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Conserved domains on  [gi|1622963184|ref|XP_028709177|]
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rho-related BTB domain-containing protein 1 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoBTB cd01873
RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB ...
13-207 1.55e-136

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: 398.96  E-value: 1.55e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  13 ETIKCVVVGDNAVGKTRLICARACNTTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHHKD 92
Cdd:cd01873     1 ETIKCVVVGDNAVGKTRLICARACNKTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDGVSVSLRLWDTFGDHDKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPE 172
Cdd:cd01873    81 RRFAYGRSDVVLLCFSIASPNSLRNVKTMWYPEIRHFCPRVPVILVGCKLDLRYADLDEVNRARRPLARPIKNADILPPE 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622963184 173 KGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAA 207
Cdd:cd01873   161 TGRAVAKELGIPYYETSVVTQFGVKDVFDNAIRAA 195
BTB2_POZ_RHOBTB1 cd18358
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
465-590 2.82e-91

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: 279.54  E-value: 2.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 465 KAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 544
Cdd:cd18358     1 KAFHVRKANRIKECLSKGTFSDVTFKLDDGTINAHKPLLICSCEWMAAMFGGSFIESANSEVVLPNISKVSMQAVLDYLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622963184 545 TKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAAMSG 590
Cdd:cd18358    81 TKQLSPTADLDPLELIALANRFCLPHLVALTEQHAVQELTKASKSG 126
BTB1_POZ_RHOBTB1 cd18355
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
248-460 1.48e-88

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: 273.27  E-value: 1.48e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 248 CPSMGTSEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESpnwsegacekekqsrdfqeqilsv 327
Cdd:cd18355     1 CPSKSRNEAGQLLDNPLCADVMFILQEQVHIFAHRIYLATSSSKFYDLFLMECEES------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 328 dseeereegpprtpqaeqwkssnkslvealgleaegavpetqtLADWSKGFIGMHREMQVNPISKRVGPVTVVRMDASVQ 407
Cdd:cd18355    57 -------------------------------------------LSSWSKGFYSMHKEMQVNPVSNRPCPMTVVKMDSSIQ 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622963184 408 PGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMN 460
Cdd:cd18355    94 HGPFKTVLRFLYTGQLDEKEKDLMRLAQIAEILEVFDLRMMVENIMNKEAFMN 146
BACK_RHOBTB1 cd18530
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 ...
593-692 1.18e-76

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: 240.70  E-value: 1.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 593 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREK 672
Cdd:cd18530     1 IDGEVLTYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSPENQEYFERHRWPPVWYLKEEDHYQRVKKEREK 80
                          90       100
                  ....*....|....*....|
gi 1622963184 673 EDIALNKHHSRRKWCFWNSS 692
Cdd:cd18530    81 EDVALHKHHSKRKWCFWNSS 100
 
Name Accession Description Interval E-value
RhoBTB cd01873
RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB ...
13-207 1.55e-136

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: 398.96  E-value: 1.55e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  13 ETIKCVVVGDNAVGKTRLICARACNTTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHHKD 92
Cdd:cd01873     1 ETIKCVVVGDNAVGKTRLICARACNKTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDGVSVSLRLWDTFGDHDKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPE 172
Cdd:cd01873    81 RRFAYGRSDVVLLCFSIASPNSLRNVKTMWYPEIRHFCPRVPVILVGCKLDLRYADLDEVNRARRPLARPIKNADILPPE 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622963184 173 KGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAA 207
Cdd:cd01873   161 TGRAVAKELGIPYYETSVVTQFGVKDVFDNAIRAA 195
BTB2_POZ_RHOBTB1 cd18358
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
465-590 2.82e-91

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: 279.54  E-value: 2.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 465 KAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 544
Cdd:cd18358     1 KAFHVRKANRIKECLSKGTFSDVTFKLDDGTINAHKPLLICSCEWMAAMFGGSFIESANSEVVLPNISKVSMQAVLDYLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622963184 545 TKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAAMSG 590
Cdd:cd18358    81 TKQLSPTADLDPLELIALANRFCLPHLVALTEQHAVQELTKASKSG 126
BTB1_POZ_RHOBTB1 cd18355
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
248-460 1.48e-88

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: 273.27  E-value: 1.48e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 248 CPSMGTSEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESpnwsegacekekqsrdfqeqilsv 327
Cdd:cd18355     1 CPSKSRNEAGQLLDNPLCADVMFILQEQVHIFAHRIYLATSSSKFYDLFLMECEES------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 328 dseeereegpprtpqaeqwkssnkslvealgleaegavpetqtLADWSKGFIGMHREMQVNPISKRVGPVTVVRMDASVQ 407
Cdd:cd18355    57 -------------------------------------------LSSWSKGFYSMHKEMQVNPVSNRPCPMTVVKMDSSIQ 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622963184 408 PGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMN 460
Cdd:cd18355    94 HGPFKTVLRFLYTGQLDEKEKDLMRLAQIAEILEVFDLRMMVENIMNKEAFMN 146
BACK_RHOBTB1 cd18530
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 ...
593-692 1.18e-76

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: 240.70  E-value: 1.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 593 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREK 672
Cdd:cd18530     1 IDGEVLTYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSPENQEYFERHRWPPVWYLKEEDHYQRVKKEREK 80
                          90       100
                  ....*....|....*....|
gi 1622963184 673 EDIALNKHHSRRKWCFWNSS 692
Cdd:cd18530    81 EDVALHKHHSKRKWCFWNSS 100
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
17-208 1.42e-50

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: 173.95  E-value: 1.42e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   17 CVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRVCQEVlersrdvvDEVSVSLRLWDTFG--DHHKDRR 94
Cdd:smart00174   1 LVVVGDGAVGKTCLLIVYTTNAFPEDY------VPTVF--ENYSADVEV--------DGKPVELGLWDTAGqeDYDRLRP 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   95 FAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPEKG 174
Cdd:smart00174  65 LSYPDTDVFLICFSVDSPASFENVKEKWYPEVKHFCPNVPIILVGTKLDLR-NDKSTLEELSKKKQEPVT------YEQG 137
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622963184  175 REVAKELG-IPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:smart00174 138 QALAKRIGaVKYLECSALTQEGVREVFEEAIRAAL 172
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
16-208 6.57e-31

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: 118.77  E-value: 6.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICaracntTLTQYQLLATHVPTVwAIDQYRvcqevlersRDV-VDEVSVSLRLWDTFG--DHHKD 92
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLI------RFTQNKFPEEYIPTI-GVDFYT---------KTIeVDGKTVKLQIWDTAGqeRFRAL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSmWYPEIKHFCP-RTPVVLVGCQLDLRyaDLEAVnrarrplarpikrgdilPP 171
Cdd:pfam00071  65 RPLYYRGADGFLLVYDITSRDSFENVKK-WVEEILRHADeNVPIVLVGNKCDLE--DQRVV-----------------ST 124
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622963184 172 EKGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:pfam00071 125 EEGEALAKELGLPFMETSAKTNENVEEAFEELAREIL 161
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
476-581 1.78e-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: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 476 KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLD 555
Cdd:pfam00651   2 NELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENVD 81
                          90       100
                  ....*....|....*....|....*.
gi 1622963184 556 plELIALANRFCLPHLVALAEQHAVQ 581
Cdd:pfam00651  82 --DLLAAADKLQIPSLVDKCEEFLIK 105
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
486-583 2.61e-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: 2.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  486 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDpLELIALANR 565
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENV-EELLELADY 79
                           90
                   ....*....|....*...
gi 1622963184  566 FCLPHLVALAEQHAVQEL 583
Cdd:smart00225  80 LQIPGLVELCEEFLLKLL 97
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
14-202 4.66e-12

