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Conserved domains on  [gi|377836445|ref|XP_003689017|]
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germ cell-less protein-like 2 [Mus musculus]

Protein Classification

BTB/POZ domain-containing protein( domain architecture ID 1000760)

BTB (BR-C, ttk and bab)/POZ (Pox virus and Zinc finger) domain-containing protein 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BTB_POZ super family cl38908
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
80-190 3.97e-44

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 cd18305:

Pssm-ID: 453885 [Multi-domain]  Cd Length: 115  Bit Score: 151.28  E-value: 3.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  80 YQNLFLDGHDSDIKIRALGRTWCLHKVFLCQSGYFANILKGTWRESRHGVINLIIKNEDIDTRSLHFVFGALYRDaDLSI 159
Cdd:cd18305    6 YQTLFLNGENSDITICALGREWKLHKIYLCQSGYFASMFSGSWKESKETVINLEIPDDNITVEALNVVFGSLYRD-EIEI 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 377836445 160 TPLEVPQVLAAACLLRVDRVIQQCEGIMKET 190
Cdd:cd18305   85 KPSRVVSILAAATLLQLDGLIQQCSEVMKET 115
BACK super family cl28903
BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal ...
191-268 8.33e-26

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


The actual alignment was detected with superfamily member cd18495:

Pssm-ID: 475122  Cd Length: 78  Bit Score: 100.40  E-value: 8.33e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 377836445 191 INRNTVCSYYLAAETYRLKAVKTRCFEWLLCNLMVHPSVALYKEVDLKLMYLLALSSDLLVMQKEIDVYTTLKIWMFL 268
Cdd:cd18495    1 ISAKTVCSYYEAACMYGLTEVKKKCLEWLLRNLMTSQNVTLLRELSIELMEQLIASPNLFVMQVEMDVYTLLKKWLFL 78
 
Name Accession Description Interval E-value
BTB_POZ_GCL cd18305
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
80-190 3.97e-44

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein germ cell-less (GCL) and similar proteins; GCL proteins are nuclear envelope proteins highly conserved between the mammalian and Drosophila orthologs. Drosophila melanogaster GCL is a key regulator required for the specification of pole cells and primordial germ cell formation in embryos. Both, human germ cell-less protein-like 1 (GMCL1) and germ cell-less protein-like 2 (GMCL2), also called germ cell-less protein-like 1-like (GMCL1P1 or GMCL1L), may function in spermatogenesis. They may also be substrate-specific adaptors of E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. They contain BTB and BACK domains. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349614 [Multi-domain]  Cd Length: 115  Bit Score: 151.28  E-value: 3.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  80 YQNLFLDGHDSDIKIRALGRTWCLHKVFLCQSGYFANILKGTWRESRHGVINLIIKNEDIDTRSLHFVFGALYRDaDLSI 159
Cdd:cd18305    6 YQTLFLNGENSDITICALGREWKLHKIYLCQSGYFASMFSGSWKESKETVINLEIPDDNITVEALNVVFGSLYRD-EIEI 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 377836445 160 TPLEVPQVLAAACLLRVDRVIQQCEGIMKET 190
Cdd:cd18305   85 KPSRVVSILAAATLLQLDGLIQQCSEVMKET 115
BACK_GCL cd18495
BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster protein germ cell-less ...
191-268 8.33e-26

BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster protein germ cell-less (GCL) and similar proteins; The GCL protein is a nuclear envelope protein highly conserved between the mammalian and Drosophila orthologs. Drosophila melanogaster GCL is a key regulator required for the specification of pole cells and primordial germ cell formation in Drosophila embryos. Both human germ cell-less protein-like 1 (GMCL1) and germ cell-less protein-like 1-like (GMCL1P1 or GMCL1L) may function in spermatogenesis. They may also be substrate-specific adaptors of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.


Pssm-ID: 350570  Cd Length: 78  Bit Score: 100.40  E-value: 8.33e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 377836445 191 INRNTVCSYYLAAETYRLKAVKTRCFEWLLCNLMVHPSVALYKEVDLKLMYLLALSSDLLVMQKEIDVYTTLKIWMFL 268
Cdd:cd18495    1 ISAKTVCSYYEAACMYGLTEVKKKCLEWLLRNLMTSQNVTLLRELSIELMEQLIASPNLFVMQVEMDVYTLLKKWLFL 78
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
80-191 1.09e-10

