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Conserved domains on  [gi|1063699070|ref|NP_565845|]
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ubiquitin-protein ligase [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
155-258 6.76e-12

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: 62.74  E-value: 6.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  155 IQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMWCVKHPHLTVHSEMDLVDGLLIWLDAGgrlsdlPE 234
Cdd:smart00875   2 LGIRRFADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSSDDLNVSSEEEVFEAVLRWVKHD------PE 75
                           90       100
                   ....*....|....*....|....
gi 1063699070  235 SSQDNTINLMEQVRFSLLPLWFIA 258
Cdd:smart00875  76 KRREHLPELLEHVRLPLLSPDYLL 99
PHA03098 super family cl33709
kelch-like protein; Provisional
42-252 1.53e-09

kelch-like protein; Provisional


The actual alignment was detected with superfamily member PHA03098:

Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 61.71  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  42 DMSEILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSEsglDHISVEWNLESFLNLLMCLYGYDIEITSSSFLPLFESALY 121
Cdd:PHA03098   11 DESIIIVNGGGIIKVHKIILSSSSEYFKKMFKNNFKE---NEINLNIDYDSFNEVIKYIYTGKINITSNNVKDILSIANY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 122 FGVEKLLSICKNW-LSVLASSNdnalpkvelsdLIQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMW 200
Cdd:PHA03098   88 LIIDFLINLCINYiIKIIDDNN-----------CIDIYRFSFFYGCKKLYSAAYNYIRNNIELIYNDPDFIYLSKNELIK 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063699070 201 CVKHPHLTVHSEMDLVDGLLIWLDAggrlsdlPESSQDNTINLM-EQVRFSLL 252
Cdd:PHA03098  157 ILSDDKLNVSSEDVVLEIIIKWLTS-------KKNNKYKDICLIlKVLRITFL 202
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
435-653 7.95e-06

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 48.09  E-value: 7.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 435 VSPIIPVQASVFYSGQghcllsSITRLTLEGRSDICDMELRSISRVCESLCYLNIKGCALLSDACIASVIQRCKKLCSLi 514
Cdd:cd09293    37 MCPISDPPLDQLSNCN------KLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTI- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 515 vcytsfsensilalcatismtnehmdinsvasNLQtlHMSKCEGISETSLLNLITHSQKMKSLCLRDTKVSDSVLCEFP- 593
Cdd:cd09293   110 --------------------------------NLG--RHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAs 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063699070 594 --GSTLEALDISN-TTISWMALARVISRN--PNLKTLKARGC------KNLLQLEVDGRTDNFSPLVSGQE 653
Cdd:cd09293   156 gcSKSLERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFRGCplitdfSRIILFKLWQPRLNKPILVEWCE 226
 
Name Accession Description Interval E-value
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
155-258 6.76e-12

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: 62.74  E-value: 6.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  155 IQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMWCVKHPHLTVHSEMDLVDGLLIWLDAGgrlsdlPE 234
Cdd:smart00875   2 LGIRRFADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSSDDLNVSSEEEVFEAVLRWVKHD------PE 75
                           90       100
                   ....*....|....*....|....
gi 1063699070  235 SSQDNTINLMEQVRFSLLPLWFIA 258
Cdd:smart00875  76 KRREHLPELLEHVRLPLLSPDYLL 99
PHA03098 PHA03098
kelch-like protein; Provisional
42-252 1.53e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 61.71  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  42 DMSEILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSEsglDHISVEWNLESFLNLLMCLYGYDIEITSSSFLPLFESALY 121
Cdd:PHA03098   11 DESIIIVNGGGIIKVHKIILSSSSEYFKKMFKNNFKE---NEINLNIDYDSFNEVIKYIYTGKINITSNNVKDILSIANY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 122 FGVEKLLSICKNW-LSVLASSNdnalpkvelsdLIQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMW 200
Cdd:PHA03098   88 LIIDFLINLCINYiIKIIDDNN-----------CIDIYRFSFFYGCKKLYSAAYNYIRNNIELIYNDPDFIYLSKNELIK 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063699070 201 CVKHPHLTVHSEMDLVDGLLIWLDAggrlsdlPESSQDNTINLM-EQVRFSLL 252
Cdd:PHA03098  157 ILSDDKLNVSSEDVVLEIIIKWLTS-------KKNNKYKDICLIlKVLRITFL 202
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
50-135 8.17e-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: 53.85  E-value: 8.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070   50 GSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVE-WNLESFLNLLMCLYGYDIEITSSSFLPLFESALYFGVEKLL 128
Cdd:smart00225   7 GGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDdVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLV 86