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 64.70  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  14 TIKCVVVGDNAVGKtrlicaracnTTLTqYQLLATHVptvwAIDQYR--VCQEVLERSrDVVDEVSVSLRLWDTFG--DH 89
Cdd:TIGR00231   1 DIKIVIVGHPNVGK----------STLL-NSLLGNKG----SITEYYpgTTRNYVTTV-IEEDGKTYKFNLLDTAGqeDY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  90 HKDRRFAYGRSDVVVLCFSIANP-NSLNHVKSMWYPEIKHFCPR-TPVVLVGCQLDLRYADleavnrarrplarpikrgd 167
Cdd:TIGR00231  65 DAIRRLYYPQVERSLRVFDIVILvLDVEEILEKQTKEIIHHADSgVPIILVGNKIDLKDAD------------------- 125
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622963184 168 iLPPEKGREVAKELGIPYYETSVFDQFGIKDVFDN 202
Cdd:TIGR00231 126 -LKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKI 159
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
406-455 5.52e-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: 5.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622963184  406 VQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNK 455
Cdd:smart00225  46 VSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLVELCEEFLLK 95
PTZ00369 PTZ00369
Ras-like protein; Provisional
16-205 2.86e-05

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 45.24  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICaracnttltqyQLLATHVptvwaIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFG-DHHKDRR 94
Cdd:PTZ00369    7 KLVVVGGGGVGKSALTI-----------QFIQNHF-----IDEYDPTIEDSYRKQCVIDEETCLLDILDTAGqEEYSAMR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FAYGRSDVVVLC-FSIANPNSLNHVKSMWYPEIK-HFCPRTPVVLVGCQLDLRYAdleavnrarrplaRPIKRGDilppe 172
Cdd:PTZ00369   71 DQYMRTGQGFLCvYSITSRSSFEEIASFREQILRvKDKDRVPMILVGNKCDLDSE-------------RQVSTGE----- 132
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622963184 173 kGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:PTZ00369  133 -GQELAKSFGIPFLETSAKQRVNVDEAFYELVR 164
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
15-214 2.86e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.19  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLIcARACNTTLTQYQLLATHVPTVWaidqyrvcqevleRSRDVVDEVSVSLRLWDT-----FGDH 89
Cdd:COG1100     4 KKIVVVGTGGVGKTSLV-NRLVGDIFSLEKYLSTNGVTID-------------KKELKLDGLDVDLVIWDTpgqdeFRET 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  90 HKDRRFAYGRSDVVVLCFSIANPNSLNHVKsMWYPEIKHFCPRTPVVLVGCQLDLryadleavnrarrplarpIKRGDIL 169
Cdd:COG1100    70 RQFYARQLTGASLYLFVVDGTREETLQSLY-ELLESLRRLGKKSPIILVLNKIDL------------------YDEEEIE 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622963184 170 PPEKGREVAKELGI-PYYETSVFDQFGIKDVFdNAIRAALISRRHL 214
Cdd:COG1100   131 DEERLKEALSEDNIvEVVATSAKTGEGVEELF-AALAEILRGEGDS 175
 
Name Accession Description Interval E-value
RhoBTB cd01873
RhoBTB protein is an atypical member of the Rho family of small GTPases; Members of the RhoBTB ...
13-207 1.55e-136

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: 398.96  E-value: 1.55e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  13 ETIKCVVVGDNAVGKTRLICARACNTTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHHKD 92
Cdd:cd01873     1 ETIKCVVVGDNAVGKTRLICARACNKTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDGVSVSLRLWDTFGDHDKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPE 172
Cdd:cd01873    81 RRFAYGRSDVVLLCFSIASPNSLRNVKTMWYPEIRHFCPRVPVILVGCKLDLRYADLDEVNRARRPLARPIKNADILPPE 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622963184 173 KGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAA 207
Cdd:cd01873   161 TGRAVAKELGIPYYETSVVTQFGVKDVFDNAIRAA 195
BTB2_POZ_RHOBTB1 cd18358
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
465-590 2.82e-91

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: 279.54  E-value: 2.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 465 KAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 544
Cdd:cd18358     1 KAFHVRKANRIKECLSKGTFSDVTFKLDDGTINAHKPLLICSCEWMAAMFGGSFIESANSEVVLPNISKVSMQAVLDYLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622963184 545 TKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAAMSG 590
Cdd:cd18358    81 TKQLSPTADLDPLELIALANRFCLPHLVALTEQHAVQELTKASKSG 126
BTB1_POZ_RHOBTB1 cd18355
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
248-460 1.48e-88

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: 273.27  E-value: 1.48e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 248 CPSMGTSEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESpnwsegacekekqsrdfqeqilsv 327
Cdd:cd18355     1 CPSKSRNEAGQLLDNPLCADVMFILQEQVHIFAHRIYLATSSSKFYDLFLMECEES------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 328 dseeereegpprtpqaeqwkssnkslvealgleaegavpetqtLADWSKGFIGMHREMQVNPISKRVGPVTVVRMDASVQ 407
Cdd:cd18355    57 -------------------------------------------LSSWSKGFYSMHKEMQVNPVSNRPCPMTVVKMDSSIQ 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622963184 408 PGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMN 460
Cdd:cd18355    94 HGPFKTVLRFLYTGQLDEKEKDLMRLAQIAEILEVFDLRMMVENIMNKEAFMN 146
BACK_RHOBTB1 cd18530
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 1 ...
593-692 1.18e-76

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: 240.70  E-value: 1.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 593 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREK 672
Cdd:cd18530     1 IDGEVLTYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSPENQEYFERHRWPPVWYLKEEDHYQRVKKEREK 80
                          90       100
                  ....*....|....*....|
gi 1622963184 673 EDIALNKHHSRRKWCFWNSS 692
Cdd:cd18530    81 EDVALHKHHSKRKWCFWNSS 100
BTB2_POZ_RHOBTB2 cd18359
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
465-588 9.95e-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: 212.56  E-value: 9.95e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 465 KAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 544
Cdd:cd18359     1 KAFHVRRTNRVKECLAKGTFSDVTFMLDDGTISAHKPLLISSCDWMAAMFGGPFVESSTTEVVFPYTSRSSMRAVLEYLY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622963184 545 TKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAAM 588
Cdd:cd18359    81 TGQFSSSPDLDDMKLIILANRLCLPHLVALTEQYTVTVLMEAAQ 124
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
15-206 1.15e-62

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: 206.24  E-value: 1.15e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRVCQEVlersrdvvDEVSVSLRLWDTFGDHHKD-- 92
Cdd:cd00157     1 IKIVVVGDGAVGKTCLLISYTTNKFPTEY------VPTVF--DNYSANVTV--------DGKQVNLGLWDTAGQEEYDrl 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRYADLeavnrarrPLARPIKRGDILPPE 172
Cdd:cd00157    65 RPLSYPQTDVFLLCFSVDSPSSFENVKTKWYPEIKHYCPNVPIILVGTKIDLRDDGN--------TLKKLEKKQKPITPE 136
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622963184 173 KGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRA 206
Cdd:cd00157   137 EGEKLAKEIGaVKYMECSALTQEGLKEVFDEAIRA 171
BACK_RHOBTB2 cd18531
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 2 ...
593-689 2.84e-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: 183.59  E-value: 2.84e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 593 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREK 672
Cdd:cd18531     1 IDGQVLVYLELAQFHNAKQLADWCLHHICTNYNSVCRKFPRDMKAMSPENQEHFEKHRWPPVWYLKEEDRYLRSKKEREK 80
                          90
                  ....*....|....*..
gi 1622963184 673 EDIALNKHHSRRKWCFW 689
Cdd:cd18531    81 EEELLRKQHPKRKWCFW 97
BTB2_POZ_RhoBTB cd18300
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
476-583 8.17e-54

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: 180.13  E-value: 8.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 476 KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLD 555
Cdd:cd18300     1 KLFLNKGLFSDVTFIVEDGTIPAHKALLVARCDVMAAMFGGNFRESSAKEVELPGVSKETFLALLEYLYTDQAPILEDGD 80
                          90       100
                  ....*....|....*....|....*...
gi 1622963184 556 PLELIALANRFCLPHLVALAEQHAVQEL 583
Cdd:cd18300    81 CVGLIVLANRLCLPRLVALCEQYIVKEL 108
BTB1_POZ_RHOBTB2 cd18356
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
246-460 1.01e-51

