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Conserved domains on  [gi|1186517988|ref|NP_001337835|]
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rho-related BTB domain-containing protein 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BTB2_POZ_RHOBTB1 cd18358
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
345-470 3.05e-92

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. 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: 349667 [Multi-domain]  Cd Length: 126  Bit Score: 278.77  E-value: 3.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 345 KAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 424
Cdd:cd18358     1 KAFHVRKANRIKECLSKGTFSDVTFKLDDGTINAHKPLLICSCEWMAAMFGGSFIESANSEVVLPNISKVSMQAVLDYLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1186517988 425 TKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAATSG 470
Cdd:cd18358    81 TKQLSPTADLDPLELIALANRFCLPHLVALTEQHAVQELTKASKSG 126
BTB1_POZ_RHOBTB1 cd18355
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
128-340 3.47e-92

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


:

Pssm-ID: 349664 [Multi-domain]  Cd Length: 146  Bit Score: 279.43  E-value: 3.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 128 CPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESpngsegacekekqsrdfqgrilsv 207
Cdd:cd18355     1 CPSKSRNEAGQLLDNPLCADVMFILQEQVHIFAHRIYLATSSSKFYDLFLMECEES------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 208 dpeeereegppripqadqwkssnkslvealgleaegavpetqtLTGWSKGFIGMHREMQVNPISKRMGPMTVVRMDASVQ 287
Cdd:cd18355    57 -------------------------------------------LSSWSKGFYSMHKEMQVNPVSNRPCPMTVVKMDSSIQ 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1186517988 288 PGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMN 340
Cdd:cd18355    94 HGPFKTVLRFLYTGQLDEKEKDLMRLAQIAEILEVFDLRMMVENIMNKEAFMN 146
BACK_RHOBTB1 cd18530
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 ...
473-572 1.73e-77

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. RhoBTB1 also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex.


:

Pssm-ID: 350605  Cd Length: 100  Bit Score: 239.93  E-value: 1.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 473 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREK 552
Cdd:cd18530     1 IDGEVLTYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSPENQEYFERHRWPPVWYLKEEDHYQRVKKEREK 80
                          90       100
                  ....*....|....*....|
gi 1186517988 553 EDIALNKHRSRRKWCFWNSS 572
Cdd:cd18530    81 EDVALHKHHSKRKWCFWNSS 100
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-87 1.36e-51

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd01873:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 195  Bit Score: 175.54  E-value: 1.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   1 MWYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPEKGREVAKELGLPYYETSVFDQFGIKDVF 80
Cdd:cd01873   109 MWYPEIRHFCPRVPVILVGCKLDLRYADLDEVNRARRPLARPIKNADILPPETGRAVAKELGIPYYETSVVTQFGVKDVF 188

                  ....*..
gi 1186517988  81 DNAIRAA 87
Cdd:cd01873   189 DNAIRAA 195
 
Name Accession Description Interval E-value
BTB2_POZ_RHOBTB1 cd18358
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
345-470 3.05e-92

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. 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: 349667 [Multi-domain]  Cd Length: 126  Bit Score: 278.77  E-value: 3.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 345 KAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 424
Cdd:cd18358     1 KAFHVRKANRIKECLSKGTFSDVTFKLDDGTINAHKPLLICSCEWMAAMFGGSFIESANSEVVLPNISKVSMQAVLDYLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1186517988 425 TKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAATSG 470
Cdd:cd18358    81 TKQLSPTADLDPLELIALANRFCLPHLVALTEQHAVQELTKASKSG 126
BTB1_POZ_RHOBTB1 cd18355
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
128-340 3.47e-92

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349664 [Multi-domain]  Cd Length: 146  Bit Score: 279.43  E-value: 3.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 128 CPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESpngsegacekekqsrdfqgrilsv 207
Cdd:cd18355     1 CPSKSRNEAGQLLDNPLCADVMFILQEQVHIFAHRIYLATSSSKFYDLFLMECEES------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 208 dpeeereegppripqadqwkssnkslvealgleaegavpetqtLTGWSKGFIGMHREMQVNPISKRMGPMTVVRMDASVQ 287
Cdd:cd18355    57 -------------------------------------------LSSWSKGFYSMHKEMQVNPVSNRPCPMTVVKMDSSIQ 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1186517988 288 PGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMN 340
Cdd:cd18355    94 HGPFKTVLRFLYTGQLDEKEKDLMRLAQIAEILEVFDLRMMVENIMNKEAFMN 146
BACK_RHOBTB1 cd18530
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 ...
473-572 1.73e-77

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. RhoBTB1 also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex.


Pssm-ID: 350605  Cd Length: 100  Bit Score: 239.93  E-value: 1.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 473 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREK 552
Cdd:cd18530     1 IDGEVLTYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSPENQEYFERHRWPPVWYLKEEDHYQRVKKEREK 80
                          90       100
                  ....*....|....*....|
gi 1186517988 553 EDIALNKHRSRRKWCFWNSS 572
Cdd:cd18530    81 EDVALHKHHSKRKWCFWNSS 100
RhoBTB cd01873
RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB ...
1-87 1.36e-51

RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB subfamily of Rho GTPases are present in vertebrates, Drosophila, and Dictyostelium. RhoBTB proteins are characterized by a modular organization, consisting of a GTPase domain, a proline rich region, a tandem of two BTB (Broad-Complex, Tramtrack, and Bric a brac) domains, and a C-terminal region of unknown function. RhoBTB proteins may act as docking points for multiple components participating in signal transduction cascades. RhoBTB genes appeared upregulated in some cancer cell lines, suggesting a participation of RhoBTB proteins in the pathogenesis of particular tumors. Note that the Dictyostelium RacA GTPase domain is more closely related to Rac proteins than to RhoBTB proteins, where RacA actually belongs. Thus, the Dictyostelium RacA is not included here. Most Rho proteins contain a lipid modification site at the C-terminus; however, RhoBTB is one of few Rho subfamilies that lack this feature.


Pssm-ID: 133275 [Multi-domain]  Cd Length: 195  Bit Score: 175.54  E-value: 1.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   1 MWYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPEKGREVAKELGLPYYETSVFDQFGIKDVF 80
Cdd:cd01873   109 MWYPEIRHFCPRVPVILVGCKLDLRYADLDEVNRARRPLARPIKNADILPPETGRAVAKELGIPYYETSVVTQFGVKDVF 188

                  ....*..
gi 1186517988  81 DNAIRAA 87
Cdd:cd01873   189 DNAIRAA 195
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
1-88 3.30e-25

Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms.


Pssm-ID: 197554 [Multi-domain]  Cd Length: 174  Bit Score: 102.31  E-value: 3.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988    1 MWYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPEKGREVAKELG-LPYYETSVFDQFGIKDV 79
Cdd:smart00174  91 KWYPEVKHFCPNVPIILVGTKLDLR-NDKSTLEELSKKKQEPVT------YEQGQALAKRIGaVKYLECSALTQEGVREV 163

                   ....*....
gi 1186517988   80 FDNAIRAAL 88
Cdd:smart00174 164 FEEAIRAAL 172
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
356-461 1.66e-16

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: 75.37  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 356 KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLD 435
Cdd:pfam00651   2 NELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENVD 81
                          90       100
                  ....*....|....*....|....*.
gi 1186517988 436 plELIALANRFCLPHLVALAEQHAVQ 461
Cdd:pfam00651  82 --DLLAAADKLQIPSLVDKCEEFLIK 105
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
366-463 2.13e-15

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: 71.95  E-value: 2.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988  366 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDpLELIALANR 445
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENV-EELLELADY 79
                           90
                   ....*....|....*...
gi 1186517988  446 FCLPHLVALAEQHAVQEL 463
Cdd:smart00225  80 LQIPGLVELCEEFLLKLL 97
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
2-88 8.95e-13

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 66.38  E-value: 8.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCP-RTPVILVGCQLDLRyaDLEAVnrarrplarpikrgdilPPEKGREVAKELGLPYYETSVFDQFGIKDVF 80
Cdd:pfam00071  93 WVEEILRHADeNVPIVLVGNKCDLE--DQRVV-----------------STEEGEALAKELGLPFMETSAKTNENVEEAF 153

                  ....*...
gi 1186517988  81 DNAIRAAL 88
Cdd:pfam00071 154 EELAREIL 161
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
276-335 4.21e-06

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: 45.37  E-value: 4.21e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988  276 PMTVVRMDaSVQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNK 335
Cdd:smart00225  37 DKSEIYLD-DVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLVELCEEFLLK 95
 
Name Accession Description Interval E-value
BTB2_POZ_RHOBTB1 cd18358
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
345-470 3.05e-92

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. 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: 349667 [Multi-domain]  Cd Length: 126  Bit Score: 278.77  E-value: 3.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 345 KAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 424
Cdd:cd18358     1 KAFHVRKANRIKECLSKGTFSDVTFKLDDGTINAHKPLLICSCEWMAAMFGGSFIESANSEVVLPNISKVSMQAVLDYLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1186517988 425 TKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAATSG 470
Cdd:cd18358    81 TKQLSPTADLDPLELIALANRFCLPHLVALTEQHAVQELTKASKSG 126
BTB1_POZ_RHOBTB1 cd18355
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
128-340 3.47e-92

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB1 functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349664 [Multi-domain]  Cd Length: 146  Bit Score: 279.43  E-value: 3.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 128 CPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESpngsegacekekqsrdfqgrilsv 207
Cdd:cd18355     1 CPSKSRNEAGQLLDNPLCADVMFILQEQVHIFAHRIYLATSSSKFYDLFLMECEES------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 208 dpeeereegppripqadqwkssnkslvealgleaegavpetqtLTGWSKGFIGMHREMQVNPISKRMGPMTVVRMDASVQ 287
Cdd:cd18355    57 -------------------------------------------LSSWSKGFYSMHKEMQVNPVSNRPCPMTVVKMDSSIQ 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1186517988 288 PGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMN 340
Cdd:cd18355    94 HGPFKTVLRFLYTGQLDEKEKDLMRLAQIAEILEVFDLRMMVENIMNKEAFMN 146
BACK_RHOBTB1 cd18530
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 ...
473-572 1.73e-77

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 (RhoBTB1); RhoBTB1 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It functions as a tumor suppressor that regulates the integrity of the Golgi complex through the methyltransferase METTL7B. RhoBTB1 also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex.


Pssm-ID: 350605  Cd Length: 100  Bit Score: 239.93  E-value: 1.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 473 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREK 552
Cdd:cd18530     1 IDGEVLTYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSPENQEYFERHRWPPVWYLKEEDHYQRVKKEREK 80
                          90       100
                  ....*....|....*....|
gi 1186517988 553 EDIALNKHRSRRKWCFWNSS 572
Cdd:cd18530    81 EDVALHKHHSKRKWCFWNSS 100
BTB2_POZ_RHOBTB2 cd18359
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
345-467 3.93e-66

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 2 (RhoBTB2); RhoBTB2, also called Deleted in breast cancer 2 gene protein (DBC2) or p83, is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB2 functions as a tumor suppressor that regulates the expression of the methyltransferase METTL7A. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. 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: 349668 [Multi-domain]  Cd Length: 124  Bit Score: 211.02  E-value: 3.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 345 KAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 424
Cdd:cd18359     1 KAFHVRRTNRVKECLAKGTFSDVTFMLDDGTISAHKPLLISSCDWMAAMFGGPFVESSTTEVVFPYTSRSSMRAVLEYLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1186517988 425 TKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAA 467
Cdd:cd18359    81 TGQFSSSPDLDDMKLIILANRLCLPHLVALTEQYTVTVLMEAA 123
BACK_RHOBTB2 cd18531
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 2 ...
473-569 4.98e-55

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 2 (RhoBTB2); RhoBTB2, also called Deleted in breast cancer 2 gene protein (DBC2), or p83, is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It functions as a tumor suppressor that regulates the expression of the methyltransferase METTL7A. RhoBTB2 also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex.