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: 58.42  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445   80 YQNLFLDGHDSDIKIRALGRTWCLHKVFLC-QSGYFANILKGTWRESRHGVINLiiknEDIDTRSLHFVFGALYRDAdlS 158
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKEFRAHKAVLAaCSPYFKALFSGQESESSVSEITL----DDVSPEDFEALLEFMYTGK--L 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 377836445  159 ITPLEVPQVLAAACLLRVDRVIQQCEGIMKETI 191
Cdd:pfam00651  75 ISEENVDDLLAAADKLQIPSLVDKCEEFLIKSL 107
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
91-191 1.21e-09

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 55.39  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445    91 DIKIRALGRTWCLHKVFLCQ-SGYFANILKGTWRESRHGVINLIikneDIDtrslHFVFGAL---YRDADLSITPLEVPQ 166
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAhSPYFKALFSSDFKESDKSEIYLD----DVS----PEDFRALlnfLYTGKLDLPEENVEE 72
                           90       100
                   ....*....|....*....|....*
gi 377836445   167 VLAAACLLRVDRVIQQCEGIMKETI 191
Cdd:smart00225  73 LLELADYLQIPGLVELCEEFLLKLL 97
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
196-266 7.56e-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: 36.17  E-value: 7.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 377836445   196 VCSYYLAAETYRLKAVKTRCFEWLLCNLMVHPSVALYKEVDLKLMYLLaLSSDLLVMQKEIDVYTTLKIWM 266
Cdd:smart00875   1 CLGIRRFADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLEL-LSSDDLNVSSEEEVFEAVLRWV 70
 
Name Accession Description Interval E-value
BTB_POZ_GCL cd18305
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
80-190 3.97e-44

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein germ cell-less (GCL) and similar proteins; GCL proteins are nuclear envelope proteins highly conserved between the mammalian and Drosophila orthologs. Drosophila melanogaster GCL is a key regulator required for the specification of pole cells and primordial germ cell formation in embryos. Both, human germ cell-less protein-like 1 (GMCL1) and germ cell-less protein-like 2 (GMCL2), also called germ cell-less protein-like 1-like (GMCL1P1 or GMCL1L), may function in spermatogenesis. They may also be substrate-specific adaptors of E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. They contain BTB and BACK domains. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349614 [Multi-domain]  Cd Length: 115  Bit Score: 151.28  E-value: 3.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  80 YQNLFLDGHDSDIKIRALGRTWCLHKVFLCQSGYFANILKGTWRESRHGVINLIIKNEDIDTRSLHFVFGALYRDaDLSI 159
Cdd:cd18305    6 YQTLFLNGENSDITICALGREWKLHKIYLCQSGYFASMFSGSWKESKETVINLEIPDDNITVEALNVVFGSLYRD-EIEI 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 377836445 160 TPLEVPQVLAAACLLRVDRVIQQCEGIMKET 190
Cdd:cd18305   85 KPSRVVSILAAATLLQLDGLIQQCSEVMKET 115
BACK_GCL cd18495
BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster protein germ cell-less ...
191-268 8.33e-26

BACK (BTB and C-terminal Kelch) domain found in Drosophila melanogaster protein germ cell-less (GCL) and similar proteins; The GCL protein is a nuclear envelope protein highly conserved between the mammalian and Drosophila orthologs. Drosophila melanogaster GCL is a key regulator required for the specification of pole cells and primordial germ cell formation in Drosophila embryos. Both human germ cell-less protein-like 1 (GMCL1) and germ cell-less protein-like 1-like (GMCL1P1 or GMCL1L) may function in spermatogenesis. They may also be substrate-specific adaptors of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.


Pssm-ID: 350570  Cd Length: 78  Bit Score: 100.40  E-value: 8.33e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 377836445 191 INRNTVCSYYLAAETYRLKAVKTRCFEWLLCNLMVHPSVALYKEVDLKLMYLLALSSDLLVMQKEIDVYTTLKIWMFL 268
Cdd:cd18495    1 ISAKTVCSYYEAACMYGLTEVKKKCLEWLLRNLMTSQNVTLLRELSIELMEQLIASPNLFVMQVEMDVYTLLKKWLFL 78
BTB_POZ_BTBD16 cd18291
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
90-199 1.92e-13

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 16 (BTBD16); BTBD16 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: 349600  Cd Length: 114  Bit Score: 66.70  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  90 SDIKIRALGRTWCLHKVFLCQSGYFANILKGTwresrhgVINLIIKNEDIDTRSLHFVFGALYRdADLSITPLEVPQVLA 169
Cdd:cd18291   13 PDVVLECLGSFWELHSPYLCKSETLAELLKPV-------TISLNINDPLVTKEAFAVALGNLYN-SEVEVNVEDAVGVLA 84
                         90       100       110
                 ....*....|....*....|....*....|
gi 377836445 170 AACLLRVDRVIQQCEGIMKETINRNTVCSY 199
Cdd:cd18291   85 AAALLRFPTLFQKCVKVMISSISSSTVCKF 114
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
80-191 1.09e-10