                   ....*..
gi 1063699070  129 SICKNWL 135
Cdd:smart00225  87 ELCEEFL 93
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
46-122 5.17e-07

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: 48.32  E-value: 5.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063699070  46 ILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVEW-NLESFLNLLMCLYGYDIEITSSSFLPLFESALYF 122
Cdd:cd18186     5 TLVVGGREFPAHRAVLAARSPYFRAMFSSGMKESSSSEIELDDvSPEAFEALLDYIYTGELELSEENVEELLAAADKL 82
BACK pfam07707
BTB And C-terminal Kelch; This domain is found associated with pfam00651 and pfam01344. The ...
155-257 5.62e-06

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


Pssm-ID: 462237 [Multi-domain]  Cd Length: 103  Bit Score: 46.00  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 155 IQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMWCVKHPHLTVHSEMDLVDGLLIWL--DAGGRLSDL 232
Cdd:pfam07707   2 LGIYRFADAYGCTELAEAALRFILQNFLEVAKSEEFLELSLEQLLELLSSDDLNVPSEEEVFEAVIRWVkhDVERRKKHL 81
                          90       100
                  ....*....|....*....|....*
gi 1063699070 233 PEssqdntinLMEQVRFSLLPLWFI 257
Cdd:pfam07707  82 PE--------LLSAVRLPLLSPQYL 98
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
435-653 7.95e-06

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 48.09  E-value: 7.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 435 VSPIIPVQASVFYSGQghcllsSITRLTLEGRSDICDMELRSISRVCESLCYLNIKGCALLSDACIASVIQRCKKLCSLi 514
Cdd:cd09293    37 MCPISDPPLDQLSNCN------KLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTI- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 515 vcytsfsensilalcatismtnehmdinsvasNLQtlHMSKCEGISETSLLNLITHSQKMKSLCLRDTKVSDSVLCEFP- 593
Cdd:cd09293   110 --------------------------------NLG--RHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAs 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063699070 594 --GSTLEALDISN-TTISWMALARVISRN--PNLKTLKARGC------KNLLQLEVDGRTDNFSPLVSGQE 653
Cdd:cd09293   156 gcSKSLERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFRGCplitdfSRIILFKLWQPRLNKPILVEWCE 226
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
50-131 7.07e-03

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: 37.24  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  50 GSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVE-WNLESFLNLLMCLYGyDIEITSSSFLPLFESALYFGVEKLL 128
Cdd:pfam00651  18 GDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDdVSPEDFEALLEFMYT-GKLISEENVDDLLAAADKLQIPSLV 96

                  ...
gi 1063699070 129 SIC 131
Cdd:pfam00651  97 DKC 99
 
Name Accession Description Interval E-value
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
155-258 6.76e-12

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: 62.74  E-value: 6.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  155 IQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMWCVKHPHLTVHSEMDLVDGLLIWLDAGgrlsdlPE 234
Cdd:smart00875   2 LGIRRFADAHGLEELAEKALRFILQNFSEVSSSEEFLELPLEQLLELLSSDDLNVSSEEEVFEAVLRWVKHD------PE 75
                           90       100
                   ....*....|....*....|....
gi 1063699070  235 SSQDNTINLMEQVRFSLLPLWFIA 258
Cdd:smart00875  76 KRREHLPELLEHVRLPLLSPDYLL 99
PHA03098 PHA03098
kelch-like protein; Provisional
42-252 1.53e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 61.71  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  42 DMSEILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSEsglDHISVEWNLESFLNLLMCLYGYDIEITSSSFLPLFESALY 121
Cdd:PHA03098   11 DESIIIVNGGGIIKVHKIILSSSSEYFKKMFKNNFKE---NEINLNIDYDSFNEVIKYIYTGKINITSNNVKDILSIANY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 122 FGVEKLLSICKNW-LSVLASSNdnalpkvelsdLIQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMW 200
Cdd:PHA03098   88 LIIDFLINLCINYiIKIIDDNN-----------CIDIYRFSFFYGCKKLYSAAYNYIRNNIELIYNDPDFIYLSKNELIK 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063699070 201 CVKHPHLTVHSEMDLVDGLLIWLDAggrlsdlPESSQDNTINLM-EQVRFSLL 252
Cdd:PHA03098  157 ILSDDKLNVSSEDVVLEIIIKWLTS-------KKNNKYKDICLIlKVLRITFL 202
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
50-135 8.17e-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: 53.85  E-value: 8.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070   50 GSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVE-WNLESFLNLLMCLYGYDIEITSSSFLPLFESALYFGVEKLL 128
Cdd:smart00225   7 GGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDdVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLV 86