Pssm-ID: 350606  Cd Length: 97  Bit Score: 180.90  E-value: 4.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 473 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREK 552
Cdd:cd18531     1 IDGQVLVYLELAQFHNAKQLADWCLHHICTNYNSVCRKFPRDMKAMSPENQEHFEKHRWPPVWYLKEEDRYLRSKKEREK 80
                          90
                  ....*....|....*..
gi 1186517988 553 EDIALNKHRSRRKWCFW 569
Cdd:cd18531    81 EEELLRKQHPKRKWCFW 97
BTB2_POZ_RhoBTB cd18300
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
356-463 7.14e-55

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: 180.90  E-value: 7.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 356 KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLD 435
Cdd:cd18300     1 KLFLNKGLFSDVTFIVEDGTIPAHKALLVARCDVMAAMFGGNFRESSAKEVELPGVSKETFLALLEYLYTDQAPILEDGD 80
                          90       100
                  ....*....|....*....|....*...
gi 1186517988 436 PLELIALANRFCLPHLVALAEQHAVQEL 463
Cdd:cd18300    81 CVGLIVLANRLCLPRLVALCEQYIVKEL 108
BTB1_POZ_RHOBTB2 cd18356
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
126-340 1.95e-54

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 2 (RhoBTB2); RhoBTB2, also called Deleted in breast cancer 2 gene protein (DBC2) or p83, is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB2 functions as a tumor suppressor that regulates the expression of the methyltransferase METTL7A. It also acts an adaptor of the Cullin-3-dependent E3 ubiquitin ligase complex. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349665 [Multi-domain]  Cd Length: 148  Bit Score: 181.29  E-value: 1.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 126 PECPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECeespngsegacekekqsrdfqGRIL 205
Cdd:cd18356     1 PDPPTKSEEHPAHLLEDPLCADVILVLQERIRIYAHKIYLSTSSSKFYDLFLMDR---------------------GRDL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 206 SvdpeeereegppripqadqwkssnkslvealgleaegavpetqtltGWSKGFIGMHREMQVNPISKRMGPMTVVRMDAS 285
Cdd:cd18356    60 S----------------------------------------------SWSRAFVSIQEEVAEDPLTYKSRLMVVVKMDSS 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1186517988 286 VQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMN 340
Cdd:cd18356    94 IQPGPFRAVLKYLYTGELDENERDLMHIAHIAELLEVFDLRMMVANILNNEAFMN 148
RhoBTB cd01873
RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB ...
1-87 1.36e-51

RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB subfamily of Rho GTPases are present in vertebrates, Drosophila, and Dictyostelium. RhoBTB proteins are characterized by a modular organization, consisting of a GTPase domain, a proline rich region, a tandem of two BTB (Broad-Complex, Tramtrack, and Bric a brac) domains, and a C-terminal region of unknown function. RhoBTB proteins may act as docking points for multiple components participating in signal transduction cascades. RhoBTB genes appeared upregulated in some cancer cell lines, suggesting a participation of RhoBTB proteins in the pathogenesis of particular tumors. Note that the Dictyostelium RacA GTPase domain is more closely related to Rac proteins than to RhoBTB proteins, where RacA actually belongs. Thus, the Dictyostelium RacA is not included here. Most Rho proteins contain a lipid modification site at the C-terminus; however, RhoBTB is one of few Rho subfamilies that lack this feature.


Pssm-ID: 133275 [Multi-domain]  Cd Length: 195  Bit Score: 175.54  E-value: 1.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   1 MWYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPEKGREVAKELGLPYYETSVFDQFGIKDVF 80
Cdd:cd01873   109 MWYPEIRHFCPRVPVILVGCKLDLRYADLDEVNRARRPLARPIKNADILPPETGRAVAKELGIPYYETSVVTQFGVKDVF 188

                  ....*..
gi 1186517988  81 DNAIRAA 87
Cdd:cd01873   189 DNAIRAA 195
BACK_RHOBTB cd18499
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing proteins ...
473-549 3.12e-36

BACK (BTB and C-terminal Kelch) 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 C-terminal BACK domain. 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.


Pssm-ID: 350574  Cd Length: 76  Bit Score: 129.66  E-value: 3.12e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1186517988 473 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCsKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKRE 549
Cdd:cd18499     1 IDEDVIDLLELAQLHNADQLAAWCLHFISTNYNAFC-KHRKEFKLLSPENQEYIEEHRWPPVWYLKELDEYEKKLKE 76
BTB1_POZ_RhoBTB cd18299
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
134-334 1.07e-32

first 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, tandem BTB domains, and a conserved C-terminal region. In vertebrates, 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 first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349608 [Multi-domain]  Cd Length: 103  Bit Score: 120.78  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 134 NEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMeceespngsegacekekqsrdfqgrilsvdpeeer 213
Cdd:cd18299     1 EDLRNLLHSPSCADVVFILQGGVRIFAHRIVLAAASSVFADLFLM----------------------------------- 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 214 eegppripqadqwkssnkslvealgleaegavpetqtltgwskgfigmhremqvnpiskrmgpMTVVRMDASVQPGPFRT 293
Cdd:cd18299    46 ---------------------------------------------------------------MTVVTLDSDITPEAFRR 62
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1186517988 294 LLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMN 334
Cdd:cd18299    63 VLEFLYTGVLDENEDDLKELKDAAELLELFDLVMMCTNVLN 103
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
1-88 3.30e-25

Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms.


Pssm-ID: 197554 [Multi-domain]  Cd Length: 174  Bit Score: 102.31  E-value: 3.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988    1 MWYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPEKGREVAKELG-LPYYETSVFDQFGIKDV 79
Cdd:smart00174  91 KWYPEVKHFCPNVPIILVGTKLDLR-NDKSTLEELSKKKQEPVT------YEQGQALAKRIGaVKYLECSALTQEGVREV 163

                   ....*....
gi 1186517988   80 FDNAIRAAL 88
Cdd:smart00174 164 FEEAIRAAL 172
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
1-86 3.56e-25

Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho (Ras homology) family include RhoA, Cdc42, Rac, Rnd, Wrch1, RhoBTB, and Rop. There are 22 human Rho family members identified currently. These proteins are all involved in the reorganization of the actin cytoskeleton in response to external stimuli. They also have roles in cell transformation by Ras in cytokinesis, in focal adhesion formation and in the stimulation of stress-activated kinase. These various functions are controlled through distinct effector proteins and mediated through a GTP-binding/GTPase cycle involving three classes of regulating proteins: GAPs (GTPase-activating proteins), GEFs (guanine nucleotide exchange factors), and GDIs (guanine nucleotide dissociation inhibitors). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Since crystal structures often lack C-terminal residues, this feature is not available for annotation in many of the CDs in the hierarchy.


Pssm-ID: 206641 [Multi-domain]  Cd Length: 171  Bit Score: 102.24  E-value: 3.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   1 MWYPEIKHFCPRTPVILVGCQLDLRYADLeavnrarrPLARPIKRGDILPPEKGREVAKELGL-PYYETSVFDQFGIKDV 79
Cdd:cd00157    93 KWYPEIKHYCPNVPIILVGTKIDLRDDGN--------TLKKLEKKQKPITPEEGEKLAKEIGAvKYMECSALTQEGLKEV 164

                  ....*..
gi 1186517988  80 FDNAIRA 86
Cdd:cd00157   165 FDEAIRA 171
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
1-103 4.49e-21

Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a GTPase that controls septum degradation by regulating secretion of Eng1 or Agn1 during cytokinesis. Rho4 also plays a role in cell morphogenesis. Rho4 regulates septation and cell morphology by controlling the actin cytoskeleton and cytoplasmic microtubules. The localization of Rho4 is modulated by Rdi1, which may function as a GDI, and by Rga9, which is believed to function as a GAP. In S. pombe, both Rho4 deletion and Rho4 overexpression result in a defective cell wall, suggesting a role for Rho4 in maintaining cell wall integrity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 206704 [Multi-domain]  Cd Length: 197  Bit Score: 91.25  E-value: 4.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   1 MWYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPEKGREVAKELG-LPYYETSVFDQFGIKDV 79
Cdd:cd04132    97 KWYPEVNHFCPGTPIVLVGLKTDLR-KDKNSVSKLRAQGLEPVT------PEQGESVAKSIGaVAYIECSAKLMENVDEV 169
                          90       100
                  ....*....|....*....|....
gi 1186517988  80 FDNAIRAALiSRRHLQFWKSHLKK 103
Cdd:cd04132   170 FDAAINVAL-SKSGRAARKKKKKK 192
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
364-446 1.30e-18

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: 80.29  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDlDPLELIALA 443
Cdd:cd18186     1 LCDVTLVVGGREFPAHRAVLAARSPYFRAMFSSGMKESSSSEIELDDVSPEAFEALLDYIYTGELELSEE-NVEELLAAA 79

                  ...
gi 1186517988 444 NRF 446
Cdd:cd18186    80 DKL 82
BTB_POZ_BTBD9 cd18287
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
355-454 7.03e-17

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: 76.89  E-value: 7.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLS-PNLD 433
Cdd:cd18287    13 IGALFLNEEYSDVTFVVEEKRFPAHRVILAARSEYFRALLYGGMRESQQSEIELKDTNAEAFKALLKYIYTGRLTlTDLK 92
                          90       100
                  ....*....|....*....|..
gi 1186517988 434 LDP-LELIALANRFCLPHLVAL 454
Cdd:cd18287    93 EDVlLDVLGLAHQYGFEELEAA 114
Cdc42 cd01874
cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential ...
2-88 1.34e-16

cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential GTPase that belongs to the Rho family of Ras-like GTPases. These proteins act as molecular switches by responding to exogenous and/or endogenous signals and relaying those signals to activate downstream components of a biological pathway. Cdc42 transduces signals to the actin cytoskeleton to initiate and maintain polarized growth and to mitogen-activated protein morphogenesis. In the budding yeast Saccharomyces cerevisiae, Cdc42 plays an important role in multiple actin-dependent morphogenetic events such as bud emergence, mating-projection formation, and pseudohyphal growth. In mammalian cells, Cdc42 regulates a variety of actin-dependent events and induces the JNK/SAPK protein kinase cascade, which leads to the activation of transcription factors within the nucleus. Cdc42 mediates these processes through interactions with a myriad of downstream effectors, whose number and regulation we are just starting to understand. In addition, Cdc42 has been implicated in a number of human diseases through interactions with its regulators and downstream effectors. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206664 [Multi-domain]  Cd Length: 175  Bit Score: 77.61  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPEKGREVAKELG-LPYYETSVFDQFGIKDVF 80
Cdd:cd01874    95 WVPEITHHCPKTPFLLVGTQIDLR-DDPSTIEKLAKNKQKPIT------PETGEKLARDLKaVKYVECSALTQKGLKNVF 167

                  ....*...
gi 1186517988  81 DNAIRAAL 88
Cdd:cd01874   168 DEAILAAL 175
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
356-461 1.66e-16

