISDAMYIFGGTVDNNIRSGEMYRFQ 417
Cdd:COG3055  236 ----------GELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLVTSAE 274
BACK1_LZTR1 cd18505
first BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional ...
 572-630 3.38e-32

first BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a Golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas.


Pssm-ID: 350580  Cd Length: 59  Bit Score: 118.54  E-value: 3.38e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568996059 572 DLQNVLVVCESAARLQLGQLKEHCLNFIVKESHFNQVIMMKEFERLSSPLIVEIVRRKQ 630
Cdd:cd18505    1 NVRNVLVALENASKLNLDQLKEHCLNFIVKESNYNQIVMSKEFEHLDQPLMVEIVRRRQ 59
BTB2_POZ_LZTR1 cd18309
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 644-686 6.03e-20

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas. LZTR-1 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349618 [Multi-domain]  Cd Length: 126  Bit Score: 85.90  E-value: 6.03e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568996059 644 IGTSLIQDMKAYLEGAGSEFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18309    1 IGTTLEQDMEAFLESVGGDFCDITLLLDGHPIPAHKAILAARC 43
PLN02153 PLN02153
epithiospecifier protein
 65-347 4.15e-11

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 65.01  E-value: 4.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  65 RSKHTVVAYKDAIYVFGGD--NGKTMLNDLLRFDVKDCSWCRAFTTGTPPA-PRYHHSAVVYGSSMFVFGGytgdiySNS 141
Cdd:PLN02153  23 RCSHGIAVVGDKLYSFGGElkPNEHIDKDLYVFDFNTHTWSIAPANGDVPRiSCLGVRMVAVGTKLYIFGG------RDE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 142 NlKNKNDLFEYKFATGQW---TEWKIEGRlPVARSAHGATVYSDKLWIFAGYDGNARLND---MWTIGLQDRELTCWEEV 215
Cdd:PLN02153  97 K-REFSDFYSYDTVKNEWtflTKLDEEGG-PEARTFHSMASDENHVYVFGGVSKGGLMKTperFRTIEAYNIADGKWVQL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 216 AQSGEippsccNFP------VAVCRDKMFVFSGQSGAKI--------TNNLFQFEFKDKTWTRIPTEhllrGSPPPPQRR 281
Cdd:PLN02153 175 PDPGE------NFEkrggagFAVVQGKIWVVYGFATSILpggksdyeSNAVQFFDPASGKWTEVETT----GAKPSARSV 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568996059 282 YGHTMVAfdRHLYVFGGA---------ADNTLPNELHCYDVDFQTWEVVqpssdSEVGGAEMPeRASSSEDASTL 347
Cdd:PLN02153 245 FAHAVVG--KYIIIFGGEvwpdlkghlGPGTLSNEGYALDTETLVWEKL-----GECGEPAMP-RGWTAYTTATV 311
mutarot_permut TIGR03548
cyclically-permuted mutarotase family protein; Members of this protein family show essentially ...
 158-328 1.61e-07

cyclically-permuted mutarotase family protein; Members of this protein family show essentially full-length homology, cyclically permuted, to YjhT from Escherichia coli. YjhT was shown to act as a mutarotase for sialic acid, and by this ability to be able to act as a virulence factor. Members of the YjhT family (TIGR03547) and this cyclically-permuted family have multiple repeats of the beta-propeller-forming Kelch repeat.


Pssm-ID: 274642 [Multi-domain]  Cd Length: 331  Bit Score: 53.64  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  158 QWTEwkiEGRLPVArSAHGATVYSDKLWIFAG-YDGNARLNDMWTIGLQDRELTCWEEVAqsGEIPPSCCNFPVAVCRDK 236
Cdd:TIGR03548  53 KWVK---AGQLPYE-IAYGASVSTPYGIYYVGgSPSSESFSDVLLLSLDDTKEALIIETL--PSLPVAFDNGSATYKDGK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  237 MFVFSGQSGAKITNNLFQFEFKDKT--WTRIPTEhllrgsppPPQRRYGHTMVAFDRHLYVFGGAA---DNTLPNELHCY 311
Cdd:TIGR03548 127 IYVGGGNANGKPSNKFYCLDLSNDTsgWEELPEF--------PGEARVQPVCQALHGKLYVFGGFQlggDAIIYTDGYAY 198

                         170
                  ....*....|....*....
gi 568996059  312 DVDFQTWEVVQ--PSSDSE 328
Cdd:TIGR03548 199 SPKTNTWQTVAdpVLSDGE 217
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 280-323 7.81e-07

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: 46.07  E-value: 7.81e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568996059  280 RRYGHTMVAFDRHLYVFGGAADNTLPNELHCYDVDFQTWEVVQP 323
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 662-686 5.11e-06

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 45.71  E-value: 5.11e-06
                          10        20
                  ....*....|....*....|....*
gi 568996059  662 EFCDITLLLDGQPRPAHKAILAARS 686
Cdd:pfam00651   9 ELCDVTLVVGDKEFRAHKAVLAACS 33
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 430-570 3.47e-05

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 43.40  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  430 YGRLWEGRQFCDVEFVLGEKEecVQGHVAIVTARSRWLRRKivqaqewLAQKLEEDgalapkeapgpavgrarpPLLRVA 509
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKE--FRAHKAVLAACSPYFKAL-------FSGQESES------------------SVSEIT 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996059  510 IREAEARPFEVLMQFLYTDKIKYPRKghvedvllIMDVYKLALSFQLCRLEQLCRQYIEAS 570
Cdd:pfam00651  54 LDDVSPEDFEALLEFMYTGKLISEEN--------VDDLLAAADKLQIPSLVDKCEEFLIKS 106
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
 576-628 3.47e-03