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: 58.42  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445   80 YQNLFLDGHDSDIKIRALGRTWCLHKVFLC-QSGYFANILKGTWRESRHGVINLiiknEDIDTRSLHFVFGALYRDAdlS 158
Cdd:pfam00651   1 LNELREQGELCDVTLVVGDKEFRAHKAVLAaCSPYFKALFSGQESESSVSEITL----DDVSPEDFEALLEFMYTGK--L 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 377836445  159 ITPLEVPQVLAAACLLRVDRVIQQCEGIMKETI 191
Cdd:pfam00651  75 ISEENVDDLLAAADKLQIPSLVDKCEEFLIKSL 107
BTB2_POZ_BTBD8 cd18286
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
82-177 1.37e-10

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 8 (BTBD8); BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental processes. It may also act as a protein-protein adaptor in a transcription complex and thus be involved in brain development. BTBD8 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: 349595 [Multi-domain]  Cd Length: 121  Bit Score: 58.81  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  82 NLFLDGHDSDIKIRALGRTWCLHKVFLC-QSGYFANILKGTWRESRHGVINL-IIKNEDIdTRSLHFVFGALYrDADLSI 159
Cdd:cd18286   10 QLFLNGEDSDITIKVDGKTFKAHRCILCaRSSYFAAMLSGSWAESNSSEITLtGVSHAAV-SFVLLFIYGGVL-DLPDDV 87
                         90
                 ....*....|....*...
gi 377836445 160 TPLEvpqVLAAACLLRVD 177
Cdd:cd18286   88 NLGE---LLSLADMYGLD 102
BACK_BTBD16 cd18492
BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 16 (BTBD16); ...
191-272 1.92e-10

BACK (BTB and C-terminal Kelch) domain found in BTB/POZ domain-containing protein 16 (BTBD16); BTBD16 is a BTB-domain-containing Kelch-like protein. Its function remains unclear. BTBD16 SNPs may be bipolar disorder (BD) genetic susceptibility variants exhibiting genetic background-dependent effects.


Pssm-ID: 350567  Cd Length: 97  Bit Score: 57.69  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445 191 INRNTVCSYYLAAETYRLKAVKTRCFEWLLCNLMVHPSVALY-KEVDLKLMYLLALSSDLLVMQkEIDVYTTLKIWMFLY 269
Cdd:cd18492    1 IKSSTVCKFHRAACKYKQESLATACERWLELNLVPQLSSQIYlRDLPLELLHKILKSPRLFTFN-EYSLYKTLCYWVFLQ 79

                 ...
gi 377836445 270 LNP 272
Cdd:cd18492   80 LNP 82
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
90-174 9.17e-10

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: 55.25  E-value: 9.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  90 SDIKIRALGRTWCLHKVFLC-QSGYFANILKGTWRESRHGVINLiiknEDIDTRSLHFVFGALYRDaDLSITPLEVPQVL 168
Cdd:cd18186    2 CDVTLVVGGREFPAHRAVLAaRSPYFRAMFSSGMKESSSSEIEL----DDVSPEAFEALLDYIYTG-ELELSEENVEELL 76

                 ....*.
gi 377836445 169 AAACLL 174
Cdd:cd18186   77 AAADKL 82
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
91-191 1.21e-09