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: 75.37  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 356 KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLD 435
Cdd:pfam00651   2 NELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENVD 81
                          90       100
                  ....*....|....*....|....*.
gi 1186517988 436 plELIALANRFCLPHLVALAEQHAVQ 461
Cdd:pfam00651  82 --DLLAAADKLQIPSLVDKCEEFLIK 105
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
2-86 2.78e-16

Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 and Rac3; The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleotide association and is more efficiently activated by the RacGEF Tiam1. Both Rac1 and Rac3 have been implicated in the regulation of cell migration and invasion in human metastatic breast cancer. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206663 [Multi-domain]  Cd Length: 174  Bit Score: 76.77  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKRgdilppEKGREVAKELG-LPYYETSVFDQFGIKDVF 80
Cdd:cd01871    95 WYPEVRHHCPNTPIILVGTKLDLR-DDKDTIEKLKEKKLTPITY------PQGLAMAKEIGaVKYLECSALTQRGLKTVF 167

                  ....*.
gi 1186517988  81 DNAIRA 86
Cdd:cd01871   168 DEAIRA 173
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
2-88 1.40e-15

Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of RhoA, RhoB, and RhoC. RhoA promotes the formation of stress fibers and focal adhesions, regulating cell shape, attachment, and motility. RhoA can bind to multiple effector proteins, thereby triggering different downstream responses. In many cell types, RhoA mediates local assembly of the contractile ring, which is necessary for cytokinesis. RhoA is vital for muscle contraction; in vascular smooth muscle cells, RhoA plays a key role in cell contraction, differentiation, migration, and proliferation. RhoA activities appear to be elaborately regulated in a time- and space-dependent manner to control cytoskeletal changes. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. RhoA and RhoC are observed only in geranylgeranylated forms; however, RhoB can be present in palmitoylated, farnesylated, and geranylgeranylated forms. RhoA and RhoC are highly relevant for tumor progression and invasiveness; however, RhoB has recently been suggested to be a tumor suppressor. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206662 [Multi-domain]  Cd Length: 175  Bit Score: 74.77  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPEKGREVAKELG-LPYYETSVFDQFGIKDVF 80
Cdd:cd01870    95 WTPEVKHFCPNVPIILVGNKKDLR-NDEHTIRELAKMKQEPVK------PEEGRAMAEKIGaFGYLECSAKTKEGVREVF 167

                  ....*...
gi 1186517988  81 DNAIRAAL 88
Cdd:cd01870   168 EMATRAAL 175
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
366-463 2.13e-15

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: 71.95  E-value: 2.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988  366 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDpLELIALANR 445
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENV-EELLELADY 79
                           90
                   ....*....|....*...
gi 1186517988  446 FCLPHLVALAEQHAVQEL 463
Cdd:smart00225  80 LQIPGLVELCEEFLLKLL 97
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
2-88 4.56e-15

Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a GTPase with high sequence similarity to members of the Rac subfamily, including the regions involved in effector recognition and binding. However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding (CRIB) motif. Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Thus RhoG activates Rac1 through Elmo and Dock180 to control cell morphology. RhoG has also been shown to play a role in caveolar trafficking and has a novel role in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor (GPCR) agonists. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 133277 [Multi-domain]  Cd Length: 191  Bit Score: 73.89  E-value: 4.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPEKGREVAKELG-LPYYETSVFDQFGIKDVF 80
Cdd:cd01875    97 WHPEVCHHCPNVPILLVGTKKDLR-NDADTLKKLKEQGQAPIT------PQQGGALAKQIHaVKYLECSALNQDGVKEVF 169

                  ....*...
gi 1186517988  81 DNAIRAAL 88
Cdd:cd01875   170 AEAVRAVL 177
BTB2_POZ_BTBD8 cd18286
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
361-458 2.57e-14

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: 69.60  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 361 KGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDPLELI 440
Cdd:cd18286    14 NGEDSDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLTGVSHAAVSFVLLFIYGGVLDLPDDVNLGELL 93
                          90
                  ....*....|....*...
gi 1186517988 441 ALANRFCLPHLVALAEQH 458
Cdd:cd18286    94 SLADMYGLDGLKDVVAYT 111
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
2-87 1.59e-13

Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 responsive Cdc42 homolog) is a Rho family GTPase that shares significant sequence and functional similarity with Cdc42. Wrch-1 was first identified in mouse mammary epithelial cells, where its transcription is upregulated in Wnt-1 transformation. Wrch-1 contains N- and C-terminal extensions relative to cdc42, suggesting potential differences in cellular localization and function. The Wrch-1 N-terminal extension contains putative SH3 domain-binding motifs and has been shown to bind the SH3 domain-containing protein Grb2, which increases the level of active Wrch-1 in cells. Unlike Cdc42, which localizes to the cytosol and perinuclear membranes, Wrch-1 localizes extensively with the plasma membrane and endosomes. The membrane association, localization, and biological activity of Wrch-1 indicate an atypical model of regulation distinct from other Rho family GTPases. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133330 [Multi-domain]  Cd Length: 173  Bit Score: 68.97  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRYaDLEAVNRARRPLARPIkrgdilPPEKGREVAKELG-LPYYETSVFDQFGIKDVF 80
Cdd:cd04130    94 WIPEIRKHNPKAPIILVGTQADLRT-DVNVLIQLARYGEKPV------SQSRAKALAEKIGaCEYIECSALTQKNLKEVF 166

                  ....*..
gi 1186517988  81 DNAIRAA 87
Cdd:cd04130   167 DTAILAG 173
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
2-88 8.95e-13

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 66.38  E-value: 8.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCP-RTPVILVGCQLDLRyaDLEAVnrarrplarpikrgdilPPEKGREVAKELGLPYYETSVFDQFGIKDVF 80
Cdd:pfam00071  93 WVEEILRHADeNVPIVLVGNKCDLE--DQRVV-----------------STEEGEALAKELGLPFMETSAKTNENVEEAF 153

                  ....*...
gi 1186517988  81 DNAIRAAL 88
Cdd:pfam00071 154 EELAREIL 161
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
2-88 2.34e-12

Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206703 [Multi-domain]  Cd Length: 176  Bit Score: 65.53  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVnrarRPLArpIKRGDILPPEKGREVAKELG-LPYYETSVFD-QFGIKDV 79
Cdd:cd04131    95 WKGEVREFCPNTPVLLVGCKSDLR-TDLSTL----TELS--NKRQIPVSHEQGRNLAKQIGaAAYVECSAKTsENSVRDV 167

                  ....*....
gi 1186517988  80 FDNAIRAAL 88
Cdd:cd04131   168 FEMATLACL 176
BACK_RHOBTB3 cd18532
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 3 ...
477-550 5.26e-12

BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical member of the Rho GTPase family of signaling proteins, which is characterized by containing a carboxyl terminal extension that harbors two BTB domains and a BACK domain and is capable of assembling cullin 3-dependent ubiquitin ligase complexes. It is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. RhoBTB3 is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) by facilitating hydroxylation and ubiquitination.


Pssm-ID: 350607  Cd Length: 83  Bit Score: 61.73  E-value: 5.26e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1186517988 477 VLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKfrKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKRER 550
Cdd:cd18532     5 VVSLLRKAKFHNADQLSTWLLHFIASNYLIFSQK--PEFQDLSAEERDFVETHRWPSSMYLQELAEYRQHIHSR 76
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
2-91 6.82e-12

Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal GTPase that plays a role in cell morphogenesis, control of cell wall integrity, control of growth polarity, and maintenance of growth direction. Rho2 activates the protein kinase C homolog Pck2, and Pck2 controls Mok1, the major (1-3) alpha-D-glucan synthase. Together with Rho1 (RhoA), Rho2 regulates the construction of the cell wall. Unlike Rho1, Rho2 is not an essential protein, but its overexpression is lethal. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for proper intracellular localization via membrane attachment. As with other Rho family GTPases, the GDP/GTP cycling is regulated by GEFs (guanine nucleotide exchange factors), GAPs (GTPase-activating proteins) and GDIs (guanine nucleotide dissociation inhibitors).


Pssm-ID: 206702 [Multi-domain]  Cd Length: 190  Bit Score: 64.47  E-value: 6.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyadLEAVNRARRPLARPIKRgdilppEKGREVAKELGL-PYYETSVFDQFGIKDVF 80
Cdd:cd04129    95 WIEEVRRYCPNVPVILVGLKKDLR---QEAVAKGNYATDEFVPI------QQAKLVARAIGAkKYMECSALTGEGVDDVF 165
                          90
                  ....*....|.
gi 1186517988  81 DNAIRAALISR 91
Cdd:cd04129   166 EAATRAALLVR 176
BTB2_POZ_RHOBTB3 cd18360
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
364-463 2.74e-11

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB3 is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. It is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) through facilitating hydroxylation and suppresses the Warburg effect. 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: 349669 [Multi-domain]  Cd Length: 110  Bit Score: 60.63  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDPLELIALA 443
Cdd:cd18360    10 LADVVFKIQGTTVPAHRAVLVARCEVMAAMFNGNYAEAKSFLVPIYGVSKDTFLSFLEYLYTDSCCPASILQAMALLICA 89
                          90       100
                  ....*....|....*....|
gi 1186517988 444 NRFCLPHLVALAEQHAVQEL 463
Cdd:cd18360    90 EMYQVSRLQHICELYIITQL 109
BTB_POZ_trishanku-like cd18314
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
364-454 2.76e-11

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: 60.05  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDpLELIALA 443
Cdd:cd18314     6 FSDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEDVEPEIFETVLKYMYTGQVTLSEENV-LDLLMLA 84
                          90
                  ....*....|.
gi 1186517988 444 NRFCLPHLVAL 454
Cdd:cd18314    85 SKYQVPDLEKL 95
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
355-457 2.36e-10

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: 58.03  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGA--ISAHKPLLICSCEWMAAMFGGSFV-ESANSEVYLPNINKISMQAVLDYLYTKQLSpn 431
Cdd:cd18294     5 MKSLINNPEFSDVKFLVGPERqeIFAHKCILAARCEVFRAMFLTGPQkESTQSPLVLSDIEPEVFRAVLEFIYTNCVT-- 82
                          90       100
                  ....*....|....*....|....*....
gi 1186517988 432 ldLDP---LELIALANRFCLPHLVALAEQ 457
Cdd:cd18294    83 --LSNhtvIEVLAAAVEYGLDELRKLCER 109
BTB_POZ_RCBTB1_2 cd18298
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
365-458 6.66e-10

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2; The RCC1-related guanine nucleotide exchange factor (GEF) family includes RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2, both of which are chromosome condensation regulator-like guanine nucleotide exchange factors. They contain an RCC1 repeat, a BTB domain, and a BACK domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349607 [Multi-domain]  Cd Length: 108  Bit Score: 56.49  E-value: 6.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 365 SDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQ--LSPNldlDPLELIAL 442
Cdd:cd18298    13 SDLKFRVDGKYIYVHKAILKIRCEYFRSMFQSHWNEDDKNVIEIDQYSYPVYYAFLRYLYTDQvdLPPE---DAIGLLDL 89
                          90
                  ....*....|....*.
gi 1186517988 443 ANRFCLPHLVALAEQH 458
Cdd:cd18298    90 ANSYCEERLKKLCEDI 105
Tc10 cd04135
Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike ...
2-88 2.57e-09

Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike formation and neurite outgrowth in vitro. Its expression changes dramatically after peripheral nerve injury, suggesting an important role in promoting axonal outgrowth and regeneration. TC10 regulates translocation of insulin-stimulated GLUT4 in adipocytes and has also been shown to bind directly to Golgi COPI coat proteins. GTP-bound TC10 in vitro can bind numerous potential effectors. Depending on its subcellular localization and distinct functional domains, TC10 can differentially regulate two types of filamentous actin in adipocytes. TC10 mRNAs are highly expressed in three types of mouse muscle tissues: leg skeletal muscle, cardiac muscle, and uterus; they were also present in brain, with higher levels in adults than in newborns. TC10 has also been shown to play a role in regulating the expression of cystic fibrosis transmembrane conductance regulator (CFTR) through interactions with CFTR-associated ligand (CAL). The GTP-bound form of TC10 directs the trafficking of CFTR from the juxtanuclear region to the secretory pathway toward the plasma membrane, away from CAL-mediated DFTR degradation in the lysosome. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206707 [Multi-domain]  Cd Length: 174  Bit Score: 56.56  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKRgdilppEKGREVAKELGLP-YYETSVFDQFGIKDVF 80
Cdd:cd04135    94 WVPELKEYAPNVPYLLIGTQIDLR-DDPKTLARLNDMKEKPITV------EQGQKLAKEIGACcYVECSALTQKGLKTVF 166

                  ....*...
gi 1186517988  81 DNAIRAAL 88
Cdd:cd04135   167 DEAIIAIL 174
BTB_POZ_KLHL34 cd18264
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
360-464 2.94e-09

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: 55.57  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 360 SKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSpnLDLDPLEL 439
Cdd:cd18264    24 AEGFLCDVVLEAEGNEFPAHRSLLACSSDYFRALFKDYTQESKARVIHLPVVSAAGLQRVLDFIYTSWLS--LSLDTLED 101
                          90       100
                  ....*....|....*....|....*.
gi 1186517988 440 IALANRFC-LPHLVALAEQHAVQELT 464
Cdd:cd18264   102 TLEAASYLqVTEAIGLCSQYLINNLA 127
BTB_POZ_ABTB2-like cd18297
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
363-456 3.04e-09

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: 54.97  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 363 TFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSpNLDLDP---LEL 439
Cdd:cd18297    11 EMSDVTFLVEGRPFYAHKIVLVTASDRFKSMLSSGSTEAQTPVIEIPDIRYDIFQLMMQYLYTGGVE-SLDVAQddaLEL 89
                          90
                  ....*....|....*..
gi 1186517988 440 IALANRFCLPHLVALAE 456
Cdd:cd18297    90 LRAASFFQLDGLKRHCE 106
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
2-88 8.49e-09

Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) subfamily plays a role in diverse cellular processes, including cytoskeletal organization, pollen and vegetative cell growth, hormone responses, stress responses, and pathogen resistance. Rops are able to regulate several downstream pathways to amplify a specific signal by acting as master switches early in the signaling cascade. They transmit a variety of extracellular and intracellular signals. Rops are involved in establishing cell polarity in root-hair development, root-hair elongation, pollen-tube growth, cell-shape formation, responses to hormones such as abscisic acid (ABA) and auxin, responses to abiotic stresses such as oxygen deprivation, and disease resistance and disease susceptibility. An individual Rop can have a unique function or an overlapping function shared with other Rop proteins; in addition, a given Rop-regulated function can be controlled by one or multiple Rop proteins. For example, Rop1, Rop3, and Rop5 are all involved in pollen-tube growth; Rop2 plays a role in response to low-oxygen environments, cell-morphology, and root-hair development; root-hair development is also regulated by Rop4 and Rop6; Rop6 is also responsible for ABA response, and ABA response is also regulated by Rop10. Plants retain some of the regulatory mechanisms that are shared by other members of the Rho family, but have also developed a number of unique modes for regulating Rops. Unique RhoGEFs have been identified that are exclusively active toward Rop proteins, such as those containing the domain PRONE (plant-specific Rop nucleotide exchanger). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206705 [Multi-domain]  Cd Length: 173  Bit Score: 55.24  E-value: 8.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLR-----YADleavnrarRPLARPIKRGdilppeKGREVAKELGLPYY-ETSVFDQFG 75
Cdd:cd04133    95 WIPELRHYAPGVPIVLVGTKLDLRddkqfFAD--------HPGAVPITTA------QGEELRKQIGAAAYiECSSKTQQN 160
                          90
                  ....*....|...
gi 1186517988  76 IKDVFDNAIRAAL 88
Cdd:cd04133   161 VKAVFDAAIKVVL 173
BTB_POZ_KLHL26 cd18255
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
360-464 1.11e-08

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: 53.55  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 360 SKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSpnLDLDPLE- 438
Cdd:cd18255    14 AKGQLLDVTLIADGQRFQAHKVVLASCSDYFRAMFTGGMRESSQDEIELKGVSAKGLKHILDFAYTSELT--LDLDCIQd 91
                          90       100
                  ....*....|....*....|....*.
gi 1186517988 439 LIALANRFCLPHLVALAEQHAVQELT 464
Cdd:cd18255    92 VLGAAVHLQMLPVVELCEEFLKSAMS 117
BTB_POZ_KLHL3 cd18339
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
348-428 1.45e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 3 (KLHL3); KLHL3 is a component of an E3 ubiquitin ligase complex that regulates blood pressure by targeting With-No-Lysine (WNK) kinases for degradation. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349648 [Multi-domain]  Cd Length: 121  Bit Score: 53.19  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 348 HVRKANRI-KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTK 426
Cdd:cd18339     4 HMKKAFKVmNELRSKQLLCDVTIVAEDVEIEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTA 83

                  ..
gi 1186517988 427 QL 428
Cdd:cd18339    84 EI 85
BTB_POZ_KLHL22 cd18251
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
362-433 1.99e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 22 (KLHL22); KLHL22 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of polo-like kinase 1 (PLK1) at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates mono-ubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. 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: 349560 [Multi-domain]  Cd Length: 125  Bit Score: 52.90  E-value: 1.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1186517988 362 GTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLD 433
Cdd:cd18251    21 GILFDVVLVVEGKPIEAHRILLAASCDYFRGMFAGGLREMQQTEVLIHGVSYNAMCKILDFIYTSELELSLD 92
BTB_POZ_KLHL2_Mayven cd18338
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
348-428 3.41e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 2 (KLHL2); KLHL2, also called actin-binding protein Mayven, is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349647 [Multi-domain]  Cd Length: 121  Bit Score: 52.00  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 348 HVRKANRI-KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTK 426
Cdd:cd18338     4 HMKKAFKVmNELRSQNLLCDVTIVAEDVEIAAHRVVLAACSPYFHAMFTGEMSESRAKRVRIKEVDGWTLKMLIDYVYTA 83

                  ..
gi 1186517988 427 QL 428
Cdd:cd18338    84 EI 85
BTB_POZ_ARIA_plant cd18352
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
363-464 5.06e-08

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant ARM repeat protein interacting with ABF2 (ARIA) and similar proteins; 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, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. ARIA is a novel abscisic acid signaling component. It negatively regulates seed germination and young seedling growth. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349661 [Multi-domain]  Cd Length: 116  Bit Score: 51.32  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 363 TFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLdPLELIAL 442
Cdd:cd18352    12 TLSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEIPNIRWEVFELMMRFIYTGSVDITNDI-AKDLLRA 90
                          90       100
                  ....*....|....*....|..
gi 1186517988 443 ANRFCLPHLVALAEQHAVQELT 464
Cdd:cd18352    91 ADQYLLEGLKRLCEYTIAQDLT 112
BTB_POZ_KLHL7 cd18237
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
361-449 5.40e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a component of a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 causes autosomal-dominant retinitis pigmentosa. 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: 349546 [Multi-domain]  Cd Length: 126  Bit Score: 51.72  E-value: 5.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 361 KGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDLDPLELI 440
Cdd:cd18237    18 QKTLCDVILIVEGREIKAHRVVLAAASHFFHLMFTSNMTESKSSEVELKDAEPDIIELLVEFAYTARISVN-SNNVQSLL 96

                  ....*....
gi 1186517988 441 ALANRFCLP 449
Cdd:cd18237    97 DAANQYQIE 105
BTB_POZ_KLHL32 cd18261
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
360-465 7.32e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 32 (KLHL32); KLHL32, also called BTB and kelch domain-containing protein 5 (BKLHD5), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. Deletion of KLHL32 may be ssociated with Tourette syndrome and obsessive-compulsive disorder. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349570 [Multi-domain]  Cd Length: 133  Bit Score: 51.51  E-value: 7.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 360 SKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQ--LSPNLDLDpl 437
Cdd:cd18261    24 NDGILCDITLVAEEQKFHAHKAVLAACSDYFRAMFSLCMVESEADEVNLHGVTSLGLKQALDFAYTGQilLEPGVIQD-- 101
                          90       100
                  ....*....|....*....|....*...
gi 1186517988 438 eLIALANRFCLPHLVALAEQHAVQELTK 465
Cdd:cd18261   102 -VLAAGSHLQLLELLSLCSHYLIQELNS 128
BTB_POZ_Rank-5 cd18303
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
355-457 1.71e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349612 [Multi-domain]  Cd Length: 120  Bit Score: 50.01  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGAISAHKPLLIC-SCEWmaamfggSFVESAN-SEVYLPNINKISMQAVLDYLYTKQLSPNL 432
Cdd:cd18303     9 VASLFDKELYSDITIKLADKSIPAHKFVLAArSEKW-------SNENLAStNELDLSDISYEVVLALLRWLYTDELDLTL 81
                          90       100
                  ....*....|....*....|....*.
gi 1186517988 433 DLDPL-ELIALANRFCLPHLVALAEQ 457
Cdd:cd18303    82 DDEFLlELMKAAKRFQLTDLVERCER 107
BTB_POZ_KLHL28_BTBD5 cd18257
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
366-425 2.69e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 28 (KLHL28); KLHL28, also called BTB/POZ domain-containing protein 5 (BTBD5), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349566 [Multi-domain]  Cd Length: 118  Bit Score: 49.46  E-value: 2.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 366 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYT 425
Cdd:cd18257    20 DVVLRVGDVKIHAHKVVLASCSPYFKAMFTGNLSEKENSEVEFQCIDETALQAIVEYAYT 79
BTB_POZ_KLHL36 cd18266
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
354-429 5.37e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 36 (KLHL36); KLHL36 may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. 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: 349575 [Multi-domain]  Cd Length: 135  Bit Score: 49.12  E-value: 5.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1186517988 354 RIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLS 429
Cdd:cd18266    15 GLNEQRQRGLFCDVVLVADEQRVPAHRNLLAVCSDYFNSMFTIGMREAHQKEVELVGASYIGLKAVIDFLYSSELP 90
BTB_POZ cd01165
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
367-446 6.99e-07

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: 46.89  E-value: 6.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 367 VTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDlDPLELIALANRF 446
Cdd:cd01165     1 VVLVVEGEKFHVNKELLAQSSEYFRALFRGGFRESGQAEINLRDISPEDFRALLEFLYGGKRDLDAS-NLLELLEAANFL 79
Rnd3_RhoE_Rho8 cd04172
Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho ...
2-88 8.17e-07

Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd2/Rho7. Rnd3/RhoE is known to bind the serine-threonine kinase ROCK I. Unphosphorylated Rnd3/RhoE associates primarily with membranes, but ROCK I-phosphorylated Rnd3/RhoE localizes in the cytosol. Phosphorylation of Rnd3/RhoE correlates with its activity in disrupting RhoA-induced stress fibers and inhibiting Ras-induced fibroblast transformation. In cells that lack stress fibers, such as macrophages and monocytes, Rnd3/RhoE induces a redistribution of actin, causing morphological changes in the cell. In addition, Rnd3/RhoE has been shown to inhibit cell cycle progression in G1 phase at a point upstream of the pRb family pocket protein checkpoint. Rnd3/RhoE has also been shown to inhibit Ras- and Raf-induced fibroblast transformation. In mammary epithelial tumor cells, Rnd3/RhoE regulates the assembly of the apical junction complex and tight junction formation. Rnd3/RhoE is underexpressed in prostate cancer cells both in vitro and in vivo; re-expression of Rnd3/RhoE suppresses cell cycle progression and increases apoptosis, suggesting it may play a role in tumor suppression. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206735 [Multi-domain]  Cd Length: 182  Bit Score: 49.67  E-value: 8.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKRgdilppEKGREVAKELG-LPYYETSVF-DQFGIKDV 79
Cdd:cd04172    99 WKGEIQEFCPNTKMLLVGCKSDLR-TDVSTLVELSNHRQTPVSY------DQGANMAKQIGaATYIECSALqSENSVRDI 171

                  ....*....
gi 1186517988  80 FDNAIRAAL 88
Cdd:cd04172   172 FHVATLACV 180
BTB_POZ_KLHL18 cd18247
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
354-428 8.77e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 18 (KLHL18); KLHL18 acts as a substrate-specific adaptor for a Cullin3 E3 ubiquitin-protein ligase complex that regulates mitotic entry and ubiquitylates Aurora-A. 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: 349556 [Multi-domain]  Cd Length: 116  Bit Score: 48.05  E-value: 8.77e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186517988 354 RIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQL 428
Cdd:cd18247     9 VMEEIRRQGKLCDVTLKVGDQKFSAHRIVLAATIPYFHAMFTHDMVESKQDEITMQGIEPSALEALINFAYSGRI 83
BTB_POZ_KLHL12_C3IP1_DKIR cd18242
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
361-427 1.18e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 12 (KLHL12); KLHL12, also called CUL3-interacting protein 1 (C3IP1) or DKIR homolog, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of the Wnt signaling pathway and ER-Golgi transport. 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: 349551 [Multi-domain]  Cd Length: 124  Bit Score: 47.82  E-value: 1.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1186517988 361 KGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQ 427
Cdd:cd18242    18 SNTLCDVTLRVEGKEFPAHRIVLAACSDYFCAMFTSEMSEKGKSEVELQGLTASTMEILLDFVYTET 84
BTB_POZ_roadkill-like cd18345
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
348-457 1.30e-06

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: 47.54  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 348 HVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQ 427
Cdd:cd18345     2 ECRLSDDLGLLFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEERKQNRVEITDVDHEVMREMLRFIYTGK 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1186517988 428 lSPNLDLDPLELIALANRFCLPHLVALAEQ 457
Cdd:cd18345    82 -APNLDKMADDLLAAADKYALERLKVMCEE 110
Rnd2_Rho7 cd04173
Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1 ...
2-106 1.31e-06

Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd3/RhoE/Rho8. Rnd2/Rho7 is transiently expressed in radially migrating cells in the brain while they are within the subventricular zone of the hippocampus and cerebral cortex. These migrating cells typically develop into pyramidal neurons. Cells that exogenously expressed Rnd2/Rho7 failed to migrate to upper layers of the brain, suggesting that Rnd2/Rho7 plays a role in the radial migration and morphological changes of developing pyramidal neurons, and that Rnd2/Rho7 degradation is necessary for proper cellular migration. The Rnd2/Rho7 GEF Rapostlin is found primarily in the brain and together with Rnd2/Rho7 induces dendrite branching. Unlike Rnd1/Rho6 and Rnd3/RhoE/Rho8, which are RhoA antagonists, Rnd2/Rho7 binds the GEF Pragmin and significantly stimulates RhoA activity and Rho-A mediated cell contraction. Rnd2/Rho7 is also found to be expressed in spermatocytes and early spermatids, with male-germ-cell Rac GTPase-activating protein (MgcRacGAP), where it localizes to the Golgi-derived pro-acrosomal vesicle. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 206736 [Multi-domain]  Cd Length: 221  Bit Score: 49.64  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVnrarrplaRPIKRGDILP--PEKGREVAKELG-LPYYE-TSVFDQFGIK 77
Cdd:cd04173    95 WQGETQEFCPNAKLVLVGCKLDMR-TDLSTL--------RELSKQRLIPvtHEQGSLLARQLGaVAYVEcSSRMSENSVR 165
                          90       100
                  ....*....|....*....|....*....
gi 1186517988  78 DVFDNAIRAALiSRRHLQFWKSHLKKVQK 106
Cdd:cd04173   166 DVFHVTTLASV-RREHPSLKRSTSRRGLK 193
BTB_POZ_KLHL41_KBTBD10 cd18341
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
355-449 1.41e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 41 (KLHL41); KLHL41 is also called Kel-like protein 23, Kelch repeat and BTB domain-containing protein 10 (KBTBD10), Kelch-related protein 1 (Krp1), or sarcosine. It is a novel kelch-related protein that is involved in pseudopod elongation in transformed cells. It is also involved in skeletal muscle development and differentiation. It regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. 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: 349650 [Multi-domain]  Cd Length: 133  Bit Score: 47.92  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDL 434
Cdd:cd18341    18 LKELLDENKFVDCTLKAGDKSLPCHRLILAACSPYFREYFLSEESEEKKKEVVLDNVDPNIMDMILKYLYSAEIDLN-DG 96
                          90
                  ....*....|....*
gi 1186517988 435 DPLELIALANRFCLP 449
Cdd:cd18341    97 NVQDIFALASRFQIP 111
BTB2_POZ_IBtk cd18302
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
364-464 1.60e-06

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk); IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains two BTB domains. 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: 349611 [Multi-domain]  Cd Length: 113  Bit Score: 46.97  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDG-AISAHKPLLICSCEWMAAMFGGSFVE-SANSEVYLPnINKISMQAVLDYLYTKQLSP---NLDLDPL- 437
Cdd:cd18302     5 LYDVTIVSEDGkEFPCHKCVLVARLEYFHSMLSSSWIEaSSCSALTMP-IPSDILEIILDYLYTDEASAvkeSQNVEFLc 83
                          90       100
                  ....*....|....*....|....*..
gi 1186517988 438 ELIALANRFCLPHLVALAEQHAVQELT 464
Cdd:cd18302    84 NVLVIADQLLITRLKEICEVALVELLS 110
BTB_POZ_KLHL27_IPP cd18256
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
364-454 2.19e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in intracisternal A particle-promoted polypeptide (IPP); IPP, also called Kelch-like protein 27 (KLHL27) or actin-binding protein IPP, is an actin-binding protein that may play a role in organizing the actin cytoskeleton. 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: 349565 [Multi-domain]  Cd Length: 125  Bit Score: 47.01  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDlDPLELIALA 443
Cdd:cd18256    20 FCDVQLQVGMELFSVHRLVLAASSPYFAALFAGGMSESSKDVVQIHGVEPDIFHILLDFIYTGVVEVTVS-NVQELLVAA 98
                          90
                  ....*....|.
gi 1186517988 444 NRFCLPHLVAL 454
Cdd:cd18256    99 DMLQLTEVVEI 109
BTB1_POZ_RhoBTB cd18299
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
359-454 2.85e-06

first 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, tandem BTB domains, and a conserved C-terminal region. In vertebrates, 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 first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349608 [Multi-domain]  Cd Length: 103  Bit Score: 46.05  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 359 LSKGTFSDVTFKLDDG-AISAHKPLLICSCEWMAAMFGgsfvesANSEVYL-PNINKISMQAVLDYLYTKQLspNLDLDP 436
Cdd:cd18299     7 LHSPSCADVVFILQGGvRIFAHRIVLAAASSVFADLFL------MMTVVTLdSDITPEAFRRVLEFLYTGVL--DENEDD 78
                          90
                  ....*....|....*....
gi 1186517988 437 L-ELIALANRFCLPHLVAL 454
Cdd:cd18299    79 LkELKDAAELLELFDLVMM 97
Rnd1_Rho6 cd04174
Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2 ...
2-110 3.07e-06

Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206737 [Multi-domain]  Cd Length: 232  Bit Score: 48.52  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRyADLEAVNRARRPLARPIKRgdilppEKGREVAKELGLP-YYETSVF-DQFGIKDV 79
Cdd:cd04174   107 WRAEILDYCPSTRILLIGCKTDLR-TDLSTLMELSNQKQAPISY------EQGCAMAKQLGAEaYLECSAFtSEKSIHSI 179
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1186517988  80 FDNAiRAALISRRHLQFWKSHLKKVQKPLLQ 110
Cdd:cd04174   180 FRTA-SLLCINKLSPLAKKSPVRSLSKRLLH 209
BTB_POZ_KLHL30 cd18259
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
364-431 3.14e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 30 (KLHL30); KLHL30 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349568 [Multi-domain]  Cd Length: 137  Bit Score: 46.75  E-value: 3.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1186517988 364 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPN 431
Cdd:cd18259    32 LSDVTLLVGGREFPCHRSVLALCSHYFNAMFTGDFVESISARVEIKDVDPAVMESLIDFAYTGKLTIN 99
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
276-335 4.21e-06

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: 45.37  E-value: 4.21e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988  276 PMTVVRMDaSVQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNK 335
Cdd:smart00225  37 DKSEIYLD-DVSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLVELCEEFLLK 95
BTB_POZ_BPM_plant cd18280
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
365-458 6.62e-06

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: 45.40  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 365 SDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQL--------SPNLDLDP 436
Cdd:cd18280    15 ADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVFKALLHFIYKDELpddvepagSDSSSLDT 94
                          90       100
                  ....*....|....*....|....*
gi 1186517988 437 L---ELIALANRFCLPHLVALAEQH 458
Cdd:cd18280    95 TmaqHLLAAADRYALERLRLLCESR 119
BTB_POZ_KLHL40-like cd18269
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
355-449 7.07e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL40 and KLHL41; This family includes Kelch-like proteins, KLHL40 and KLHL41. KLHL40 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. KLHL41 is a novel kelch related protein that is involved in pseudopod elongation in transformed cells. They both contain 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: 349578 [Multi-domain]  Cd Length: 133  Bit Score: 45.86  E-value: 7.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDL 434
Cdd:cd18269    18 LKDLLDENKFVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYTSEIDLN-DQ 96
                          90
                  ....*....|....*
gi 1186517988 435 DPLELIALANRFCLP 449
Cdd:cd18269    97 NVQDIFALASRFQIP 111
BTB1_POZ_ABTB1_BPOZ1 cd18295
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
358-443 8.46e-06

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349604 [Multi-domain]  Cd Length: 119  Bit Score: 45.32  E-value: 8.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 358 CLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFveSANSEVYL--PNINKISMQAVLDYLYTKQLspNLDLD 435
Cdd:cd18295    13 LLEQGSYSDVTFNVHGESFPAHRCILSARSPYFAEMFETKW--KDKREINLkhPLVNPDAFRALLQYLYTGRL--EIHVD 88