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: 37.32  E-value: 3.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568996059   576 VLVVCESAARLQLGQLKEHCLNFIVKesHFNQVIMMKEFERLSSPLIVEIVRR 628
Cdd:smart00875   1 CLGIRRFADAHGLEELAEKALRFILQ--NFSEVSSSEEFLELPLEQLLELLSS 51
Kelch smart00612
Kelch domain;
77-124 9.48e-03

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 34.84  E-value: 9.48e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568996059    77 IYVFGGDNGKTMLNDLLRFDVKDCSWcrafTTGTP-PAPRYHHSAVVYG 124
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKW----TPLPSmPTPRSGHGVAVIN 46
 
Name Accession Description Interval E-value
BTB1_POZ_LZTR1 cd18308
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 417-568 1.85e-86

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas. LZTR-1 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349617 [Multi-domain]  Cd Length: 156  Bit Score: 268.47  E-value: 1.85e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 417 QFSCYPKCTLHEDYGRLWEGRQFCDVEFVLGEKEECVQGHVAIVTARSRWLRRKIVQAQEWLAQKLEEDGALAPKEAPGP 496
Cdd:cd18308    1 QFSSYPKCTLHDDFGRLLESRQFCDVEFIVGEEEERIPAHIAFVAARSKWLRNKILQARERQKQKAEQEVEDEGSEADSS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568996059 497 AVGRARPPLLRVAIREAEARPFEVLMQFLYTDKIKYPRKG----HVEDVLLIMDVYKLALSFQLCRLEQLCRQYIE 568
Cdd:cd18308   81 SASKNDSPMLEVRLPEADPEAFELILSFIYTDKIDPTRKGqdpgSNEVVLLMMDVYRLALQFQMSRLEQLCVQYLE 156
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
51-417 2.80e-32

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 126.42  E-value: 2.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  51 WRRLPPcdeFVGARRSkHTVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWcraFTTGTPPAPRYHHSA-VVYGSSMFV 129
Cdd:COG3055    3 WSSLPD---LPTPRSE-AAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTW---SELAPLPGPPRHHAAaVAQDGKLYV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 130 FGGYTGDIYSNSNLknkNDLFEYKFATGQWTEwkiEGRLPVARSAHGATVYSDKLWIFAGYDGNARLNDMWtigLQDREL 209
Cdd:COG3055   76 FGGFTGANPSSTPL---NDVYVYDPATNTWTK---LAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVE---VYDPAT 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 210 TCWEEVAqsgEIPPSCCNFPVAVCRD-KMFVFSGQSGakitnnlfqfEFKDKTWTRIptehllrgsPPPPQRRYGHTMVA 288
Cdd:COG3055  147 GTWTQLA---PLPTPRDHLAAAVLPDgKILVIGGRNG----------SGFSNTWTTL---------APLPTARAGHAAAV 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 289 FDRHLYVFGGaaDNTLPNELHCYDVDFQTWEVVqpssdsevggaemperasssedastltseerssfkksrdvfgldfgt 368
Cdd:COG3055  205 LGGKILVFGG--ESGFSDEVEAYDPATNTWTAL----------------------------------------------- 235

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 568996059 369 tsakqpvhlaSELPSGRLFHAAAVISDAMYIFGGTVDNNIRSGEMYRFQ 417
Cdd:COG3055  236 ----------GELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLVTSAE 274
BACK1_LZTR1 cd18505
first BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional ...
 572-630 3.38e-32

first BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a Golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas.


Pssm-ID: 350580  Cd Length: 59  Bit Score: 118.54  E-value: 3.38e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568996059 572 DLQNVLVVCESAARLQLGQLKEHCLNFIVKESHFNQVIMMKEFERLSSPLIVEIVRRKQ 630
Cdd:cd18505    1 NVRNVLVALENASKLNLDQLKEHCLNFIVKESNYNQIVMSKEFEHLDQPLMVEIVRRRQ 59
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
50-302 2.36e-31

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 123.73  E-value: 2.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  50 RWRRLPPcdeFVGARRSKHTVVAYKDAIYVFGGDNGK----TMLNDLLRFDVKDCSWcraFTTGTPPAPRYHHSAVVYGS 125
Cdd:COG3055   49 TWSELAP---LPGPPRHHAAAVAQDGKLYVFGGFTGAnpssTPLNDVYVYDPATNTW---TKLAPMPTPRGGATALLLDG 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 126 SMFVFGGYTGDiysnsnlKNKNDLFEYKFATGQWTEwkiEGRLPVARSAHGATV-YSDKLWIFAGYDGNARlNDMWTIGl 204
Cdd:COG3055  123 KIYVVGGWDDG-------GNVAWVEVYDPATGTWTQ---LAPLPTPRDHLAAAVlPDGKILVIGGRNGSGF-SNTWTTL- 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 205 qdreltcweevaqsGEIPPSCCNFPVAVCRDKMFVFSGQSGAkiTNNLFQFEFKDKTWTRIPtehllrgspPPPQRRYGH 284
Cdd:COG3055  191 --------------APLPTARAGHAAAVLGGKILVFGGESGF--SDEVEAYDPATNTWTALG---------ELPTPRHGH 245

                        250
                 ....*....|....*...
gi 568996059 285 TMVAFDRHLYVFGGAADN 302
Cdd:COG3055  246 AAVLTDGKVYVIGGETKP 263
BTB2_POZ_LZTR1 cd18309
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 644-686 6.03e-20

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas. LZTR-1 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349618 [Multi-domain]  Cd Length: 126  Bit Score: 85.90  E-value: 6.03e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568996059 644 IGTSLIQDMKAYLEGAGSEFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18309    1 IGTTLEQDMEAFLESVGGDFCDITLLLDGHPIPAHKAILAARC 43
PLN02153 PLN02153
epithiospecifier protein
 65-347 4.15e-11