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: 175.90  E-value: 1.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 246 PECPSMGTSEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECeespnwsegacekekqSRDfqeqil 325
Cdd:cd18356     1 PDPPTKSEEHPAHLLEDPLCADVILVLQERIRIYAHKIYLSTSSSKFYDLFLMDR----------------GRD------ 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 326 svdseeereegpprtpqaeqwkssnkslvealgleaegavpetqtLADWSKGFIGMHREMQVNPISKRVGPVTVVRMDAS 405
Cdd:cd18356    59 ---------------------------------------------LSSWSRAFVSIQEEVAEDPLTYKSRLMVVVKMDSS 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622963184 406 VQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMN 460
Cdd:cd18356    94 IQPGPFRAVLKYLYTGELDENERDLMHIAHIAELLEVFDLRMMVANILNNEAFMN 148
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
17-208 1.42e-50

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: 173.95  E-value: 1.42e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   17 CVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRVCQEVlersrdvvDEVSVSLRLWDTFG--DHHKDRR 94
Cdd:smart00174   1 LVVVGDGAVGKTCLLIVYTTNAFPEDY------VPTVF--ENYSADVEV--------DGKPVELGLWDTAGqeDYDRLRP 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   95 FAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPEKG 174
Cdd:smart00174  65 LSYPDTDVFLICFSVDSPASFENVKEKWYPEVKHFCPNVPIILVGTKLDLR-NDKSTLEELSKKKQEPVT------YEQG 137
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622963184  175 REVAKELG-IPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:smart00174 138 QALAKRIGaVKYLECSALTQEGVREVFEEAIRAAL 172
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
15-223 1.39e-43

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: 155.58  E-value: 1.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVwaIDQYRvcqevlersRDVVDEVS--VSLRLWDTFG--DHH 90
Cdd:cd04132     4 VKIVVVGDGGCGKTCLLMVYAQGSFPEEY------VPTV--FENYV---------TTLQVPNGkiIELALWDTAGqeDYD 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  91 KDRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKrgdilp 170
Cdd:cd04132    67 RLRPLSYPDVDVILICYSVDNPTSLDNVEDKWYPEVNHFCPGTPIVLVGLKTDLR-KDKNSVSKLRAQGLEPVT------ 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622963184 171 PEKGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRAALiSRRHLQFWKSHLKK 223
Cdd:cd04132   140 PEQGESVAKSIGaVAYIECSAKLMENVDEVFDAAINVAL-SKSGRAARKKKKKK 192
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
12-208 5.20e-41

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: 148.23  E-value: 5.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  12 VETIKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRvcqevlerSRDVVDEVSVSLRLWDTFGDHHK 91
Cdd:cd01875     1 MQSIKCVVVGDGAVGKTCLLICYTTNAFPKEY------IPTVF--DNYS--------AQTAVDGRTVSLNLWDTAGQEEY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  92 DR--RFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKrgdil 169
Cdd:cd01875    65 DRlrTLSYPQTNVFIICFSIASPSSYENVRHKWHPEVCHHCPNVPILLVGTKKDLR-NDADTLKKLKEQGQAPIT----- 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622963184 170 pPEKGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:cd01875   139 -PQQGGALAKQIHaVKYLECSALNQDGVKEVFAEAVRAVL 177
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
15-206 3.44e-39

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: 142.64  E-value: 3.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYrvcqevlerSRDV-VDEVSVSLRLWDTFG--DHHK 91
Cdd:cd01871     2 IKCVVVGDGAVGKTCLLISYTTNAFPGEY------IPTVF--DNY---------SANVmVDGKPVNLGLWDTAGqeDYDR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  92 DRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKRgdilpp 171
Cdd:cd01871    65 LRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR-DDKDTIEKLKEKKLTPITY------ 137
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622963184 172 EKGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRA 206
Cdd:cd01871   138 PQGLAMAKEIGaVKYLECSALTQRGLKTVFDEAIRA 173
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
15-207 1.33e-38

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: 140.62  E-value: 1.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTvwAIDQYRVcqEVLersrdvVDEVSVSLRLWDTFGDHHKD-- 92
Cdd:cd04130     1 LKCVLVGDGAVGKTSLIVSYTTNGYPTEY------VPT--AFDNFSV--VVL------VDGKPVRLQLCDTAGQDEFDkl 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRYaDLEAVNRARRPLARPIkrgdilPPE 172
Cdd:cd04130    65 RPLCYPDTDVFLLCFSVVNPSSFQNISEKWIPEIRKHNPKAPIILVGTQADLRT-DVNVLIQLARYGEKPV------SQS 137
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622963184 173 KGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRAA 207
Cdd:cd04130   138 RAKALAEKIGaCEYIECSALTQKNLKEVFDTAILAG 173
Cdc42 cd01874
cell division cycle 42 (Cdc42) is a small GTPase of the Rho family; Cdc42 is an essential ...
14-208 4.69e-38

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: 139.24  E-value: 4.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  14 TIKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRVCQevlersrdVVDEVSVSLRLWDTFG--DHHK 91
Cdd:cd01874     1 TIKCVVVGDGAVGKTCLLISYTTNKFPSEY------VPTVF--DNYAVTV--------MIGGEPYTLGLFDTAGqeDYDR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  92 DRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKrgdilpP 171
Cdd:cd01874    65 LRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR-DDPSTIEKLAKNKQKPIT------P 137
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622963184 172 EKGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:cd01874   138 ETGEKLARDLKaVKYVECSALTQKGLKNVFDEAILAAL 175
BACK_RHOBTB cd18499
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing proteins ...
593-669 3.53e-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: 130.43  E-value: 3.53e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622963184 593 IDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCsKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKRE 669
Cdd:cd18499     1 IDEDVIDLLELAQLHNADQLAAWCLHFISTNYNAFC-KHRKEFKLLSPENQEYIEEHRWPPVWYLKELDEYEKKLKE 76
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
16-208 1.47e-33

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: 126.77  E-value: 1.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLIcaracnTTLTQYQLLATHVPTVWaiDQYrvcqevlerSRDV-VDEVSVSLRLWDTFG--DHHKD 92
Cdd:cd01870     3 KLVIVGDGACGKTCLL------IVFSKDQFPEVYVPTVF--ENY---------VADIeVDGKQVELALWDTAGqeDYDRL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKrgdilpPE 172
Cdd:cd01870    66 RPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLR-NDEHTIRELAKMKQEPVK------PE 138
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622963184 173 KGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:cd01870   139 EGRAMAEKIGaFGYLECSAKTKEGVREVFEMATRAAL 175
BTB1_POZ_RhoBTB cd18299
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
254-454 9.92e-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: 118.85  E-value: 9.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 254 SEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMEceespnwsegacekekqsrdfqeqilsvdseeer 333
Cdd:cd18299     1 EDLRNLLHSPSCADVVFILQGGVRIFAHRIVLAAASSVFADLFLMM---------------------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 334 eegpprtpqaeqwkssnkslvealgleaegavpetqtladwskgfigmhremqvnpiskrvgpvTVVRMDASVQPGPFRT 413
Cdd:cd18299    47 ----------------------------------------------------------------TVVTLDSDITPEAFRR 62
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622963184 414 LLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMN 454
Cdd:cd18299    63 VLEFLYTGVLDENEDDLKELKDAAELLELFDLVMMCTNVLN 103
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
15-208 6.53e-31

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: 119.07  E-value: 6.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNttltqyQLLATHVPTVWaiDQYRVCQEVlersrdvvDEVSVSLRLWDTFGDHHKD-- 92
Cdd:cd04131     2 CKIVLVGDSQCGKTALLQVFAKD------SFPENYVPTVF--ENYTASFEV--------DKQRIELSLWDTSGSPYYDnv 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVnrarRPLArpIKRGDILPPE 172
Cdd:cd04131    66 RPLSYPDSDAVLICFDISRPETLDSVLKKWKGEVREFCPNTPVLLVGCKSDLR-TDLSTL----TELS--NKRQIPVSHE 138
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622963184 173 KGREVAKELG-IPYYETSVFD-QFGIKDVFDNAIRAAL 208
Cdd:cd04131   139 QGRNLAKQIGaAAYVECSAKTsENSVRDVFEMATLACL 176
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
16-208 6.57e-31