                  ....*....
gi 1186517988 436 PLE-LIALA 443
Cdd:cd18295    89 DVEdCKRLA 97
BTB_POZ_KBTBD8 cd18274
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
354-471 9.82e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 8 (KBTBD8); KBTBD8, also called T-cell activation kelch repeat protein (TA-KRP), is a BTB-kelch family protein that is located in the Golgi apparatus and translocates to the spindle apparatus during mitosis. It acts as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex monoubiquitylates NOLC1 and its paralog TCOF1, the mutation of which underlies the neurocristopathy Treacher Collins syndrome. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349583 [Multi-domain]  Cd Length: 129  Bit Score: 45.36  E-value: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 354 RIKECLSKGTFSDVTFKLDDG-AISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNl 432
Cdd:cd18274    12 QLKAMYDEGQLTDIVVEVDHGkTFSCHRNVLAAISPYFRSMFTSGLTESTQKEVRIVGVEAESMHLVLDYAYTSRVTLT- 90
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1186517988 433 DLDPLELIALANRFCLPHLVALAEQHAVQELTKAATSGV 471
Cdd:cd18274    91 EANVQALFTAASIFQIPSLQDQCAQFMISRLDPQNSIGV 129
BTB_POZ_KLHL35 cd18265
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
362-451 1.03e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 35 (KLHL35); KLHL35 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. Significant differences in DNA methylation of the KLHL35 gene in abdominal aortic aneurysm (AAA) patients compared to non-AAA controls suggest a potential role in AAA pathology. Hypermethylation of the KLHL35 gene has also been associated with the development of hepatocellular carcinoma. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349574 [Multi-domain]  Cd Length: 128  Bit Score: 45.15  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 362 GTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSpnLDLDPLE-LI 440
Cdd:cd18265    21 GTFTDVVLLVDGKDFPCHRATLSANSAYFRAMFGGHLKESRQAVVEIQKVSAAAMEVLLDYMYGGGLR--IQEDNVEsVL 98
                          90
                  ....*....|.
gi 1186517988 441 ALANRFCLPHL 451
Cdd:cd18265    99 EASDLLQVSKL 109
BTB_POZ_KLHL8 cd18238
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
355-433 1.04e-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: 44.97  E-value: 1.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLD 433
Cdd:cd18238     6 LHQFYENGELCDVTLKVGEKSIHCHRLVLACVSPYFRAMFTSEMAESKQDSITIKDIDEEAVELLVDFAYTGKLTLTVD 84
BTB_POZ_KLHL9_13 cd18239
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
360-438 1.46e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins KLHL9 and KLHL13; KLHL9 and KLHL13 (also called BTB and kelch domain-containing protein 2, or BKLHD2) are substrate-specific adaptors of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes, thereby coordinating faithful mitotic progression and completion of cytokinesis. They contain 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: 349548 [Multi-domain]  Cd Length: 128  Bit Score: 44.80  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 360 SKGTFSDVTFKLDDG--AISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLD--LD 435
Cdd:cd18239    19 GEGLLCDVTLVPGDGdeTFPVHRAMMASASDYFKAMFTGGMKEQELMCIKLHGVSKIGLKNIIDFIYTAKLSLNMDnlQD 98

                  ...
gi 1186517988 436 PLE 438
Cdd:cd18239    99 TLE 101
BTB_POZ_KBTBD2_BKLHD1 cd18270
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
341-431 3.40e-05

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: 43.84  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 341 QEITKAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVL 420
Cdd:cd18270     3 RQINTEYAVSLLEQLKFFYEQQLLTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAATLQIII 82
                          90
                  ....*....|.
gi 1186517988 421 DYLYTKQLSPN 431
Cdd:cd18270    83 TYAYTGNLAIN 93
BTB_POZ_BAB-like cd18315
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
364-441 3.96e-05

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster proteins bric-a-brac 1 (BAB1), bric-a-brac 2 (BAB2), modifier of mdg4 (doom), and similar proteins; BAB1 and BAB2 probably act as transcriptional regulators that are required for specification of the tarsal segment and are involved in antenna development. Doom is a product of the Drosophila mod(mdg4) gene. It induces apoptosis and binds to baculovirus inhibitor-of-apoptosis proteins. This subfamily also includes Drosophila melanogaster sex determination protein fruitless (FRU), protein jim lovell (LOV), zinc finger protein chinmo, transcription factor GAGA, transcription factor Ken, and longitudinals lacking proteins (LOLA). FRU probably acts as a transcriptional regulator that plays a role in male courtship behavior and sexual orientation, and enhances male-specific expression of takeout in brain-associated fat body. LOV, also called tyrosine kinase-related (TKR), has a regulatory role during midline cell development. Chinmo is a functional effector of the JAK/STAT pathway that regulates eye development, tumor formation, and stem cell self-renewal in Drosophila. GAGA is a transcriptional activator that functions by regulating chromatin structure. Ken, also termed protein Ken and Barbie, is a transcription factor required for Terminalia development. LOLA proteins are putative transcription factors required for axon growth and guidance in the central and peripheral nervous systems. Proteins in this subfamily contain a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349624 [Multi-domain]  Cd Length: 85  Bit Score: 42.15  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDGAISAHKPLLI-CSCeWMAAMFGgSFVESANSEVYLPNINKISMQAVLDYLYTKQLS-PNLDLDPLELIA 441
Cdd:cd18315     1 LVDVTLACEGGSLKAHKLVLAaASP-YFAALLK-ETPPDEHPVIILPDVPYSELKALLDFIYTGEVNvSQEQLESLLKLA 78
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
2-88 4.54e-05

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 44.04  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988    2 WYPEIKHFC-PRTPVILVGCQLDLryADLEAVNRarrplarpikrgdilppEKGREVAKELGLPYYETSVFDQFGIKDVF 80
Cdd:smart00175  94 WLKELREYAsPNVVIMLVGNKSDL--EEQRQVSR-----------------EEAEAFAEEHGLPFFETSAKTNTNVEEAF 154

                   ....*...
gi 1186517988   81 DNAIRAAL 88
Cdd:smart00175 155 EELAREIL 162
BTB_POZ_KLHL38 cd18268
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
364-434 6.27e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 38 (KLHL38); KLHL38 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The KLHL38 gene is significantly up-regulated during diapause, a temporary arrest of development during early ontogeny. It may also function in preadipocyte differentiation in the chicken. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349577 [Multi-domain]  Cd Length: 129  Bit Score: 42.85  E-value: 6.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1186517988 364 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDL 434
Cdd:cd18268    23 LTDVILCTGDKEIPCHRNVLASSSPYFRAMFCNNFRESSQAKVDLKGIDSDVLDQIVDYVYTGEILITRDN 93
BTB_POZ_SPOPL cd18343
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
364-464 7.55e-05

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: 42.68  E-value: 7.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQlSPNLDLDPLELIALA 443
Cdd:cd18343    21 FTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTGK-APNLDKMADNLLAAA 99
                          90       100
                  ....*....|....*....|.
gi 1186517988 444 NRFCLPHLVALAEQHAVQELT 464
Cdd:cd18343   100 DKYALERLKVMCEEALCNNLS 120
BTB_POZ_ARMC5 cd18191
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
366-424 9.15e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in armadillo repeat-containing protein 5 (ARMC5); ARMC5 plays a role in steroidogenesis, and modulates the expression and cortisol production of steroidogenic enzymes. It negatively regulates adrenal cells survival. It contains armadillo (ARM) repeats and a BTB domain, which is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349500 [Multi-domain]  Cd Length: 100  Bit Score: 41.72  E-value: 9.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 366 DVTFKLDDGA-ISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 424
Cdd:cd18191     3 DLRFLLDGGTqLPASRAALTGASEVFRAMLEGGFAEAQQDLVPLRQVPSGAFLPVLHYLH 62
BTB_POZ_BTBD1_2 cd18281
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
354-465 1.45e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD1 and BTBD2; This family includes BTB/POZ domain-containing proteins BTBD1 and BTBD2, both of which are BTB-domain-containing Kelch-like proteins that interact with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349590 [Multi-domain]  Cd Length: 127  Bit Score: 41.65  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 354 RIKECLSKGTFSDVTFKLDDGA----ISAHKPLLICSCEWMAAMFGGSFVeSANSEVYLPNINKISMQAVLDYLYTKQls 429
Cdd:cd18281    12 RFAFLFNNETLSDVHFIVGKGDneqrIPAHKFVLSIGSAVFDAMFNGGMA-TTSAEIELPDVEPAAFLALLRFLYSDE-- 88
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1186517988 430 pnLDLDPLELIAL---ANRFCLPHLvalaEQHAVQELTK 465
Cdd:cd18281    89 --VQIGPETVMTTlytAKKYAVPAL----ESACVEFLKK 121
BTB_POZ_RCBTB1_CLLD7 cd18353
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
348-457 1.69e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing protein 1 (RCBTB1); RCBTB1 is also called chronic lymphocytic leukemia deletion region gene 7 protein (CLLD7), CLL deletion region gene 7 protein, regulator of chromosome condensation and BTB domain-containing protein 1, or E4.5. It is a novel chromosome condensation regulator-like guanine nucleotide exchange factor that may be involved in cell cycle regulation by chromatin remodeling. It may also function as a tumor suppressor that regulates pathways of DNA damage/repair and apoptosis. RCBTB1 may also be a substrate adaptor for a cullin3 (CUL3) E3 ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Biallelic mutations in RCBTB1 may cause isolated and syndromic retinal dystrophy. It contains an RCC1 repeat, a BTB domain, and a BACK domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349662 [Multi-domain]  Cd Length: 117  Bit Score: 41.47  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 348 HVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKq 427
Cdd:cd18353     4 FLTVAESLKKEFDSPETSDLKFRVDGKYIHVHKAVLKIRCEHFRTMFQSHWNEDMKEVIEIDQFSYPVYRAFLEYLYTD- 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1186517988 428 lspNLDLDP---LELIALANRFCLPHLVALAEQ 457
Cdd:cd18353    83 ---SVDLPPedaIGLLDLATSYCENRLKKLCQH 112
BTB_POZ_KLHL10 cd18240
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
362-446 1.77e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 10 (KLHL10); KLHL10 is a substrate-specific adaptor of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins specifically in the testis during spermatogenesis. Haploinsufficiency of Klhl10 causes infertility in male mice. KLHL10 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: 349549 [Multi-domain]  Cd Length: 120  Bit Score: 41.54  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 362 GTFSDVTFKLDDGAISAHKPLLiCSCE-WMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDlDPLELI 440
Cdd:cd18240    15 GKLCDVVIRVNGVEFPAHRNIL-CACSpYFRALFTNGWNETEKKVYKIPGVSPEMMELIIEYAYTRTVPITAE-NVEELL 92

                  ....*.
gi 1186517988 441 ALANRF 446
Cdd:cd18240    93 PAADQF 98
BTB_POZ_KLHL23 cd18252
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
362-428 2.00e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 23 (KLHL23); KLHL23 overexpression is associated with increased cell proliferation and invasion in gastric cancer. Downregulation of KLHL23 is associated with invasion, metastasis, and poor prognosis of hepatocellular carcinoma and pancreatic cancer. KLHL23 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: 349561 [Multi-domain]  Cd Length: 127  Bit Score: 41.35  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1186517988 362 GTFSDVTFKLDDGAI-SAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQL 428
Cdd:cd18252    19 GLFTDITLQCASGQIfHCHKAALAACSSYFKVMFTADMKEKSNNVIKLSGIDHDILEALVNYVYTSQI 86
BTB2_POZ_KLHL33 cd18263
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
355-429 2.11e-04