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 65.01  E-value: 4.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  65 RSKHTVVAYKDAIYVFGGD--NGKTMLNDLLRFDVKDCSWCRAFTTGTPPA-PRYHHSAVVYGSSMFVFGGytgdiySNS 141
Cdd:PLN02153  23 RCSHGIAVVGDKLYSFGGElkPNEHIDKDLYVFDFNTHTWSIAPANGDVPRiSCLGVRMVAVGTKLYIFGG------RDE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 142 NlKNKNDLFEYKFATGQW---TEWKIEGRlPVARSAHGATVYSDKLWIFAGYDGNARLND---MWTIGLQDRELTCWEEV 215
Cdd:PLN02153  97 K-REFSDFYSYDTVKNEWtflTKLDEEGG-PEARTFHSMASDENHVYVFGGVSKGGLMKTperFRTIEAYNIADGKWVQL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 216 AQSGEippsccNFP------VAVCRDKMFVFSGQSGAKI--------TNNLFQFEFKDKTWTRIPTEhllrGSPPPPQRR 281
Cdd:PLN02153 175 PDPGE------NFEkrggagFAVVQGKIWVVYGFATSILpggksdyeSNAVQFFDPASGKWTEVETT----GAKPSARSV 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568996059 282 YGHTMVAfdRHLYVFGGA---------ADNTLPNELHCYDVDFQTWEVVqpssdSEVGGAEMPeRASSSEDASTL 347
Cdd:PLN02153 245 FAHAVVG--KYIIIFGGEvwpdlkghlGPGTLSNEGYALDTETLVWEKL-----GECGEPAMP-RGWTAYTTATV 311
PLN02153 PLN02153
epithiospecifier protein
 157-404 4.76e-09

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 58.46  E-value: 4.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 157 GQWTewKIE---GRLPVARSAHGATVYSDKLWIFAG-YDGNARLN-DMWTIglqDRELTCWEEVAQSGEIPP-SCCNFPV 230
Cdd:PLN02153   7 GGWI--KVEqkgGKGPGPRCSHGIAVVGDKLYSFGGeLKPNEHIDkDLYVF---DFNTHTWSIAPANGDVPRiSCLGVRM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 231 AVCRDKMFVFSGQSGAKITNNLFQFEFKDKTWTRIPTEHLLRGspppPQRRYGHTMVAFDRHLYVFGGAADNTLPN---- 306
Cdd:PLN02153  82 VAVGTKLYIFGGRDEKREFSDFYSYDTVKNEWTFLTKLDEEGG----PEARTFHSMASDENHVYVFGGVSKGGLMKtper 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 307 --ELHCYDVDFQTW-EVVQPSSDSEV-GGAEMPERASS----SEDASTLTSEERSSFKKSRDVFgldFGTTSAK-QPVHL 377
Cdd:PLN02153 158 frTIEAYNIADGKWvQLPDPGENFEKrGGAGFAVVQGKiwvvYGFATSILPGGKSDYESNAVQF---FDPASGKwTEVET 234

                        250       260
                 ....*....|....*....|....*..
gi 568996059 378 ASELPSGRLFHAAAVISDAMYIFGGTV 404
Cdd:PLN02153 235 TGAKPSARSVFAHAVVGKYIIIFGGEV 261
BTB_POZ_SPOPL cd18343
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 422-575 1.32e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein-like (SPOPL); SPOPL, also called HIB homolog 2 or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes may contain homodimeric SPOPL or the heterodimers formed by speckle-type POZ protein (SPOP) and SPOPL, which are less efficient than ubiquitin ligase complexes containing only SPOP. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349652 [Multi-domain]  Cd Length: 123  Bit Score: 53.47  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 422 PKCTLHEDYGRLWEGRQFCDVEFVLGEKEecVQGHVAIVTARSrwlrrKIVQAQewLAQKLEEdgalAPKEapgpavgra 501
Cdd:cd18343    4 PECRLAEDLGNLWENSRFTDCSLFVGGQE--FKAHKSILAARS-----PVFNAM--FEHEMEE----SKKN--------- 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996059 502 rppllRVAIREAEARPFEVLMQFLYTDKIkyPRKGHVEDVLLimdvyKLALSFQLCRLEQLCRQYIEASVDLQN 575
Cdd:cd18343   62 -----RVEINDVDPEVFKEMMRFIYTGKA--PNLDKMADNLL-----AAADKYALERLKVMCEEALCNNLSVEN 123
BACK cd14733
BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal ...
 572-628 1.39e-08

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: 51.51  E-value: 1.39e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568996059 572 DLQNVLVVCESAARLQLGQLKEHCLNFIVKesHFNQVIMMKEFERLSSPLIVEIVRR 628
Cdd:cd14733    1 DPENCLGILELADLYNLEELKEKALKFILE--NFEEVSKSEEFLELSVELLLELLSS 55
PLN02153 PLN02153
epithiospecifier protein
 41-220 1.41e-08

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 57.30  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  41 NFGPFETVHR-WRRLPPCDEFVGAR-RSKHTVVAYKDAIYVFGGDNGKTMLNDLLRF------DVKDCSWCRAFTTGTPP 112
Cdd:PLN02153 102 DFYSYDTVKNeWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGGVSKGGLMKTPERFrtieayNIADGKWVQLPDPGENF 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 113 APRYHHS-AVVYGSSMFVFGGYTGDIYSNSNLKNKNDLFEYKFATGQWTEWKIEGRLPVARSAHGATVYSDKLWIFAGY- 190
Cdd:PLN02153 182 EKRGGAGfAVVQGKIWVVYGFATSILPGGKSDYESNAVQFFDPASGKWTEVETTGAKPSARSVFAHAVVGKYIIIFGGEv 261

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568996059 191 --DGNARL------NDMWTIglqDRELTCWEEVAQSGE 220
Cdd:PLN02153 262 wpDLKGHLgpgtlsNEGYAL---DTETLVWEKLGECGE 296
PRK14131 PRK14131
N-acetylneuraminate epimerase;
50-189 4.75e-08