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: 118.77  E-value: 6.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICaracntTLTQYQLLATHVPTVwAIDQYRvcqevlersRDV-VDEVSVSLRLWDTFG--DHHKD 92
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLI------RFTQNKFPEEYIPTI-GVDFYT---------KTIeVDGKTVKLQIWDTAGqeRFRAL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSmWYPEIKHFCP-RTPVVLVGCQLDLRyaDLEAVnrarrplarpikrgdilPP 171
Cdd:pfam00071  65 RPLYYRGADGFLLVYDITSRDSFENVKK-WVEEILRHADeNVPIVLVGNKCDLE--DQRVV-----------------ST 124
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622963184 172 EKGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:pfam00071 125 EEGEALAKELGLPFMETSAKTNENVEEAFEELAREIL 161
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
16-211 8.37e-31

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: 119.17  E-value: 8.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRV-CQevlersrdvVDEVSVSLRLWDTFG--DHHKD 92
Cdd:cd04129     3 KLVIVGDGACGKTSLLYVFTLGEFPEEY------HPTVF--ENYVTdCR---------VDGKPVQLALWDTAGqeEYERL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyadLEAVNRARRPLARPIKRgdilppE 172
Cdd:cd04129    66 RPLSYSKAHVILIGFAIDTPDSLENVRTKWIEEVRRYCPNVPVILVGLKKDLR---QEAVAKGNYATDEFVPI------Q 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622963184 173 KGREVAKELGI-PYYETSVFDQFGIKDVFDNAIRAALISR 211
Cdd:cd04129   137 QAKLVARAIGAkKYMECSALTGEGVDDVFEAATRAALLVR 176
Tc10 cd04135
Rho GTPase TC10 (Tc10); TC10 is a Rho family protein that has been shown to induce microspike ...
15-208 1.63e-28

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: 112.42  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRVCQEVLERSrdvvdevsVSLRLWDTFG--DHHKD 92
Cdd:cd04135     1 LKCVVVGDGAVGKTCLLMSYANDAFPEEY------VPTVF--DHYAVSVTVGGKQ--------YLLGLYDTAGqeDYDRL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKRgdilppE 172
Cdd:cd04135    65 RPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPYLLIGTQIDLR-DDPKTLARLNDMKEKPITV------E 137
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622963184 173 KGREVAKELGIP-YYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:cd04135   138 QGQKLAKEIGACcYVECSALTQKGLKTVFDEAIIAIL 174
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
15-208 5.72e-28

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: 110.71  E-value: 5.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRvcqevlerSRDVVDEVSVSLRLWDTFG--DHHKD 92
Cdd:cd04133     2 IKCVTVGDGAVGKTCMLISYTSNTFPTDY------VPTVF--DNFS--------ANVVVDGNTVNLGLWDTAGqeDYNRL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLR-----YADleavnrarRPLARPIKRGd 167
Cdd:cd04133    66 RPLSYRGADVFLLAFSLISKASYENVLKKWIPELRHYAPGVPIVLVGTKLDLRddkqfFAD--------HPGAVPITTA- 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622963184 168 ilppeKGREVAKELGIPYY-ETSVFDQFGIKDVFDNAIRAAL 208
Cdd:cd04133   137 -----QGEELRKQIGAAAYiECSSKTQQNVKAVFDAAIKVVL 173
Rnd3_RhoE_Rho8 cd04172
Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho ...
13-208 6.54e-25

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: 102.05  E-value: 6.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  13 ETIKC--VVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRVCQEVlersrdvvDEVSVSLRLWDTFGDHH 90
Cdd:cd04172     2 QNVKCkiVVVGDSQCGKTALLHVFAKDCFPENY------VPTVF--ENYTASFEI--------DTQRIELSLWDTSGSPY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  91 KD--RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIKRgdi 168
Cdd:cd04172    66 YDnvRPLSYPDSDAVLICFDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLR-TDVSTLVELSNHRQTPVSY--- 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622963184 169 lppEKGREVAKELG-IPYYETSVF-DQFGIKDVFDNAIRAAL 208
Cdd:cd04172   142 ---DQGANMAKQIGaATYIECSALqSENSVRDIFHVATLACV 180
Rnd1_Rho6 cd04174
Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2 ...
9-230 9.66e-25

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: 103.21  E-value: 9.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   9 RPNVETIKCVVVGDNAVGKTRL--ICARACNTTltqyqllaTHVPTVWaiDQYRVCQEVlersrdvvDEVSVSLRLWDTF 86
Cdd:cd04174     8 QPLVVRCKLVLVGDVQCGKTAMlqVLAKDCYPE--------TYVPTVF--ENYTACLET--------EEQRVELSLWDTS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  87 GDHHKD--RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVNRARRPLARPIK 164
Cdd:cd04174    70 GSPYYDnvRPLCYSDSDAVLLCFDISRPEIFDSALKKWRAEILDYCPSTRILLIGCKTDLR-TDLSTLMELSNQKQAPIS 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622963184 165 RgdilppEKGREVAKELGIP-YYETSVF-DQFGIKDVFDNAiRAALISRRHLQFWKSHLKKVQKPLLQ 230
Cdd:cd04174   149 Y------EQGCAMAKQLGAEaYLECSAFtSEKSIHSIFRTA-SLLCINKLSPLAKKSPVRSLSKRLLH 209
Rnd2_Rho7 cd04173
Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1 ...
16-226 1.48e-24

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: 102.41  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVWaiDQYRVCQEVlersrdvvDEVSVSLRLWDTFGDHHKD--R 93
Cdd:cd04173     3 KIVVVGDTQCGKTALLHVFAKDNYPESY------VPTVF--ENYTASFEI--------DKHRIELNMWDTSGSSYYDnvR 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  94 RFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRyADLEAVnrarrplaRPIKRGDILP--P 171
Cdd:cd04173    67 PLAYPDSDAVLICFDISRPETLDSVLKKWQGETQEFCPNAKLVLVGCKLDMR-TDLSTL--------RELSKQRLIPvtH 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622963184 172 EKGREVAKELG-IPYYE-TSVFDQFGIKDVFDNAIRAALiSRRHLQFWKSHLKKVQK 226
Cdd:cd04173   138 EQGSLLARQLGaVAYVEcSSRMSENSVRDVFHVTTLASV-RREHPSLKRSTSRRGLK 193
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
15-205 1.57e-24

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. 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 mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 100.22  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICaRACNTTLTQyqllaTHVPTVwAIDQyrvcqevleRSRDV-VDEVSVSLRLWDTFGDHhkdr 93
Cdd:cd00154     1 FKIVLIGDSGVGKTSLLL-RFVDNKFSE-----NYKSTI-GVDF---------KSKTIeVDGKKVKLQIWDTAGQE---- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  94 RFA------YGRSDVVVLCFSIANPNSLNHVKSmWYPEIKHFCP-RTPVVLVGCQLDLryADLEAVnrarrplarpikrg 166
Cdd:cd00154    61 RFRsitssyYRGAHGAILVYDVTNRESFENLDK-WLNELKEYAPpNIPIILVGNKSDL--EDERQV-------------- 123
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622963184 167 dilPPEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:cd00154   124 ---STEEAQQFAKENGLLFFETSAKTGENVDEAFESLAR 159
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
16-211 4.09e-22