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 33 (KLHL33); KLHL33 contains BTB domains and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. KLHL33 gene expression in normal and tumor tissue suggest a significant association with prostate cancer risk. KLHL33 contains two BTB domains. 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: 349572 [Multi-domain]  Cd Length: 118  Bit Score: 41.34  E-value: 2.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLS 429
Cdd:cd18263     4 IEGLWEKGVGCDVQLEADGSIFRVHRVILAAGSDYFRAMFTSGMKESTQSVVQLPTIPAKDLRLLISFAYSGILH 78
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
145-186 2.14e-04

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: 40.23  E-value: 2.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1186517988 145 CADVLFILQDQEhIFAHRIYLATSSSKFYDLFLMECEESPNG 186
Cdd:cd18186     1 LCDVTLVVGGRE-FPAHRAVLAARSPYFRAMFSSGMKESSSS 41
BTB_POZ_KLHL40_KBTBD5 cd18340
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
355-449 2.19e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 40 (KLHL40); KLHL40, also called Kelch repeat and BTB domain-containing protein 5 (KBTBD5) or sarcosynapsin, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. Mutations in KLHL40 may cause severe autosomal-recessive nemaline myopathy. KLHL40 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: 349649 [Multi-domain]  Cd Length: 134  Bit Score: 41.36  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDL 434
Cdd:cd18340    18 LKDLLDHNKFVDCVLKIKEKEFPCHRLVLAACSPYFRAMFLSDLEESKKREIVLEDVDPDVMGKILHYIYTSEIEIT-EQ 96
                          90
                  ....*....|....*
gi 1186517988 435 DPLELIALANRFCLP 449
Cdd:cd18340    97 NVQDIFAAANMFQIP 111
BTB_POZ_KLHL20_KLEIP cd18249
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
366-429 2.79e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 20 (KLHL20); KLHL20, also called Kelch-like ECT2-interacting protein (KLEIP) or Kelch-like protein X, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. KLHL20 plays a role in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells. It also controls endothelial migration and sprouting angiogenesis. 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: 349558 [Multi-domain]  Cd Length: 128  Bit Score: 40.90  E-value: 2.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1186517988 366 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLS 429
Cdd:cd18249    25 DVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVTIRDIDERAMELLIDFAYTSQIT 88
BTB_POZ_SPOP-like cd18279
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
350-464 3.71e-04

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: 40.59  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 350 RKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQlS 429
Cdd:cd18279     4 RLAEDLGNLWENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTGK-A 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1186517988 430 PNLDLDPLELIALANRFCLPHLVALAEQHAVQELT 464
Cdd:cd18279    83 PNLDKMADDLLAAADKYALERLKVMCEDALCSNLS 117
BTB_POZ_KLHL1-like cd18234
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
365-463 3.83e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5; This family contains the Kelch-like proteins: KLHL1, KLHL4 and KLHL5, all of which share high identity and similarity with the Drosophila kelch protein, a component of ring canals. KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. Family members contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349543 [Multi-domain]  Cd Length: 105  Bit Score: 40.04  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 365 SDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLspNLDLDPLE-LIALA 443
Cdd:cd18234     2 CDVILIAGDRRIPAHRLVLSAVSDYFAAMFTNDVREATEEEIKLKDVDPDALWTLVQYCYTGRL--ELKEDNVEsLLATA 79
                          90       100
                  ....*....|....*....|
gi 1186517988 444 NRFCLPHLVALAEQHAVQEL 463
Cdd:cd18234    80 CLLQLSEVVEACCGFLMKQL 99
BTB_POZ_BTBD3_6 cd18282
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
365-452 4.19e-04

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: 40.07  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 365 SDVTFKL--DDGA--ISAHKPLLICSCEWMAAMFGGSFVESANsEVYLPNINKISMQAVLDYLYTKQlspnLDLDP---L 437
Cdd:cd18282     8 ADVHFIVgpPGGTqrIPAHKYVLATGSSVFYAMFYGGLAENKN-EIEIPDVEPAAFLNLLRYLYCDE----IDLEPdtvL 82
                          90
                  ....*....|....*
gi 1186517988 438 ELIALANRFCLPHLV 452
Cdd:cd18282    83 ATLYAAKKYLVPHLA 97
BTB_POZ_KLHL25 cd18254
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
356-431 8.49e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 25 (KLHL25); KLHL25, also called ectoderm-neural cortex protein 2 (ENC-2), is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that is required for translational homeostasis. The BCR(KLHL25) ubiquitin ligase complex acts by mediating ubiquitination of hypophosphorylated EIF4EBP1 (4E-BP1). Cullin3-KLHL25 ubiquitin ligase also targets ATP-citrate lyase (ACLY), a key enzyme for lipid synthesis, for degradation to inhibit lipid synthesis and tumor progression. KLHL25 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: 349563 [Multi-domain]  Cd Length: 128  Bit Score: 39.61  E-value: 8.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1186517988 356 KECLskgtFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEV-YLPNINKISMQAVLDYLYTKQLSPN 431
Cdd:cd18254    18 KQCM----FTDVTLWAGNRSFPCHRAVLAACSRYFEAMFSNGLRESLDSTVnFHDSLHPEVLELLLDFAYSSRIIIN 90
BTB_POZ_KLHL19_KEAP1 cd18248
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
366-452 8.72e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like ECH-associated protein 1 (KEAP1); KEAP1, also called cytosolic inhibitor of Nrf2 (INrf2) or Kelch-like protein 19 (KLHL19), is a redox-regulated substrate adaptor protein for a Cullin3-dependent ubiquitin ligase complex that targets NFE2L2/NRF2 for ubiquitination and degradation by the proteasome, thus resulting in the suppression of its transcriptional activity and the repression of antioxidant response element-mediated detoxifying enzyme gene expression. 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: 349557 [Multi-domain]  Cd Length: 124  Bit Score: 39.67  E-value: 8.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 366 DVTFKLDDGA----ISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDLDPLELIA 441
Cdd:cd18248    23 DVTLKVKYQDpkeeFMAHKVVLASSSPYFKAMFTSGLRECGMEVVPIEGVHPCVMSRLIEFAYTASISVG-EKCVLHVLP 101
                          90
                  ....*....|.
gi 1186517988 442 LANRFCLPHLV 452
Cdd:cd18248   102 GAVMYQMDSVV 112
BTB_POZ_KLHL24_KRIP6 cd18253
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
353-433 9.56e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 24 (KLHL24); KLHL24, also called kainate receptor-interacting protein for GluR6 (KRIP6) or protein DRE1, is necessary to maintain the balance between intermediate filament stability and degradation, a process that is essential for skin integrity. KLHL24 is a component of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates ubiquitination of KRT14 and controls its levels during keratinocyte differentiation. 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: 349562 [Multi-domain]  Cd Length: 121  Bit Score: 39.43  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 353 NRIKEclsKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNL 432
Cdd:cd18253    10 NEFRD---SRLFTDVIICVEGREFPCHRAILSACSSYFRAMFCNDHRESREMLVEINGILAEAMDCFLQYVYTGKVKITT 86

                  .
gi 1186517988 433 D 433
Cdd:cd18253    87 E 87
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
2-91 9.62e-04

Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of the Rho family found only in fungi. Rho3 is believed to regulate cell polarity by interacting with the diaphanous/formin family protein For3 to control both the actin cytoskeleton and microtubules. Rho3 is also believed to have a direct role in exocytosis that is independent of its role in regulating actin polarity. The function in exocytosis may be two-pronged: first, in the transport of post-Golgi vesicles from the mother cell to the bud, mediated by myosin (Myo2); second, in the docking and fusion of vesicles to the plasma membrane, mediated by an exocyst (Exo70) protein. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 206706 [Multi-domain]  Cd Length: 185  Bit Score: 40.61  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARrplarpikrgdILPPEKGREVAKELG-LPYYETSVFDQFGIKDVF 80
Cdd:cd04134    94 WLAEIRHHCPGVKLVLVALKCDLREPRNERDRGTH-----------TISYEEGLAVAKRINaCRYLECSAKLNRGVNEAF 162
                          90
                  ....*....|.
gi 1186517988  81 DNAIRAALISR 91
Cdd:cd04134   163 TEAARVALNAR 173
BTB_POZ_ETO1-like cd18190
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
366-446 1.19e-03

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Arabidopsis thaliana ethylene-overproduction protein 1 (ETO1) and similar proteins; ETO1, also called protein ethylene overproducer 1, is an essential regulator of the ethylene pathway, which acts by regulating the stability of 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes. It may act as a substrate-specific adaptor that connects ACS enzymes, such as ACS5, to ubiquitin ligase complexes, leading to proteasomal degradation of ACS enzymes. The family also includes ETO1-like proteins 1 (EOL1) and 2 (EOL2). ETO1, EOL1, and EOL2 contain a BTB domain and tetratricopeptide (TPR) repeats. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349499 [Multi-domain]  Cd Length: 83  Bit Score: 38.27  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 366 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNiNKIS---MQAVLDYLYTKQLSPNLDLDPLELIAL 442
Cdd:cd18190     1 DLVFCVGGEKFCCVRKKIASLSRPFKAMLYGNFRESTSDCIDFEE-NGISieaMRAVIDFSVTGRLDLFSVENVHEVLEL 79

                  ....
gi 1186517988 443 ANRF 446
Cdd:cd18190    80 ASKF 83
BTB2_POZ_ABTB1_BPOZ1 cd18296
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
363-451 1.27e-03

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. 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: 349605 [Multi-domain]  Cd Length: 121  Bit Score: 38.82  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 363 TFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVES-----ANSEVYLPNINKISMQAVLDYLYTKqlspNLDLDP- 436
Cdd:cd18296    16 SFPDVCFQVEGHRFPCHKAFFCGRSDYFKALLRDHFAESeenngSIPVVTLHDVSPEVFAIVLYYIYTD----DTDLPPe 91
                          90
                  ....*....|....*..
gi 1186517988 437 --LELIALANRFCLPHL 451
Cdd:cd18296    92 naYDVLYVADMYLLPGL 108
BTB_POZ_NPR_plant cd18310
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
364-458 1.40e-03

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant regulatory proteins, NPR1-4, and similar proteins; NPR1 and NPR2 are essential for pathogenicity and the utilization of many nitrogen sources. NPR1 is also called nitrogen pathogenicity regulation protein NPR1, non-inducible immunity protein 1 (Nim1), nonexpresser of PR genes 1, or salicylic acid insensitive 1 (Sai1). It acts as a transcription coactivator that plays dual roles in regulating plant immunity. NPR3 and NPR4 are involved in negative regulation of defense responses against pathogens in plant. NPR proteins contain a BTB domain, DUF3420, ankyrin (ANK) repeats, and a conserved C-terminal domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349619 [Multi-domain]  Cd Length: 145  Bit Score: 39.21  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDGA-ISAHKPLLICSCEWMAAMFGGSFVESANSEVYLP--------NINKISMQAVLDYLYTKQLSPNLD- 433
Cdd:cd18310    18 YSDAEIIVEGGRpVPVHRCILAARSPFFRDIFASAKAEGANTKPKLElrelipggIVGYDAFMLVLSYLYSGRLRLVPKe 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1186517988 434 ----LDP--------------LELIALANRFCLPHLVALAEQH 458
Cdd:cd18310    98 gsacVDSdcwhvacrpavdfaLEVLYAASVFQIPELVSLFQRR 140
RabL2 cd04124
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...
2-88 1.56e-03

Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab proteins identified recently which display features that are distinct from other Rabs, and have been termed Rab-like. RabL2 contains RabL2a and RabL2b, two very similar Rab proteins that share > 98% sequence identity in humans. RabL2b maps to the subtelomeric region of chromosome 22q13.3 and RabL2a maps to 2q13, a region that suggests it is also a subtelomeric gene. Both genes are believed to be expressed ubiquitously, suggesting that RabL2s are the first example of duplicated genes in human proximal subtelomeric regions that are both expressed actively. Like other Rab-like proteins, RabL2s lack a prenylation site at the C-terminus. The specific functions of RabL2a and RabL2b remain unknown. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.