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 55.79  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  50 RWRRLPpcdEFVGARRSKHTVVAYKDAIYVFGGdNGKT-------MLNDLLRFDVKDCSWCRAFTTgtppAPRY---HHS 119
Cdd:PRK14131  63 GWTKIA---AFPGGPREQAVAAFIDGKLYVFGG-IGKTnsegspqVFDDVYKYDPKTNSWQKLDTR----SPVGlagHVA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 120 AVVYGSSMFVFGGYTGDIY-----------SNSNLKNK--NDLFEYKFATGQWT-----------EWKIEGRLPVARSAH 175
Cdd:PRK14131 135 VSLHNGKAYITGGVNKNIFdgyfedlaaagKDKTPKDKinDAYFDKKPEDYFFNkevlsydpstnQWKNAGESPFLGTAG 214

                        170
                 ....*....|....*
gi 568996059 176 GATVYSD-KLWIFAG 189
Cdd:PRK14131 215 SAVVIKGnKLWLING 229
PLN02193 PLN02193
nitrile-specifier protein
 157-318 5.37e-08

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 55.73  E-value: 5.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 157 GQWTEWKIEGRLPVARSAHGATVYSDKLWIFAG-YDGNARLND-MWTIGLQDREltcWEEVAQSGEIPP-SCCNFPVAVC 233
Cdd:PLN02193 151 GKWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGeFTPNQPIDKhLYVFDLETRT---WSISPATGDVPHlSCLGVRMVSI 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 234 RDKMFVFSGQSGAKITNNLFQFEFKDKTWTRI-PTEHllrgSPPPpqrRYGHTMVAFDRHLYVFGGAADNTLPNELHCYD 312
Cdd:PLN02193 228 GSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLtPVEE----GPTP---RSFHSMAADEENVYVFGGVSATARLKTLDSYN 300


                 ....*.
gi 568996059 313 VDFQTW 318
Cdd:PLN02193 301 IVDKKW 306
PLN02153 PLN02153
epithiospecifier protein
 55-243 5.91e-08

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 55.38  E-value: 5.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  55 PPCDEFVGARrskhtVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWcrAFTT-----GTPPApRYHHSAVVYGSSMFV 129
Cdd:PLN02153  71 VPRISCLGVR-----MVAVGTKLYIFGGRDEKREFSDFYSYDTVKNEW--TFLTkldeeGGPEA-RTFHSMASDENHVYV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 130 FGGytgdiYSNSNLKNKNDLFE----YKFATGQWTEWKIEGRLPVARSAHGATVYSDKLWIFAGYDGN---ARLNDMWTI 202
Cdd:PLN02153 143 FGG-----VSKGGLMKTPERFRtieaYNIADGKWVQLPDPGENFEKRGGAGFAVVQGKIWVVYGFATSilpGGKSDYESN 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568996059 203 GLQ--DRELTCWEEVAQSGEIPPSCCNFPVAVCRDKMFVFSGQ 243
Cdd:PLN02153 218 AVQffDPASGKWTEVETTGAKPSARSVFAHAVVGKYIIIFGGE 260
PHA03098 PHA03098
kelch-like protein; Provisional
 65-263 6.58e-08

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 55.54  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  65 RSKHTVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWcraftTGTPP--APRYHHSAVVYGSSMFVFGGytgdIYSNSN 142
Cdd:PHA03098 333 RKNPGVTVFNNRIYVIGGIYNSISLNTVESWKPGESKW-----REEPPliFPRYNPCVVNVNNLIYVIGG----ISKNDE 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 143 LKNKNDLFEYKFatgqwTEWKIEGRLPVARSAHGATVYSDKLWIFAGYDGNARLNDMWTIGLQDRELTCWEEVaqsgeip 222
Cdd:PHA03098 404 LLKTVECFSLNT-----NKWSKGSPLPISHYGGCAIYHDGKIYVIGGISYIDNIKVYNIVESYNPVTNKWTEL------- 471

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568996059 223 pSCCNFP-----VAVCRDKMFVFSGQSGAKITNNLFQFEFKDKTWT 263
Cdd:PHA03098 472 -SSLNFPrinasLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTWT 516
mutarot_permut TIGR03548
cyclically-permuted mutarotase family protein; Members of this protein family show essentially ...
 158-328 1.61e-07

cyclically-permuted mutarotase family protein; Members of this protein family show essentially full-length homology, cyclically permuted, to YjhT from Escherichia coli. YjhT was shown to act as a mutarotase for sialic acid, and by this ability to be able to act as a virulence factor. Members of the YjhT family (TIGR03547) and this cyclically-permuted family have multiple repeats of the beta-propeller-forming Kelch repeat.


Pssm-ID: 274642 [Multi-domain]  Cd Length: 331  Bit Score: 53.64  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  158 QWTEwkiEGRLPVArSAHGATVYSDKLWIFAG-YDGNARLNDMWTIGLQDRELTCWEEVAqsGEIPPSCCNFPVAVCRDK 236
Cdd:TIGR03548  53 KWVK---AGQLPYE-IAYGASVSTPYGIYYVGgSPSSESFSDVLLLSLDDTKEALIIETL--PSLPVAFDNGSATYKDGK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  237 MFVFSGQSGAKITNNLFQFEFKDKT--WTRIPTEhllrgsppPPQRRYGHTMVAFDRHLYVFGGAA---DNTLPNELHCY 311
Cdd:TIGR03548 127 IYVGGGNANGKPSNKFYCLDLSNDTsgWEELPEF--------PGEARVQPVCQALHGKLYVFGGFQlggDAIIYTDGYAY 198

                         170
                  ....*....|....*....
gi 568996059  312 DVDFQTWEVVQ--PSSDSE 328
Cdd:TIGR03548 199 SPKTNTWQTVAdpVLSDGE 217
PLN02193 PLN02193
nitrile-specifier protein
 70-314 1.78e-07