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: 94.16  E-value: 4.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLIcaracnTTLTQYQLLATHVPTV---WAIDQYrvcqevlersrdvVDEVSVSLRLWDTFGDHHKD 92
Cdd:cd04134     2 KVVVLGDGACGKTSLL------NVFTRGYFPQVYEPTVfenYIHDIF-------------VDGLAVELSLWDTAGQEEFD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 --RRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLRYADLEAVNRARrplarpikrgdILP 170
Cdd:cd04134    63 rlRSLSYADTHVIMLCFSVDNPDSLENVESKWLAEIRHHCPGVKLVLVALKCDLREPRNERDRGTH-----------TIS 131
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622963184 171 PEKGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRAALISR 211
Cdd:cd04134   132 YEEGLAVAKRINaCRYLECSAKLNRGVNEAFTEAARVALNAR 173
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
484-566 2.09e-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: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDlDPLELIALA 563
Cdd:cd18186     1 LCDVTLVVGGREFPAHRAVLAARSPYFRAMFSSGMKESSSSEIELDDVSPEAFEALLDYIYTGELELSEE-NVEELLAAA 79

                  ...
gi 1622963184 564 NRF 566
Cdd:cd18186    80 DKL 82
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
15-208 4.99e-17

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 79.09  E-value: 4.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   15 IKCVVVGDNAVGKTRLICaRACNTTLTQyqllaTHVPTVwAIDQyrvcqevleRSRDV-VDEVSVSLRLWDTFGDHhkdr 93
Cdd:smart00175   1 FKIILIGDSGVGKSSLLS-RFTDGKFSE-----QYKSTI-GVDF---------KTKTIeVDGKRVKLQIWDTAGQE---- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   94 RF-----AYGR-SDVVVLCFSIANPNSLNHVKSmWYPEIKHFC-PRTPVVLVGCQLDLryADLEAVNRarrplarpikrg 166
Cdd:smart00175  61 RFrsitsSYYRgAVGALLVYDITNRESFENLEN-WLKELREYAsPNVVIMLVGNKSDL--EEQRQVSR------------ 125
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1622963184  167 dilppEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:smart00175 126 -----EEAEAFAEEHGLPFFETSAKTNTNVEEAFEELAREIL 162
BTB_POZ_BTBD9 cd18287
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
475-574 8.27e-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: 8.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 475 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLS-PNLD 553
Cdd:cd18287    13 IGALFLNEEYSDVTFVVEEKRFPAHRVILAARSEYFRALLYGGMRESQQSEIELKDTNAEAFKALLKYIYTGRLTlTDLK 92
                          90       100
                  ....*....|....*....|..
gi 1622963184 554 LDP-LELIALANRFCLPHLVAL 574
Cdd:cd18287    93 EDVlLDVLGLAHQYGFEELEAA 114
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
476-581 1.78e-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: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 476 KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLD 555
Cdd:pfam00651   2 NELREQGELCDVTLVVGDKEFRAHKAVLAACSPYFKALFSGQESESSVSEITLDDVSPEDFEALLEFMYTGKLISEENVD 81
                          90       100
                  ....*....|....*....|....*.
gi 1622963184 556 plELIALANRFCLPHLVALAEQHAVQ 581
Cdd:pfam00651  82 --DLLAAADKLQIPSLVDKCEEFLIK 105
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
486-583 2.61e-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: 2.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  486 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDpLELIALANR 565
Cdd:smart00225   1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSEIYLDDVSPEDFRALLNFLYTGKLDLPEENV-EELLELADY 79
                           90
                   ....*....|....*...
gi 1622963184  566 FCLPHLVALAEQHAVQEL 583
Cdd:smart00225  80 LQIPGLVELCEEFLLKLL 97
BTB2_POZ_BTBD8 cd18286
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
481-578 2.93e-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: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 481 KGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDPLELI 560
Cdd:cd18286    14 NGEDSDITIKVDGKTFKAHRCILCARSSYFAAMLSGSWAESNSSEITLTGVSHAAVSFVLLFIYGGVLDLPDDVNLGELL 93
                          90
                  ....*....|....*...
gi 1622963184 561 ALANRFCLPHLVALAEQH 578
Cdd:cd18286    94 SLADMYGLDGLKDVVAYT 111
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
14-202 4.66e-12

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 64.70  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  14 TIKCVVVGDNAVGKtrlicaracnTTLTqYQLLATHVptvwAIDQYR--VCQEVLERSrDVVDEVSVSLRLWDTFG--DH 89
Cdd:TIGR00231   1 DIKIVIVGHPNVGK----------STLL-NSLLGNKG----SITEYYpgTTRNYVTTV-IEEDGKTYKFNLLDTAGqeDY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  90 HKDRRFAYGRSDVVVLCFSIANP-NSLNHVKSMWYPEIKHFCPR-TPVVLVGCQLDLRYADleavnrarrplarpikrgd 167
Cdd:TIGR00231  65 DAIRRLYYPQVERSLRVFDIVILvLDVEEILEKQTKEIIHHADSgVPIILVGNKIDLKDAD------------------- 125
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622963184 168 iLPPEKGREVAKELGIPYYETSVFDQFGIKDVFDN 202
Cdd:TIGR00231 126 -LKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKI 159
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
18-201 5.32e-12

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 64.40  E-value: 5.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  18 VVVGDNAVGKTRLIcaracNTTLTQYQLL--ATHVPTVWaIDQYRVcqevlersrdVVDEVSVSLRLWDTFG-------D 88
Cdd:cd00882     1 VVVGRGGVGKSSLL-----NALLGGEVGEvsDVPGTTRD-PDVYVK----------ELDKGKVKLVLVDTPGldefgglG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  89 HHKDRRFAYGRSDVVVLCFSIANPNSLNHVKSMWypEIKHFCPRTPVVLVGCQLDLRYADleavnrarrplarpikrgDI 168
Cdd:cd00882    65 REELARLLLRGADLILLVVDSTDRESEEDAKLLI--LRRLRKEGIPIILVGNKIDLLEER------------------EV 124
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622963184 169 LPPEKGREVAKELGIPYYETSVFDQFGIKDVFD 201
Cdd:cd00882   125 EELLRLEELAKILGVPVFEVSAKTGEGVDELFE 157
BACK_RHOBTB3 cd18532
BACK (BTB and C-terminal Kelch) domain found in Rho-related BTB domain-containing protein 3 ...
597-670 6.06e-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: 6.06e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622963184 597 VLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKfrKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKRER 670
Cdd:cd18532     5 VVSLLRKAKFHNADQLSTWLLHFIASNYLIFSQK--PEFQDLSAEERDFVETHRWPSSMYLQELAEYRQHIHSR 76
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
16-205 1.23e-11

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras 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 Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 63.31  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVwaidqyrvcqEVLERSRDVVDEVSVSLRLWDTFGDH-HKDRR 94
Cdd:cd00876     1 KLVVLGAGGVGKSALTIRFVSGEFVEEY------DPTI----------EDSYRKQIVVDGETYTLDILDTAGQEeFSAMR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FAYGRS-DVVVLCFSIANPNSLNHVKSMwYPEIK--HFCPRTPVVLVGCQLDLryADLEAVnrarrplarpikrgdilPP 171
Cdd:cd00876    65 DQYIRNgDGFILVYSITSRESFEEIKNI-REQILrvKDKEDVPIVLVGNKCDL--ENERQV-----------------ST 124
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622963184 172 EKGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:cd00876   125 EEGEALAEEWGCPFLETSAKTNINIDELFNTLVR 158
BTB2_POZ_RHOBTB3 cd18360
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
484-583 4.13e-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: 60.25  E-value: 4.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDPLELIALA 563
Cdd:cd18360    10 LADVVFKIQGTTVPAHRAVLVARCEVMAAMFNGNYAEAKSFLVPIYGVSKDTFLSFLEYLYTDSCCPASILQAMALLICA 89
                          90       100
                  ....*....|....*....|
gi 1622963184 564 NRFCLPHLVALAEQHAVQEL 583
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 ...
484-574 4.15e-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: 4.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDpLELIALA 563
Cdd:cd18314     6 FSDVVLCVGDRKFFAHRIVLCARSPVFRSMLTGSMIESNLKEVTLEDVEPEIFETVLKYMYTGQVTLSEENV-LDLLMLA 84
                          90
                  ....*....|.
gi 1622963184 564 NRFCLPHLVAL 574
Cdd:cd18314    85 SKYQVPDLEKL 95
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
18-189 5.48e-11

Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell lines, but is distributed widely in various human tissues and cell lines. It is believed to be a novel Rab protein involved in regulating Golgi-associated vesicular transport during cellular endocytosis. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133311 [Multi-domain]  Cd Length: 211  Bit Score: 62.85  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  18 VVVGDNAVGKTRLIcaracnTTLTQYQLLATHVPTVwAIDQYrvcqevlERSRDVVDEVSVSLRLWDTFGdhhkDRRF-- 95
Cdd:cd04111     6 IVIGDSTVGKSSLL------KRFTEGRFAEVSDPTV-GVDFF-------SRLIEIEPGVRIKLQLWDTAG----QERFrs 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  96 ---AYGRSDV-VVLCFSIANPNSLNHVKSmWYPEIK-HFCPRTPV-VLVGCQLDLRyaDLEAVNRarrplarpikrgdil 169
Cdd:cd04111    68 itrSYYRNSVgVLLVFDITNRESFEHVHD-WLEEARsHIQPHRPVfILVGHKCDLE--SQRQVTR--------------- 129
                         170       180
                  ....*....|....*....|
gi 1622963184 170 ppEKGREVAKELGIPYYETS 189
Cdd:cd04111   130 --EEAEKLAKDLGMKYIETS 147
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
16-208 1.09e-10

Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways through the Golgi and from endosomes to the Golgi. Rab6A of mammals is implicated in retrograde transport through the Golgi stack, and is also required for a slow, COPI-independent, retrograde transport pathway from the Golgi to the endoplasmic reticulum (ER). This pathway may allow Golgi residents to be recycled through the ER for scrutiny by ER quality-control systems. Yeast Ypt6p, the homolog of the mammalian Rab6 GTPase, is not essential for cell viability. Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206654 [Multi-domain]  Cd Length: 161  Bit Score: 60.71  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLIcaracnTTLTQYQLLATHVPTVwAIDQYRVCQEvlersrdvVDEVSVSLRLWDTFGdhhkDRRF 95
Cdd:cd01861     2 KLVFLGDQSVGKTSII------TRFMYDTFDNQYQATI-GIDFLSKTMY--------VDDKTVRLQLWDTAG----QERF 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  96 -----AYGR-SDVVVLCFSIANPNSLNHVKSmWYPEIKHFCPRTP-VVLVGCQLDLryADLEAVnrarrplarpikrgdi 168
Cdd:cd01861    63 rslipSYIRdSSVAVVVYDITNRQSFDNTDK-WIDDVRDERGNDViIVLVGNKTDL--SDKRQV---------------- 123
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622963184 169 lPPEKGREVAKELGIPYYETSVFDQFGIKDVFDNaIRAAL 208
Cdd:cd01861   124 -STEEGEKKAKENNAMFIETSAKAGHNVKQLFKK-IAQAL 161
H_N_K_Ras_like cd04138
Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B; H-Ras/N-Ras/K-Ras subfamily. H-Ras, ...
16-205 1.16e-10

Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B; H-Ras/N-Ras/K-Ras subfamily. H-Ras, N-Ras, and K-Ras4A/4B are the prototypical members of the Ras family. These isoforms generate distinct signal outputs despite interacting with a common set of activators and effectors, and are strongly associated with oncogenic progression in tumor initiation. Mutated versions of Ras that are insensitive to GAP stimulation (and are therefore constitutively active) are found in a significant fraction of human cancers. Many Ras guanine nucleotide exchange factors (GEFs) have been identified. They are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active (GTP-bound) Ras interacts with several effector proteins that stimulate a variety of diverse cytoplasmic signaling activities. Some are known to positively mediate the oncogenic properties of Ras, including Raf, phosphatidylinositol 3-kinase (PI3K), RalGEFs, and Tiam1. Others are proposed to play negative regulatory roles in oncogenesis, including RASSF and NORE/MST1. Most Ras 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 Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133338 [Multi-domain]  Cd Length: 162  Bit Score: 60.51  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTrlicarACNTTLTQYQLLATHVPTVWaiDQYRvcQEVlersrdVVDEVSVSLRLWDTFG-DHHKDRR 94
Cdd:cd04138     3 KLVVVGAGGVGKS------ALTIQLIQNHFVDEYDPTIE--DSYR--KQV------VIDGETCLLDILDTAGqEEYSAMR 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FAYGRSDVVVLC-FSIANPNSLNHVkSMWYPEIKHFCPRT--PVVLVGCQLDLRYADLeavnrarrplarpikrgdilPP 171
Cdd:cd04138    67 DQYMRTGEGFLCvFAINSRKSFEDI-HTYREQIKRVKDSDdvPMVLVGNKCDLAARTV--------------------ST 125
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622963184 172 EKGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:cd04138   126 RQGQDLAKSYGIPYIETSAKTRQGVEEAFYTLVR 159
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
15-200 1.97e-10

Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family of small GTPases. In mouse, Rab23 has been shown to function as a negative regulator in the sonic hedgehog (Shh) signaling pathway. Rab23 mediates the activity of Gli2 and Gli3, transcription factors that regulate Shh signaling in the spinal cord, primarily by preventing Gli2 activation in the absence of Shh ligand. Rab23 also regulates a step in the cytoplasmic signal transduction pathway that mediates the effect of Smoothened (one of two integral membrane proteins that are essential components of the Shh signaling pathway in vertebrates). In humans, Rab23 is expressed in the retina. Mice contain an isoform that shares 93% sequence identity with the human Rab23 and an alternative splicing isoform that is specific to the brain. This isoform causes the murine open brain phenotype, indicating it may have a role in the development of the central nervous system. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133306 [Multi-domain]  Cd Length: 162  Bit Score: 59.76  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLIcARACNTTLTqyqllathvptvwaiDQYR--VCQEVLERSRDV-VDEVSVSLRLWDTFGDHHK 91
Cdd:cd04106     1 IKVIVVGNGNVGKSSMI-QRFVKGIFT---------------KDYKktIGVDFLEKQIFLrQSDEDVRLMLWDTAGQEEF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  92 D--RRFAYGRSDVVVLCFSIANPNSLNHVkSMWYPEIKHFCPRTPVVLVGCQLDLryADlEAVNRArrplarpikrgdil 169
Cdd:cd04106    65 DaiTKAYYRGAQACILVFSTTDRESFEAI-ESWKEKVEAECGDIPMVLVQTKIDL--LD-QAVITN-------------- 126
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622963184 170 ppEKGREVAKELGIPYYETSVFDQFGIKDVF 200
Cdd:cd04106   127 --EEAEALAKRLQLPLFRTSVKDDFNVTELF 155
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
475-577 2.41e-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: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 475 IKECLSKGTFSDVTFKLDDGA--ISAHKPLLICSCEWMAAMFGGSFV-ESANSEVYLPNINKISMQAVLDYLYTKQLSpn 551
Cdd:cd18294     5 MKSLINNPEFSDVKFLVGPERqeIFAHKCILAARCEVFRAMFLTGPQkESTQSPLVLSDIEPEVFRAVLEFIYTNCVT-- 82
                          90       100
                  ....*....|....*....|....*....
gi 1622963184 552 ldLDP---LELIALANRFCLPHLVALAEQ 577
Cdd:cd18294    83 --LSNhtvIEVLAAAVEYGLDELRKLCER 109
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
15-145 4.46e-10

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: 58.89  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICAracnttltqyqlLATH--VPTVwaidqyrvcQEVLERSR---DVVDEvSVSLRLWDTFGD- 88
Cdd:cd01893     3 VRIVLIGDEGVGKSSLIMS------------LVSEefPENV---------PRVLPEITipaDVTPE-RVPTTIVDTSSRp 60
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622963184  89 -HHKDRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVVLVGCQLDLR 145
Cdd:cd01893    61 qDRANLAAEIRKANVICLVYSVDRPSTLERIRTKWLPLIRRLGVKVPIILVGNKSDLR 118
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
16-200 8.43e-10

Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small GTPases of the ARF, RAB, RAN, RAS, and SAR subfamilies. Others that could not be classified in this way are predicted to be members of the small GTPase superfamily without predictions of the subfamily.