                   ....*..
gi 1063699070  129 SICKNWL 135
Cdd:smart00225  87 ELCEEFL 93
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
46-122 5.17e-07

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: 48.32  E-value: 5.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063699070  46 ILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVEW-NLESFLNLLMCLYGYDIEITSSSFLPLFESALYF 122
Cdd:cd18186     5 TLVVGGREFPAHRAVLAARSPYFRAMFSSGMKESSSSEIELDDvSPEAFEALLDYIYTGELELSEENVEELLAAADKL 82
BACK pfam07707
BTB And C-terminal Kelch; This domain is found associated with pfam00651 and pfam01344. The ...
155-257 5.62e-06

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


Pssm-ID: 462237 [Multi-domain]  Cd Length: 103  Bit Score: 46.00  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 155 IQIWSFGLEHAGEFVPDLCVAYLAKNFMLVKSDKYFGNVPYELLMWCVKHPHLTVHSEMDLVDGLLIWL--DAGGRLSDL 232
Cdd:pfam07707   2 LGIYRFADAYGCTELAEAALRFILQNFLEVAKSEEFLELSLEQLLELLSSDDLNVPSEEEVFEAVIRWVkhDVERRKKHL 81
                          90       100
                  ....*....|....*....|....*
gi 1063699070 233 PEssqdntinLMEQVRFSLLPLWFI 257
Cdd:pfam07707  82 PE--------LLSAVRLPLLSPQYL 98
BTB_POZ_trishanku-like cd18314
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
46-131 5.76e-06

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Dictyostelium discoideum trishanku and similar proteins; Trishanku is a novel regulator required for normal morphogenesis and cell-type stability in Dictyostelium discoideum. It contains a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349623 [Multi-domain]  Cd Length: 96  Bit Score: 45.80  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  46 ILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVE-WNLESFLNLLMCLYGYDIEITSSSFLPLFESALYFGV 124
Cdd:cd18314    10 VLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEdVEPEIFETVLKYMYTGQVTLSEENVLDLLMLASKYQV 89

                  ....*..
gi 1063699070 125 EKLLSIC 131
Cdd:cd18314    90 PDLEKLC 96
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
435-653 7.95e-06

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 48.09  E-value: 7.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 435 VSPIIPVQASVFYSGQghcllsSITRLTLEGRSDICDMELRSISRVCESLCYLNIKGCALLSDACIASVIQRCKKLCSLi 514
Cdd:cd09293    37 MCPISDPPLDQLSNCN------KLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTI- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 515 vcytsfsensilalcatismtnehmdinsvasNLQtlHMSKCEGISETSLLNLITHSQKMKSLCLRDTKVSDSVLCEFP- 593
Cdd:cd09293   110 --------------------------------NLG--RHRNGHLITDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAs 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063699070 594 --GSTLEALDISN-TTISWMALARVISRN--PNLKTLKARGC------KNLLQLEVDGRTDNFSPLVSGQE 653
Cdd:cd09293   156 gcSKSLERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFRGCplitdfSRIILFKLWQPRLNKPILVEWCE 226
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
483-633 1.78e-04