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 54.19  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  70 VVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWCRAFTTGTPPAPRYHHSAVVYGSSMFVFGGYtgdiysnSNLKNKNDL 149
Cdd:PLN02193 224 MVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGV-------SATARLKTL 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 150 FEYKFATGQWTEWKIEGRLPVARSAHGATVYSDKLWIFAGYDGnARLNDMWTIG-LQDReltcWEEVAQSGEIPPSCCNF 228
Cdd:PLN02193 297 DSYNIVDKKWFHCSTPGDSFSIRGGAGLEVVQGKVWVVYGFNG-CEVDDVHYYDpVQDK----WTQVETFGVRPSERSVF 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 229 PVAVCRDKMFVFSGQSG---------AKITNNLFQFEFKDKTWTRIptEHLLRGSPPPPQRRY-GHTMVAFD--RHLYVF 296
Cdd:PLN02193 372 ASAAVGKHIVIFGGEIAmdplahvgpGQLTDGTFALDTETLQWERL--DKFGEEEETPSSRGWtASTTGTIDgkKGLVMH 449

                        250
                 ....*....|....*....
gi 568996059 297 GGAA-DNTLPNELHCYDVD 314
Cdd:PLN02193 450 GGKApTNDRFDDLFFYGID 468
BTB_POZ_SPOP-like cd18279
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 422-564 2.48e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP) and similar proteins; This family includes speckle-type POZ protein (SPOP), speckle-type POZ protein-like (SPOPL), TD and POZ domain-containing proteins (TDPOZ), Drosophila melanogaster protein roadkill and similar proteins. Both, SPOP and SPOPL, serve as adaptors of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and proteasomal degradation of target proteins. TDPOZ is a family of bipartite animal and plant proteins that contain a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domains. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349588 [Multi-domain]  Cd Length: 120  Bit Score: 49.84  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 422 PKCTLHEDYGRLWEGRQFCDVEFVLGEKEecVQGHVAIVTARSRWLRrkivqaqEWLAQKLEEDgalapkeapgpavgra 501
Cdd:cd18279    1 PECRLAEDLGNLWENSRFTDCCLCVGGQE--FQAHKAILAARSPVFS-------AMFEHEMEES---------------- 55

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568996059 502 rpPLLRVAIREAEARPFEVLMQFLYTDKIKYPRKgHVEDVLLIMDVYKLALSFQLCRlEQLCR 564
Cdd:cd18279   56 --KKNRVEINDVDPEVFKEMMRFIYTGKAPNLDK-MADDLLAAADKYALERLKVMCE-DALCS 114
PLN02193 PLN02193
nitrile-specifier protein
 47-220 5.18e-07

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 52.65  E-value: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  47 TVHRWRRLPPCDEfvGAR-RSKHTVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWCRAFTTGTPPAPRYHHSAVVYGS 125
Cdd:PLN02193 252 TTNEWKLLTPVEE--GPTpRSFHSMAADEENVYVFGGVSATARLKTLDSYNIVDKKWFHCSTPGDSFSIRGGAGLEVVQG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 126 SMFVFGGYTGdiysnsnlKNKNDLFEYKFATGQWTEWKIEGRLPVARSAHGATVYSDKLWIFAG--------YDGNARLN 197
Cdd:PLN02193 330 KVWVVYGFNG--------CEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAAVGKHIVIFGGeiamdplaHVGPGQLT 401

                        170       180
                 ....*....|....*....|...
gi 568996059 198 DmWTIGLqDRELTCWEEVAQSGE 220
Cdd:PLN02193 402 D-GTFAL-DTETLQWERLDKFGE 422
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 280-323 7.81e-07

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: 46.07  E-value: 7.81e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568996059  280 RRYGHTMVAFDRHLYVFGGAADNTLPNELHCYDVDFQTWEVVQP 323
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 428-567 8.41e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349603 [Multi-domain]  Cd Length: 111  Bit Score: 48.01  E-value: 8.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 428 EDYGRLWEGRQFCDVEFVLGEKEECVQGHVAIVTARSRWLRRKivqaqewLAQKLEEDGALAPkeapgpavgrarppllr 507
Cdd:cd18294    3 ADMKSLINNPEFSDVKFLVGPERQEIFAHKCILAARCEVFRAM-------FLTGPQKESTQSP----------------- 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 508 VAIREAEARPFEVLMQFLYTDKIKyprkghvEDVLLIMDVYKLALSFQLCRLEQLCRQYI 567
Cdd:cd18294   59 LVLSDIEPEVFRAVLEFIYTNCVT-------LSNHTVIEVLAAAVEYGLDELRKLCERFI 111
BACK2_LZTR1 cd18506
second BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional ...
 571-627 1.36e-06

second BACK (BTB and C-terminal Kelch) domain found in leucine-zipper-like transcriptional regulator 1 (LZTR-1); LZTR-1 is a Golgi BTB-kelch protein that is degraded upon induction of apoptosis. It may also function as a transcriptional regulator that plays a crucial role in embryogenesis. Germline loss-of-function mutations in LZTR-1 predispose to an inherited disorder of multiple schwannomas.