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 55.39  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445    91 DIKIRALGRTWCLHKVFLCQ-SGYFANILKGTWRESRHGVINLIikneDIDtrslHFVFGAL---YRDADLSITPLEVPQ 166
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAhSPYFKALFSSDFKESDKSEIYLD----DVS----PEDFRALlnfLYTGKLDLPEENVEE 72
                           90       100
                   ....*....|....*....|....*
gi 377836445   167 VLAAACLLRVDRVIQQCEGIMKETI 191
Cdd:smart00225  73 LLELADYLQIPGLVELCEEFLLKLL 97
BTB_POZ_KLHL34 cd18264
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
80-197 1.29e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 34 (KLHL34); KLHL34 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The methylation status of KLHL34 cg14232291 appears to be predictive of pathologic response to preoperative chemoradiation therapy in rectal cancer patients. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349573 [Multi-domain]  Cd Length: 136  Bit Score: 47.87  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  80 YQNLFLDGHDSDIKIRALGRTWCLHKVFL-CQSGYFANILKGTWRESRHGVINLIIKNEDIDTRSLHFVFGALyrdadLS 158
Cdd:cd18264   19 YQSLRAEGFLCDVVLEAEGNEFPAHRSLLaCSSDYFRALFKDYTQESKARVIHLPVVSAAGLQRVLDFIYTSW-----LS 93
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 377836445 159 ITPLEVPQVLAAACLLRVDRVIQQCEGIMKETINRNTVC 197
Cdd:cd18264   94 LSLDTLEDTLEAASYLQVTEAIGLCSQYLINNLAPENCC 132
BTB_POZ_KLHL8 cd18238
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
91-189 2.07e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 8 (KLHL8); KLHL8 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for the ubiquitination and degradation of rapsyn, a postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. 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: 349547 [Multi-domain]  Cd Length: 120  Bit Score: 43.82  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  91 DIKIRALGRTWCLHKVFL-CQSGYFANILKGTWRESRHGVINLiiknEDIDTRSLHFVFGALYRdADLSITPLEVPQVLA 169
Cdd:cd18238   17 DVTLKVGEKSIHCHRLVLaCVSPYFRAMFTSEMAESKQDSITI----KDIDEEAVELLVDFAYT-GKLTLTVDNVQSLLY 91
                         90       100
                 ....*....|....*....|
gi 377836445 170 AACLLRVDRVIQQCEGIMKE 189
Cdd:cd18238   92 AASLLQVEEVAKACCEFMKD 111
BTB_POZ_ZBTB28_BCL6B cd18332
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
90-183 4.71e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in B-cell CLL/lymphoma 6 member B protein (BCL6B); BCL6B is also called Bcl6-associated zinc finger protein, zinc finger protein 62, or zinc finger and BTB domain-containing protein 28 (ZBTB28). It is a sequence-specific transcriptional repressor in association with BCL-6. It may function in a narrow stage or be related to some events in the early B-cell development. BCL6B plays an important role as a potential tumor suppressor in gastric cancer; it is found preferentially methylated in gastric cancer. It also inhibits both colorectal cancer growth and hepatocellular carcinoma metastases. BCL6B contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349641 [Multi-domain]  Cd Length: 114  Bit Score: 39.84  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  90 SDIKIRALGRTWCLHK-VFLCQSGYFANILKGtwrESRHGVINLIIKnEDIDTRSLHFVFGALYrDADLSITPLEVPQVL 168
Cdd:cd18332   20 TDVTLLVGGTPLRAHKaVLIACSGFFYSIFSG---RVGEGVSVLTLP-SGLEARGFQLLLDFMY-TSRLPLTPRTVPAVL 94
                         90
                 ....*....|....*
gi 377836445 169 AAACLLRVDRVIQQC 183
Cdd:cd18332   95 AAATYLQMEHVVETC 109
BTB_POZ_KBTBD2_BKLHD1 cd18270
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
90-192 1.32e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 2 (KBTBD2); KBTBD2, also called BTB and kelch domain-containing protein 1 (BKLHD1), plays an essential role in the regulation of insulin-signaling pathway. It is a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase, which targets p85alpha, the regulatory subunit of the phosphoinositol-3-kinase (PI3K) heterodimer, causing p85alpha ubiquitination and proteasome-mediated degradation. 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: 349579 [Multi-domain]  Cd Length: 133  Bit Score: 38.83  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 377836445  90 SDIKIRALGRTWCLHKVFLCQ-SGYFANILKGTWRESRHGVINLiiknEDIDTRSLHFVFGALYrDADLSITPLEVPQVL 168
Cdd:cd18270   27 TDIVLIVEGTEFPCHKMVLATcSSYFRAMFMSGLSESKQTHVHL----RNVDAATLQIIITYAY-TGNLAINDSTVEQLY 101
                         90       100
                 ....*....|....*....|....
gi 377836445 169 AAACLLRVDRVIQQCEGIMKETIN 192
Cdd:cd18270  102 ETACFLQVEDVLQRCREYLIKKIN 125
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
196-266 7.56e-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: 36.17  E-value: 7.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 377836445   196 VCSYYLAAETYRLKAVKTRCFEWLLCNLMVHPSVALYKEVDLKLMYLLaLSSDLLVMQKEIDVYTTLKIWM 266
Cdd:smart00875   1 CLGIRRFADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLEL-LSSDDLNVSSEEEVFEAVLRWV 70
 
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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