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


Pssm-ID: 467830 [Multi-domain]  Cd Length: 349  Bit Score: 44.68  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 483 SLCYLNIKGCALLSDACIASVIQRCKKLCSLIVCYTSFSENSILALCATISMTNEHMDINSVASNLQTLHMSKcegISET 562
Cdd:cd23951   121 TLELLKMKSCPRVSPRGILAVADHCQHLRELSLNYHLLSDDLLLALSSEEHVRLEHLRIDVVSENDGPMPLHQ---ISKE 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070 563 SLLNLITHSQKMkSLCLRDTKVSDSVLCEFPGSTLEALDIS-NTTISWMALARVISRNPNLKTLK--------------- 626
Cdd:cd23951   198 SWDALIKHSPDV-NLVMYFFVLEDEDFDPFFRSYTPVTHLYfGRSVPKAVLGRVGQHCPRLVELVvcangnspideelir 276

                  ....*...
gi 1063699070 627 -ARGCKNL 633
Cdd:cd23951   277 iAKNCKQL 284
BTB_POZ_KBTBD2_BKLHD1 cd18270
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
57-135 1.88e-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: 39.60  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  57 HRTRLIQESSYFHGLLSGSFSESGLDHISVEwNLESFLNLLMCLYGY--DIEITSSSFLPLFESALYFGVEKLLSICKNW 134
Cdd:cd18270    41 HKMVLATCSSYFRAMFMSGLSESKQTHVHLR-NVDAATLQIIITYAYtgNLAINDSTVEQLYETACFLQVEDVLQRCREY 119

                  .
gi 1063699070 135 L 135
Cdd:cd18270   120 L 120
BTB_POZ cd01165
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
46-122 2.68e-03

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.


Pssm-ID: 349496 [Multi-domain]  Cd Length: 79  Bit Score: 37.65  E-value: 2.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063699070  46 ILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISV-EWNLESFLNLLMCLYGYDIEITSSSFLPLFESALYF 122
Cdd:cd01165     2 VLVVEGEKFHVNKELLAQSSEYFRALFRGGFRESGQAEINLrDISPEDFRALLEFLYGGKRDLDASNLLELLEAANFL 79
BTB_POZ_ABTB2-like cd18297
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
56-136 5.11e-03

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: 37.64  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  56 AHRTRLIQESSYFHGLLSGSFSESGLDHISV-EWNLESFLNLLMCLYGYDIEITSSS---FLPLFESALYFGVEKLLSIC 131
Cdd:cd18297    26 AHKIVLVTASDRFKSMLSSGSTEAQTPVIEIpDIRYDIFQLMMQYLYTGGVESLDVAqddALELLRAASFFQLDGLKRHC 105

                  ....*
gi 1063699070 132 KNWLS 136
Cdd:cd18297   106 EILLS 110
BTB_POZ_BTBD3_6 cd18282
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
53-135 5.45e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD3 and BTBD6; This family includes BTB/POZ domain-containing proteins BTBD3 and BTBD6, both of which are BTB-domain-containing Kelch-like proteins. BTBD3 controls dendrite orientation toward active axons in mammalian neocortex. BTBD6 is required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349591 [Multi-domain]  Cd Length: 108  Bit Score: 37.37  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  53 KVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVEWNLESFLNLLMCLYGYDIEITSSSFLPLFESALYFGVEKLLSICK 132
Cdd:cd18282    22 RIPAHKYVLATGSSVFYAMFYGGLAENKNEIEIPDVEPAAFLNLLRYLYCDEIDLEPDTVLATLYAAKKYLVPHLARACV 101

                  ...
gi 1063699070 133 NWL 135
Cdd:cd18282   102 QFL 104
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
50-131 7.07e-03

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: 37.24  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699070  50 GSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVE-WNLESFLNLLMCLYGyDIEITSSSFLPLFESALYFGVEKLL 128
Cdd:pfam00651  18 GDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDdVSPEDFEALLEFMYT-GKLISEENVDDLLAAADKLQIPSLV 96

                  ...
gi 1063699070 129 SIC 131
Cdd:pfam00651  97 DKC 99
BTB2_POZ_BTBD8 cd18286
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
40-102 7.95e-03

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: 37.24  E-value: 7.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063699070  40 SWDMSEILSYGSVKVRAHRTRLIQESSYFHGLLSGSFSESGLDHISVE-WNLESFLNLLMCLYG 102
Cdd:cd18286    15 GEDSDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLTgVSHAAVSFVLLFIYG 78
 
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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