Pssm-ID: 350581  Cd Length: 61  Bit Score: 45.80  E-value: 1.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568996059 571 VDLQNVLVVCESAARLQLGQLKEHCLNFIVKesHFNQVIMMKEFERLSSPLIVEIVR 627
Cdd:cd18506    1 VSFENVLQILEAADKIQALDMKKHALHIIVH--HFPKVARLPKLRSLSRELLLDIID 55
BTB_POZ_BTBD9 cd18287
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 642-686 2.34e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 9 (BTBD9); BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349596 [Multi-domain]  Cd Length: 119  Bit Score: 46.85  E-value: 2.34e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568996059 642 VDIGTSLIQDMKAYLEGagSEFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18287    3 IDHVHFLSEDIGALFLN--EEYSDVTFVVEEKRFPAHRVILAARS 45
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 662-686 5.11e-06

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 45.71  E-value: 5.11e-06
                          10        20
                  ....*....|....*....|....*
gi 568996059  662 EFCDITLLLDGQPRPAHKAILAARS 686
Cdd:pfam00651   9 ELCDVTLVVGDKEFRAHKAVLAACS 33
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 64-105 6.70e-06

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


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 43.37  E-value: 6.70e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568996059   64 RRSKHTVVAYKDAIYVFGGDNGKTMLNDLLRFDVKDCSWCRA 105
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKL 42
PLN02193 PLN02193
nitrile-specifier protein
 209-323 7.60e-06

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 49.18  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 209 LTCWEEVAQSGEIPPSCCNFPVAVCRDKMFVFSGQ--SGAKITNNLFQFEFKDKTWTRIPTEhllrgSPPPPQRRYGHTM 286
Cdd:PLN02193 150 LGKWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEftPNQPIDKHLYVFDLETRTWSISPAT-----GDVPHLSCLGVRM 224

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568996059 287 VAFDRHLYVFGGAADNTLPNELHCYDVDFQTWEVVQP 323
Cdd:PLN02193 225 VSIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTP 261
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 663-686 7.81e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing (ZBTB) proteins, Kelch-like (KLHL) proteins, and similar proteins; This family includes a variety of BTB/POZ domain-containing proteins, such as zinc finger and BTB domain-containing (ZBTB) proteins and Kelch-like (KLHL) proteins. They 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. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349497 [Multi-domain]  Cd Length: 82  Bit Score: 44.47  E-value: 7.81e-06
                         10        20
                 ....*....|....*....|....
gi 568996059 663 FCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18186    1 LCDVTLVVGGREFPAHRAVLAARS 24
Kelch_3 pfam13415
Galactose oxidase, central domain;
74-123 9.07e-06

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 43.05  E-value: 9.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568996059   74 KDAIYVFGG--DNGKTMLNDLLRFDVKDCSWcraFTTGTPPAPRYHHSAVVY 123
Cdd:pfam13415   1 GDKLYIFGGlgFDGQTRLNDLYVYDLDTNTW---TQIGDLPPPRSGHSATYI 49
PLN02153 PLN02153
epithiospecifier protein
 109-327 1.05e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 48.06  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 109 GTPPAPRYHHSAVVYGSSMFVFGgytGDIYSNSNLknKNDLFEYKFATGQWTEWKIEGRLPVArSAHGATVYS--DKLWI 186
Cdd:PLN02153  17 GKGPGPRCSHGIAVVGDKLYSFG---GELKPNEHI--DKDLYVFDFNTHTWSIAPANGDVPRI-SCLGVRMVAvgTKLYI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 187 FAGYDGNARLNDMWTIGLQDRELTCWEEVAQSGEiPPSCCNFPVAVCRDKMFVFSGQS--GAKITNNLFQ----FEFKDK 260
Cdd:PLN02153  91 FGGRDEKREFSDFYSYDTVKNEWTFLTKLDEEGG-PEARTFHSMASDENHVYVFGGVSkgGLMKTPERFRtieaYNIADG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 261 TWTRIPT--EHLlrgsppppQRRYGHTMVAFDRHLYVFGGAADNTLP--------NELHCYDVDFQTWEVVQ-----PSS 325
Cdd:PLN02153 170 KWVQLPDpgENF--------EKRGGAGFAVVQGKIWVVYGFATSILPggksdyesNAVQFFDPASGKWTEVEttgakPSA 241


                 ..
gi 568996059 326 DS 327
Cdd:PLN02153 242 RS 243
Kelch_4 pfam13418
Galactose oxidase, central domain;
64-107 2.96e-05

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 41.83  E-value: 2.96e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568996059   64 RRSKHTVVA-YKDAIYVFGGDNGK-TMLNDLLRFDVKDCSWCRAFT 107
Cdd:pfam13418   1 PRAYHTSTSiPDDTIYLFGGEGEDgTLLSDLWVFDLSTNEWTRLGS 46
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
 430-570 3.47e-05

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 43.40  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059  430 YGRLWEGRQFCDVEFVLGEKEecVQGHVAIVTARSRWLRRKivqaqewLAQKLEEDgalapkeapgpavgrarpPLLRVA 509
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKE--FRAHKAVLAACSPYFKAL-------FSGQESES------------------SVSEIT 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568996059  510 IREAEARPFEVLMQFLYTDKIKYPRKghvedvllIMDVYKLALSFQLCRLEQLCRQYIEAS 570
Cdd:pfam00651  54 LDDVSPEDFEALLEFMYTGKLISEEN--------VDDLLAAADKLQIPSLVDKCEEFLIKS 106
BTB_POZ_roadkill-like cd18345
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 422-576 4.45e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein roadkill and similar proteins; Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349654 [Multi-domain]  Cd Length: 121  Bit Score: 43.30  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 422 PKCTLHEDYGRLWEGRQFCDVEFVLGEKEecVQGHVAIVTARSrwlrrKIVQAQewLAQKLEEDgalapkeapgpavgra 501
Cdd:cd18345    1 PECRLSDDLGLLFERSAFSDVTLCVGGRE--FQAHKAILAARS-----PVFNAM--FEHEMEER---------------- 55