Pssm-ID: 133324 [Multi-domain]  Cd Length: 161  Bit Score: 39.46  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLryadleavnrarrplarpikrgDILPPEKGREVAKELGLPYYETSVFDQFGIKDVFD 81
Cdd:cd04124    94 WYEELREYRPEIPCIVVANKIDL----------------------DPSVTQKKFNFAEKHNLPLYYVSAADGTNVVKLFQ 151

                  ....*..
gi 1186517988  82 NAIRAAL 88
Cdd:cd04124   152 DAIKLAV 158
BTB_POZ_BTBD14B_NAC1 cd18290
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
353-432 1.63e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in nucleus accumbens-associated protein 1 (NAC-1); NAC-1, also called BTB/POZ domain-containing protein 14B (BTBD14B), is a transcriptional repressor that contributes to tumor progression, tumor cell proliferation, and survival. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349599 [Multi-domain]  Cd Length: 123  Bit Score: 38.86  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 353 NRIKECLS----KGTFSDVTFKLDDGAISAHKPLLICScewmAAMFGGSFVESANSEVYLP-NINKISMQAVLDYLYTKQ 427
Cdd:cd18290    12 NSILECLNeqrlQGLYCDVSVVVKGHAFKAHRAVLAAS----SSYFRDLFNSSRSAVVELPaAVQPQSFQQILSFCYTGR 87

                  ....*
gi 1186517988 428 LSPNL 432
Cdd:cd18290    88 LSMNV 92
BTB_POZ_BTBD12_SLX4 cd18288
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
365-456 1.88e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Structure-specific endonuclease subunit SLX4; SLX4, also called BTB/POZ domain-containing protein 12 (BTBD12), is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases and is required for DNA repair. Mutations of the SLX4 gene are found in Fanconi anemia. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349597 [Multi-domain]  Cd Length: 116  Bit Score: 38.21  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 365 SDVTFKLDDG-AISAHKPLLICSCEWMAAMF--GGSFVESANS----EVYLPNINKISMQAVLDYLYTKQLSPNLDLDPl 437
Cdd:cd18288    19 SDVQFQTDSGeVLYAHSFVLYARCPLLIQMVhsEGFSVEEEGGvttrRVLLGDVSGEAARCFLQYLYTADTGLPPGLSP- 97
                          90
                  ....*....|....*....
gi 1186517988 438 ELIALANRFCLPHLVALAE 456
Cdd:cd18288    98 HVSELADRFGVSELVHLCE 116
BTB_POZ_BTBD1 cd18346
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
364-465 1.98e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 1 (BTBD1); BTBD1, also called Hepatitis C virus NS5A-transactivated protein 8 or HCV NS5A-transactivated protein 8, is a BTB-domain-containing Kelch-like protein that is expressed in skeletal muscle and interacts with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. BTBD1 may serve as substrate-specific adaptor of an E3 ubiquitin-protein ligase complex that 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: 349655 [Multi-domain]  Cd Length: 133  Bit Score: 38.89  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 364 FSDVTFKLDDGA----------ISAHKPLLICSCEWMAAMFGGSFVeSANSEVYLPNINKISMQAVLDYLYTK--QLSPN 431
Cdd:cd18346    22 LSDVRFVVGKGRprgpgpgaqrIPAHRFVLAAGSAVFDAMFNGGMA-TTSAEIELPDVEPAAFLALLRFLYSDevQIGPE 100
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1186517988 432 LDLDPLeliALANRFCLPHLvalaEQHAVQELTK 465
Cdd:cd18346   101 TVMTTL---YTAKKYAVPAL----EAHCVEFLTK 127
BTB_POZ_BTBD3_6 cd18282
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
139-176 2.20e-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: 38.15  E-value: 2.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1186517988 139 LLDNPLCADVLFIL---QDQEHIFAHRIYLATSSSKFYDLF 176
Cdd:cd18282     1 MFNNELMADVHFIVgppGGTQRIPAHKYVLATGSSVFYAMF 41
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
2-25 2.96e-03

Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206680 [Multi-domain]  Cd Length: 168  Bit Score: 38.86  E-value: 2.96e-03
                          10        20
                  ....*....|....*....|....
gi 1186517988   2 WYPEIKHFCPRTPVILVGCQLDLR 25
Cdd:cd01893    95 WLPLIRRLGVKVPIILVGNKSDLR 118
BTB_POZ_KLHL2-like cd18235
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
345-428 2.99e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL2 and KLHL3; The family includes Kelch-like proteins, KLHL2 and KLHL3. KLHL2 is a novel actin-binding protein predominantly expressed in brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 and KLHL3 each functions as a component of an E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins. They contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349544 [Multi-domain]  Cd Length: 121  Bit Score: 37.79  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 345 KAFHVRKANRIKECLSkgtfsDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 424
Cdd:cd18235     7 KAFDVMNELRKQNLLC-----DVILVADGVEIPAHRVVLASCSPYFHAMFTGDLSESRANRVTLQDVDGKALLLLIDYVY 81

                  ....
gi 1186517988 425 TKQL 428
Cdd:cd18235    82 TAEI 85
BACK cd14733
BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal ...
477-509 3.74e-03

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: 35.71  E-value: 3.74e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1186517988 477 VLSYLELAQFHNAHQLAAWCLHHICTNYNSVCS 509
Cdd:cd14733     5 CLGILELADLYNLEELKEKALKFILENFEEVSK 37
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
139-177 5.02e-03

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: 36.84  E-value: 5.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1186517988 139 LLDNPLCADVLFIL-QDQEHIFAHRIYLATSSSKFYDLFL 177
Cdd:cd18294     8 LINNPEFSDVKFLVgPERQEIFAHKCILAARCEVFRAMFL 47
BTB2_POZ_LZTR1 cd18309
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
362-394 5.64e-03

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: 37.37  E-value: 5.64e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1186517988 362 GTFSDVTFKLDDGAISAHKPLLICSCEWMAAMF 394
Cdd:cd18309    18 GDFCDITLLLDGHPIPAHKAILAARCSYFEAMF 50
BTB_POZ_GCL cd18305
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
365-457 5.71e-03

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: 36.87  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 365 SDVTFKLDDGAISAHKpLLICSCEWMAAMFGGSFVESANSEVYL----PNINKISMQAVLDYLYtkqlSPNLDLDPLELI 440
Cdd:cd18305    16 SDITICALGREWKLHK-IYLCQSGYFASMFSGSWKESKETVINLeipdDNITVEALNVVFGSLY----RDEIEIKPSRVV 90
                          90
                  ....*....|....*..
gi 1186517988 441 ALANRFCLPHLVALAEQ 457
Cdd:cd18305    91 SILAAATLLQLDGLIQQ 107
BTB_POZ_ZBTB48_TZAP_KR3 cd18232
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
361-456 6.16e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in telomere zinc finger-associated protein (TZAP); TZAP is also called Krueppel-related zinc finger protein 3 (KR3), zinc finger and BTB domain-containing protein 48 (ZBTB48), or zinc finger protein 855 (ZNF855). It is a vertebrate telomere-binding protein involved in telomere length control. It directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat. TZAP also acts as a transcription regulator that binds to promoter regions. It is a transcriptional activator of alternate reading frame (ARF) gene. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349541 [Multi-domain]  Cd Length: 108  Bit Score: 36.66  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 361 KGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGsfVESANseVYLPNINKISMQAVLDYLYTKQL---SPNLDldpl 437
Cdd:cd18232    15 EGQYCDATLDVGGRVFKAHWSVLACCSHFFQSLYGD--GTSGS--VVLPESFAEVFGLLLDFFYTGELaltRENRD---- 86
                          90
                  ....*....|....*....
gi 1186517988 438 ELIALANRFCLPHLVALAE 456
Cdd:cd18232    87 RVLLAAKELRVPEAVELCQ 105
BTB_POZ_KBTBD6_7 cd18273
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
360-425 7.82e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing proteins KBTBD6 and KBTBD7; KBTBD6 and KBTBD7 are substrate adaptors of a cullin-3 RING ubiquitin ligase complex that mediates ubiquitylation and proteasomal degradation of T-lymphoma and metastasis gene 1 (TIAM1), a RAC1-specific guanine exchange factor (GEF), by cooperating with gamma-aminobutyric acid receptor-associated proteins (GABARAP). KBTBD7 may also act as a new transcriptional activator in mitogen-activated protein kinase (MAPK) signaling. They both contain 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: 349582 [Multi-domain]  Cd Length: 142  Bit Score: 37.11  E-value: 7.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1186517988 360 SKGTFSDVTFKLDDGA--------ISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYT 425
Cdd:cd18273    22 DARLLTDVTIEVNGPGsgpgsgrlFPCNRNVLAAASPYFKSMFTGGLYESKQETVTIHDVDSESMALIIDYCYT 95
BTB_POZ_KBTBD4 cd18272
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
338-424 8.03e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 4 (KBTBD4); KBTBD4, also called BTB and kelch domain-containing protein 4 (BKLHD4), is a BTB-BACK-Kelch domain protein belonging to a large family of cullin-RING ubiquitin ligase adaptors that facilitate the ubiquitination of target substrates. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349581 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 338 FMNQEITKAFHVRKANR--IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKIS 415
Cdd:cd18272     4 FVSYTFTDRSHSSRVAQsiMDLCLEDGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEARNRVIELKDVSESV 83

                  ....*....
gi 1186517988 416 MQAVLDYLY 424
Cdd:cd18272    84 FQLLVDYIY 92
BTB_POZ_KLHL11 cd18241
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
352-451 8.48e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 11 (KLHL11); KLHL11 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal 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: 349550 [Multi-domain]  Cd Length: 135  Bit Score: 36.76  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 352 ANRIKECLSKGTFSDVTFKLDDGA---ISAHKPLLICSCEWMAAMFGGSFVESANSEVYL------PNINKISMQAVLDY 422
Cdd:cd18241    11 SWRQNEQRKQGLFCDITLAFGGAGgreFRAHRSVLAAATEYFTPLLSGQFSESRSGRVEMrkwssePGPDPDTVEAVIQY 90
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1186517988 423 LYTKQL---SPNLDldplELIALANRFCLPHL 451
Cdd:cd18241    91 MYTGRIrvsTGNVH----EVLELADRFLLIRL 118
BTB_POZ_KLHL21 cd18250
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
355-437 9.96e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 21 (KLHL21); KLHL21 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of aurora B. KLHL21 also targets IkappaB kinase-beta to regulate nuclear factor kappa-light chain enhancer of activated B cells (NF-kappaB) signaling negatively. 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: 349559 [Multi-domain]  Cd Length: 124  Bit Score: 36.28  E-value: 9.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186517988 355 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLD- 433
Cdd:cd18250    12 LSELRAERKFFDVTLCAGGREFPCHRTVLAAASSYFRAMFAGELRESRADRVVLHGVSAEILGLLLDFSYTGRVTVTQDn 91

                  ....
gi 1186517988 434 LDPL 437
Cdd:cd18250    92 VEAL 95
 
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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