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568996059 502 rpPLLRVAIREAEARPFEVLMQFLYTDKIKYPRKgHVEDVLLIMDVYKLAlsfqlcRLEQLCRQYIEASVDLQNV 576
Cdd:cd18345   56 --KQNRVEITDVDHEVMREMLRFIYTGKAPNLDK-MADDLLAAADKYALE------RLKVMCEEALCSNLSVENV 121
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 112-142 4.53e-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: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 41.01  E-value: 4.53e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568996059  112 PAPRYHHSAVVYGSSMFVFGGYTGDIYSNSN 142
Cdd:pfam13854   1 PVPRYGHCAVTVGDYIYLYGGYTGGEGQPSD 31
PHA02713 PHA02713
hypothetical protein; Provisional
 175-298 5.01e-05

hypothetical protein; Provisional


Pssm-ID: 165086 [Multi-domain]  Cd Length: 557  Bit Score: 46.54  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 175 HGATVYSDKLWIFAGYD-GNARLNDMWTIGLQDRelTCWEevaqsgeIPPSC---CNFPVAVCRDKMFVFSGQSGAKITN 250
Cdd:PHA02713 297 YASAIVDNEIIIAGGYNfNNPSLNKVYKINIENK--IHVE-------LPPMIknrCRFSLAVIDDTIYAIGGQNGTNVER 367

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568996059 251 NLFQFEFKDKTWTRIPtehllrgSPPPPQRRYGhtMVAFDRHLYVFGG 298
Cdd:PHA02713 368 TIECYTMGDDKWKMLP-------DMPIALSSYG--MCVLDQYIYIIGG 406
Kelch_6 pfam13964
Kelch motif;
281-323 5.39e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 41.17  E-value: 5.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568996059  281 RYGHTMVAFDRHLYVFGGAADNTLP-NELHCYDVDFQTWEVVQP 323
Cdd:pfam13964   2 RTFHSVVSVGGYIYVFGGYTNASPAlNKLEVYNPLTKSWEELPP 45
PHA03098 PHA03098
kelch-like protein; Provisional
 176-331 1.02e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 45.53  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996059 176 GATVYSDKLWIFAGYDGNA-RLNDMWTIGLQDREltcWEEVAqsgEIPPSCCNFPVAVCRDKMFVFSGQSGAKITNNLFQ 254
Cdd:PHA03098 289 GSVVLNNVIYFIGGMNKNNlSVNSVVSYDTKTKS---WNKVP---ELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTVES 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568996059 255 FEFKDKTWTRiptehllrgSPPPPQRRYGHTMVAFDRHLYVFGGAADN-TLPNELHCYDVDFQTWEVVQPSSDSEVGG 331
Cdd:PHA03098 363 WKPGESKWRE---------EPPLIFPRYNPCVVNVNNLIYVIGGISKNdELLKTVECFSLNTNKWSKGSPLPISHYGG 431
Kelch_3 pfam13415
Galactose oxidase, central domain;
124-180 1.12e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 39.97  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568996059  124 GSSMFVFGGYTGDiySNSNLknkNDLFEYKFATGQWTEwkIeGRLPVARSAHGATVY 180
Cdd:pfam13415   1 GDKLYIFGGLGFD--GQTRL---NDLYVYDLDTNTWTQ--I-GDLPPPRSGHSATYI 49
BTB_POZ_ZBTB11 cd18202
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 661-686 1.29e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 11 (ZBTB11); ZBTB11 is a transcriptional repressor of TP53. It is critical for basal and emergency granulopoiesis. It regulates neutrophil development through its integrase-like zinc finger domain. ZBTB11 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349511 [Multi-domain]  Cd Length: 118  Bit Score: 42.15  E-value: 1.29e-04
                         10        20
                 ....*....|....*....|....*.
gi 568996059 661 SEFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18202   17 NQFCDVTLLIEGEEYKAHKSVLAANS 42
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 114-161 1.78e-04

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


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 39.52  E-value: 1.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568996059  114 PRYHHSAVVYGSSMFVFGGYTGDIYSNSnlknkndLFEYKFATGQWTE 161
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNS-------VEVYDPETNTWSK 41
Kelch_3 pfam13415
Galactose oxidase, central domain;
234-289 2.57e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 39.20  E-value: 2.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568996059  234 RDKMFVFSG--QSGAKITNNLFQFEFKDKTWTRIptehllrGSPPPPqrRYGHTMVAF 289
Cdd:pfam13415   1 GDKLYIFGGlgFDGQTRLNDLYVYDLDTNTWTQI-------GDLPPP--RSGHSATYI 49
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 225-267 3.38e-04

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


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 38.75  E-value: 3.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568996059  225 CCNFPVAVCRDKMFVFSGQSGAKITNNLFQFEFKDKTWTRIPT 267
Cdd:pfam01344   2 RSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
Kelch_6 pfam13964
Kelch motif;
65-115 3.82e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.86  E-value: 3.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568996059   65 RSKHTVVAYKDAIYVFGG-DNGKTMLNDLLRFDVKDCSWcraFTTGTPPAPR 115
Cdd:pfam13964   2 RTFHSVVSVGGYIYVFGGyTNASPALNKLEVYNPLTKSW---EELPPLPTPR 50
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 648-686 4.32e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349603 [Multi-domain]  Cd Length: 111  Bit Score: 40.31  E-value: 4.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568996059 648 LIQDMKAYLEGagSEFCDITLLL--DGQPRPAHKAILAARS 686
Cdd:cd18294    1 FAADMKSLINN--PEFSDVKFLVgpERQEIFAHKCILAARC 39
BTB_POZ_ABTB2-like cd18297
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 518-575 7.76e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; This family includes ABTB2, BTBD11, plant ARM repeat protein interacting with ABF2 (ARIA), and similar proteins. ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. The BTBD11 gene has been recently identified as an all-trans retinoic acid (atRA)-responsive gene that lies downstream of atRA and its receptors in the regulation of neurite outgrowth and cell adhesion in neural as well as non-neural tissues. ARIA is an armadillo (ARM) repeat and BTB domain-containing protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349606 [Multi-domain]  Cd Length: 117  Bit Score: 39.56  E-value: 7.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568996059 518 FEVLMQFLYTdkikyprkGHVEDVLL----IMDVYKLALSFQLCRLEQLCRQYIEASVDLQN 575
Cdd:cd18297   64 FQLMMQYLYT--------GGVESLDVaqddALELLRAASFFQLDGLKRHCEILLSQQIDLDN 117
Kelch_4 pfam13418
Galactose oxidase, central domain;
114-162 1.14e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 37.21  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568996059  114 PRYHHSAV-VYGSSMFVFGGYtgdiysNSNLKNKNDLFEYKFATGQWTEW 162
Cdd:pfam13418   1 PRAYHTSTsIPDDTIYLFGGE------GEDGTLLSDLWVFDLSTNEWTRL 44
Kelch_4 pfam13418
Galactose oxidase, central domain;
280-324 1.28e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 37.21  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568996059  280 RRYGHTMVAFDRH-LYVFGGA-ADNTLPNELHCYDVDFQTWEVVQPS 324
Cdd:pfam13418   1 PRAYHTSTSIPDDtIYLFGGEgEDGTLLSDLWVFDLSTNEWTRLGSL 47
BTB_POZ_roadkill-like cd18345
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 661-686 1.34e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein roadkill and similar proteins; Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349654 [Multi-domain]  Cd Length: 121  Bit Score: 39.06  E-value: 1.34e-03
                         10        20
                 ....*....|....*....|....*.
gi 568996059 661 SEFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18345   16 SAFSDVTLCVGGREFQAHKAILAARS 41
BTB_POZ_BPM_plant cd18280
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 650-686 1.66e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in plant BTB/POZ-MATH (BPM) protein family; The BPM protein family includes Arabidopsis thaliana BTB/POZ and MATH domain-containing proteins, AtBPM1-6, and similar proteins from other plants. BPM protein, also called protein BTB-POZ and MATH domain, may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349589 [Multi-domain]  Cd Length: 121  Bit Score: 38.85  E-value: 1.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568996059 650 QDMKAYLEGagSEFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18280    3 QHFGALLES--EEGADVTFNVDGEKFRAHKLVLAARS 37
BACK_BTBD19 cd18494
BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 19 (BTBD19); ...
 579-627 2.40e-03

BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB-domain-containing Kelch-like protein. Its function remains unclear.


Pssm-ID: 350569  Cd Length: 73  Bit Score: 37.29  E-value: 2.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568996059 579 VCE---SAARLQLGQLKEHCLNFIvkESHFNQVIMMKEFERLSSPLIVEIVR 627
Cdd:cd18494    5 ACEalqAAVTYGQDELKERCLAFI--EEHTEEVFKTKGFHELSDEALSVILR 54
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
 576-628 3.47e-03

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: 37.32  E-value: 3.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568996059   576 VLVVCESAARLQLGQLKEHCLNFIVKesHFNQVIMMKEFERLSSPLIVEIVRR 628
Cdd:smart00875   1 CLGIRRFADAHGLEELAEKALRFILQ--NFSEVSSSEEFLELPLEQLLELLSS 51
BTB_POZ_KLHL26 cd18255
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 645-686 3.68e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 26 (KLHL26); KLHL26 is encoded by the klhl26 gene, which is regulated by p53 via fuzzy tandem repeats. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349564 [Multi-domain]  Cd Length: 121  Bit Score: 37.76  E-value: 3.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568996059 645 GTSLIQDMKAYLegAGSEFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18255    2 SVTLLQGLNALR--AKGQLLDVTLIADGQRFQAHKVVLASCS 41
Kelch_6 pfam13964
Kelch motif;
114-172 6.65e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 35.39  E-value: 6.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568996059  114 PRYHHSAVVYGSSMFVFGGYTGDIYSnsnlknKNDLFEYKFATGQWTEWkieGRLPVAR 172
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNASPA------LNKLEVYNPLTKSWEEL---PPLPTPR 50
BTB2_POZ_RhoBTB cd18300
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
 518-567 6.65e-03

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, a tandem of 2 BTB domains, and a conserved C-terminal region. In humans, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349609 [Multi-domain]  Cd Length: 108  Bit Score: 36.83  E-value: 6.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568996059 518 FEVLMQFLYTDKIKYPRKGHVedvlliMDVYKLALSFQLCRLEQLCRQYI 567
Cdd:cd18300   61 FLALLEYLYTDQAPILEDGDC------VGLIVLANRLCLPRLVALCEQYI 104
Kelch_4 pfam13418
Galactose oxidase, central domain;
171-218 6.99e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 35.28  E-value: 6.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568996059  171 ARSAHGAT-VYSDKLWIFAGYDGNA-RLNDMWTIGLQDREltcWEEVAQS 218
Cdd:pfam13418   1 PRAYHTSTsIPDDTIYLFGGEGEDGtLLSDLWVFDLSTNE---WTRLGSL 47
BTB_POZ_NS1BP cd18306
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
 662-686 8.44e-03

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: 36.85  E-value: 8.44e-03
                         10        20
                 ....*....|....*....|....*
gi 568996059 662 EFCDITLLLDGQPRPAHKAILAARS 686
Cdd:cd18306   17 QFCDVILQVGGHEIPAHRAVLACAS 41
Kelch smart00612
Kelch domain;
77-124 9.48e-03

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 34.84  E-value: 9.48e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 568996059    77 IYVFGGDNGKTMLNDLLRFDVKDCSWcrafTTGTP-PAPRYHHSAVVYG 124
Cdd:smart00612   2 IYVVGGFDGGQRLKSVEVYDPETNKW----TPLPSmPTPRSGHGVAVIN 46
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 169-201 9.88e-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: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 34.46  E-value: 9.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568996059  169 PVARSAHGATVYSDKLWIFAGYDGNAR--LNDMWT 201
Cdd:pfam13854   1 PVPRYGHCAVTVGDYIYLYGGYTGGEGqpSDDVYV 35
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 114-161 9.91e-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: 9.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568996059  114 PRYHHSAVVYGSSMFVFGGYTGdiysnSNLKNKNDLFEYKFATGQWTE 161
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDG-----LGDLSSSDVLVYDPETNVWTE 43
 
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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