Pssm-ID: 197466 [Multi-domain]  Cd Length: 166  Bit Score: 57.96  E-value: 8.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   16 KCVVVGDNAVGKTRLicaracntT--LTQYQLLATHVPTVWaiDQYRvcQEVlersrdVVDEVSVSLRLWDTFGDHhkdr 93
Cdd:smart00010   4 KLVVLGGGGVGKSAL--------TiqFVQGHFVDEYDPTIE--DSYR--KQI------EIDGEVCLLDILDTAGQE---- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   94 RFA-----YGRS-DVVVLCFSIANPNSLNHVKSMwYPEIKHF--CPRTPVVLVGCQldlryADLEAvnrarrplarpiKR 165
Cdd:smart00010  62 EFSamrdqYMRTgEGFLLVYSITDRQSFEEIAKF-REQILRVkdRDDVPIVLVGNK-----CDLEN------------ER 123
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622963184  166 gdILPPEKGREVAKELGIPYYETSVFDQFGIKDVF 200
Cdd:smart00010 124 --VVSTEEGKELARQWGCPFLETSAKERINVDEAF 156
BTB_POZ_RCBTB1_2 cd18298
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
485-578 9.02e-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: 9.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 485 SDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQ--LSPNldlDPLELIAL 562
Cdd:cd18298    13 SDLKFRVDGKYIYVHKAILKIRCEYFRSMFQSHWNEDDKNVIEIDQYSYPVYYAFLRYLYTDQvdLPPE---DAIGLLDL 89
                          90
                  ....*....|....*.
gi 1622963184 563 ANRFCLPHLVALAEQH 578
Cdd:cd18298    90 ANSYCEERLKKLCEDI 105
BTB_POZ_KLHL26 cd18255
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
480-589 1.38e-09

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: 56.25  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 480 SKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSpnLDLDPLE- 558
Cdd:cd18255    14 AKGQLLDVTLIADGQRFQAHKVVLASCSDYFRAMFTGGMRESSQDEIELKGVSAKGLKHILDFAYTSELT--LDLDCIQd 91
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622963184 559 LIALANrfclpHLVALAEQHAVQELTKAAMS 589
Cdd:cd18255    92 VLGAAV-----HLQMLPVVELCEEFLKSAMS 117
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
16-200 1.39e-09

Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early endosome compartments, but not with late endosomal markers. It codistributes with Rab4 and Rab5 on early/sorting endosomes, and with Rab11 on pericentriolar recycling endosomes. It is believed to function as an inhibitory GTPase that regulates distinct steps in early endocytic trafficking. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206698 [Multi-domain]  Cd Length: 164  Bit Score: 57.68  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICaracntTLTQYQLLATHVPTVwAIDqYRVcqEVLErsrdvVDEVSVSLRLWDTFGD--HHKDR 93
Cdd:cd04117     2 RLLLIGDSGVGKTCLLC------RFTDNEFHSSHISTI-GVD-FKM--KTIE-----VDGIKVRIQIWDTAGQerYQTIT 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  94 RFAYGRSDVVVLCFSIANPNSLNHVKSmWYPEIKHFCPR-TPVVLVGcqldlryadleavNRARRPLARPIkrgdilPPE 172
Cdd:cd04117    67 KQYYRRAQGIFLVYDISSERSYQHIMK-WVSDVDEYAPEgVQKILIG-------------NKADEEQKRQV------GDE 126
                         170       180
                  ....*....|....*....|....*...
gi 1622963184 173 KGREVAKELGIPYYETSVFDQFGIKDVF 200
Cdd:cd04117   127 QGNKLAKEYGMDFFETSACTNKNIKESF 154
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
16-205 1.44e-09

Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G protein receptors to protein kinase cascades


Pssm-ID: 214541 [Multi-domain]  Cd Length: 164  Bit Score: 57.57  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   16 KCVVVGDNAVGKTrlicarACNTTLTQYQLLATHVPTVWaiDQYRvcQEVlersrdVVDEVSVSLRLWDTFGDHhkdrRF 95
Cdd:smart00173   2 KLVVLGSGGVGKS------ALTIQFIQGHFVDDYDPTIE--DSYR--KQI------EIDGEVCLLDILDTAGQE----EF 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184   96 A-----YGRS-DVVVLCFSIANPNSLNHVKSMwYPEIKHF--CPRTPVVLVGCQldlryADLEAvnrarrplarpiKRgd 167
Cdd:smart00173  62 SamrdqYMRTgEGFLLVYSITDRQSFEEIKKF-REQILRVkdRDDVPIVLVGNK-----CDLES------------ER-- 121
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1622963184  168 ILPPEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:smart00173 122 VVSTEEGKELARQWGCPFLETSAKERVNVDEAFYDLVR 159
BTB_POZ_ABTB2-like cd18297
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
483-576 3.60e-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: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 483 TFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSpNLDLDP---LEL 559
Cdd:cd18297    11 EMSDVTFLVEGRPFYAHKIVLVTASDRFKSMLSSGSTEAQTPVIEIPDIRYDIFQLMMQYLYTGGVE-SLDVAQddaLEL 89
                          90
                  ....*....|....*..
gi 1622963184 560 IALANRFCLPHLVALAE 576
Cdd:cd18297    90 LRAASFFQLDGLKRHCE 106
BTB_POZ_KLHL34 cd18264
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
480-584 3.64e-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: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 480 SKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSpnLDLDPLEL 559
Cdd:cd18264    24 AEGFLCDVVLEAEGNEFPAHRSLLACSSDYFRALFKDYTQESKARVIHLPVVSAAGLQRVLDFIYTSWLS--LSLDTLED 101
                          90       100
                  ....*....|....*....|....*.
gi 1622963184 560 IALANRFC-LPHLVALAEQHAVQELT 584
Cdd:cd18264   102 TLEAASYLqVTEAIGLCSQYLINNLA 127
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
16-208 9.14e-09

Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206655 [Multi-domain]  Cd Length: 172  Bit Score: 55.36  E-value: 9.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLIcARACNTTLTQyqllathvptvwaidQYR-------VCQEVlersrdVVDEVSVSLRLWDTFGd 88
Cdd:cd01862     2 KVIILGDSGVGKTSLM-NQYVNKKFSN---------------QYKatigadfLTKEV------TVDDRLVTLQIWDTAG- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  89 hhkDRRFA------YGRSDVVVLCFSIANPNSLNHVKSmWYPE-IKHFCPRT----PVVLVGCQLDLryadleAVNRArr 157
Cdd:cd01862    59 ---QERFQslgvafYRGADCCVLVYDVTNPKSFESLDS-WRDEfLIQASPRDpenfPFVVLGNKIDL------EEKRQ-- 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622963184 158 plarpikrgdiLPPEKGREVAKELG-IPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:cd01862   127 -----------VSTKKAQQWCKSKGnIPYFETSAKEAINVDQAFETIARLAL 167
BTB_POZ_KLHL3 cd18339
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
468-548 1.79e-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: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 468 HVRKANRI-KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTK 546
Cdd:cd18339     4 HMKKAFKVmNELRSKQLLCDVTIVAEDVEIEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTA 83

                  ..
gi 1622963184 547 QL 548
Cdd:cd18339    84 EI 85
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
16-201 2.30e-08

Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206657 [Multi-domain]  Cd Length: 165  Bit Score: 54.15  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLIcARACNTTLTqyqllATHVPTVwAIDqYRVcQEVLERSRdvvdevSVSLRLWDTFG-DHHKDRR 94
Cdd:cd01865     3 KLLIIGNSSVGKTSFL-FRYADDSFT-----SAFVSTV-GID-FKV-KTVYRNDK------RIKLQIWDTAGqERYRTIT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FAYGRSDV-VVLCFSIANPNSLNHVKSmWYPEIKHFCPRTP-VVLVGCQLDLryadleavnrarrplarpiKRGDILPPE 172
Cdd:cd01865    68 TAYYRGAMgFILMYDITNEESFNAVQD-WSTQIKTYSWDNAqVILVGNKCDM-------------------EDERVVSAE 127
                         170       180
                  ....*....|....*....|....*....
gi 1622963184 173 KGREVAKELGIPYYETSVFDQFGIKDVFD 201
Cdd:cd01865   128 RGRQLADQLGFEFFEASAKENINVKQVFE 156
BTB_POZ_KLHL22 cd18251
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
482-553 2.58e-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: 2.58e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622963184 482 GTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLD 553
Cdd:cd18251    21 GILFDVVLVVEGKPIEAHRILLAASCDYFRGMFAGGLREMQQTEVLIHGVSYNAMCKILDFIYTSELELSLD 92
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
15-205 3.04e-08

Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206656 [Multi-domain]  Cd Length: 161  Bit Score: 53.47  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQyqllatHVPTVwAIDqYRVcqEVLErsrdvVDEVSVSLRLWDTFGdhhkDRR 94
Cdd:cd01863     1 LKILLIGDSGVGKSSLLLRFTDDTFDED------LSSTI-GVD-FKV--KTVT-----VDGKKVKLAIWDTAG----QER 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 F-----AYGR-SDVVVLCFSIANPNSLNHVKSmWYPEIKHFCPRTPVV--LVGCQLDLryadleaVNRArrplarpikrg 166
Cdd:cd01863    62 FrtltsSYYRgAQGVILVYDVTRRDTFDNLDT-WLNELDTYSTNPDAVkmLVGNKIDK-------ENRE----------- 122
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622963184 167 diLPPEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:cd01863   123 --VTREEGQKFARKHNMLFIETSAKTRIGVQQAFEELVE 159
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
16-200 3.09e-08

Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in every eukaryote and is a key regulatory component for the transport of vesicles from the ER to the Golgi apparatus. Studies on mutations of Ypt1, the yeast homolog of Rab1, showed that this protein is necessary for the budding of vesicles of the ER as well as for their transport to, and fusion with, the Golgi apparatus. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206661 [Multi-domain]  Cd Length: 166  Bit Score: 53.49  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICaRACNTTLTQyqllaTHVPTVWAIDQYRVCQevlersrdvVDEVSVSLRLWDTFGDhhkdRRF 95
Cdd:cd01869     4 KLLLIGDSGVGKSCLLL-RFADDTYTE-----SYISTIGVDFKIRTIE---------LDGKTVKLQIWDTAGQ----ERF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  96 -----AYGR-SDVVVLCFSIANPNSLNHVKSmWYPEIKHF-CPRTPVVLVGCQLDLryADLEAVNrarrplarpikrgdi 168
Cdd:cd01869    65 rtitsSYYRgAHGIIIVYDVTDQESFNNVKQ-WLQEIDRYaSENVNKLLVGNKCDL--TDKKVVD--------------- 126
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622963184 169 lpPEKGREVAKELGIPYYETSVFDQFGIKDVF 200
Cdd:cd01869   127 --YTEAKEFADELGIPFLETSAKNATNVEEAF 156
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
16-143 3.82e-08

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 52.12  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLIcARACNTTLTQYQLlathvPTVwAIDQYrvCQEVLERSRDVVDevsVSLRLWDTFGD--HHKDR 93
Cdd:pfam08477   1 KVVLLGDSGVGKTSLL-KRFVDDTFDPKYK-----STI-GVDFK--TKTVLENDDNGKK---IKLNIWDTAGQerFRSLH 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622963184  94 RFAYGRSDVVVLCFSIANPNSLNHvksmWYPEIKHFCPRTPVVLVGCQLD 143
Cdd:pfam08477  69 PFYYRGAAAALLVYDSRTFSNLKY----WLRELKKYAGNSPVILVGNKID 114
BTB_POZ_KLHL2_Mayven cd18338
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
468-548 4.55e-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: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 468 HVRKANRI-KECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTK 546
Cdd:cd18338     4 HMKKAFKVmNELRSQNLLCDVTIVAEDVEIAAHRVVLAACSPYFHAMFTGEMSESRAKRVRIKEVDGWTLKMLIDYVYTA 83

                  ..
gi 1622963184 547 QL 548
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 ...
483-584 5.83e-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: 51.71  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 483 TFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLdPLELIAL 562
Cdd:cd18352    12 TLSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEIPNIRWEVFELMMRFIYTGSVDITNDI-AKDLLRA 90
                          90       100
                  ....*....|....*....|..
gi 1622963184 563 ANRFCLPHLVALAEQHAVQELT 584
Cdd:cd18352    91 ADQYLLEGLKRLCEYTIAQDLT 112
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
15-201 5.84e-08

Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, with conflicting data reported. Rab21 has been reported to localize in the ER in human intestinal epithelial cells, with partial colocalization with alpha-glucosidase, a late endosomal/lysosomal marker. More recently, Rab21 was shown to colocalize with and affect the morphology of early endosomes. In Dictyostelium, GTP-bound Rab21, together with two novel LIM domain proteins, LimF and ChLim, has been shown to regulate phagocytosis. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133323 [Multi-domain]  Cd Length: 162  Bit Score: 52.61  E-value: 5.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLIcARACNTTLTQyqllaTHVPTVwaidqyrvcQEVLERSRDVVDEVSVSLRLWDTFGdhhKDRR 94
Cdd:cd04123     1 FKVVLLGEGRVGKTSLV-LRYVENKFNE-----KHESTT---------QASFFQKTVNIGGKRIDLAIWDTAG---QERY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FA-----YGRSDVVVLCFSIANPNSLNHVKSmWYPEIKHFCPRT-PVVLVGCQLDLryadleavnrarrplarPIKRgdI 168
Cdd:cd04123    63 HAlgpiyYRDADGAILVYDITDADSFQKVKK-WIKELKQMRGNNiSLVIVGNKIDL-----------------ERQR--V 122
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622963184 169 LPPEKGREVAKELGIPYYETSVFDQFGIKDVFD 201
Cdd:cd04123   123 VSKSEAEEYAKSVGAKHFETSAKTGKGIEELFL 155
M_R_Ras_like cd04145
R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, ...
13-206 6.22e-08

R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, and related members of the Ras family. M-Ras is expressed in lympho-hematopoetic cells. It interacts with some of the known Ras effectors, but appears to also have its own effectors. Expression of mutated M-Ras leads to transformation of several types of cell lines, including hematopoietic cells, mammary epithelial cells, and fibroblasts. Overexpression of M-Ras is observed in carcinomas from breast, uterus, thyroid, stomach, colon, kidney, lung, and rectum. In addition, expression of a constitutively active M-Ras mutant in murine bone marrow induces a malignant mast cell leukemia that is distinct from the monocytic leukemia induced by H-Ras. TC21, along with H-Ras, has been shown to regulate the branching morphogenesis of ureteric bud cell branching in mice. Most Ras 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 Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133345 [Multi-domain]  Cd Length: 164  Bit Score: 52.80  E-value: 6.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  13 ETIKCVVVGDNAVGKTrlicarACNTTLTQYQLLATHVPTVWaiDQY-RVCQevlersrdvVDEVSVSLRLWDTFG-DHH 90
Cdd:cd04145     1 PTYKLVVVGGGGVGKS------ALTIQFIQSYFVTDYDPTIE--DSYtKQCE---------IDGQWARLDILDTAGqEEF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  91 KDRRFAYGRS-DVVVLCFSIANPNSLNHVKSMwYPEIKHFCPRT--PVVLVGCQLDLRYadleavnraRRPLARpikrgd 167
Cdd:cd04145    64 SAMREQYMRTgEGFLLVFSVTDRGSFEEVDKF-HTQILRVKDRDefPMILVGNKADLEH---------QRQVSR------ 127
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622963184 168 ilppEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIRA 206
Cdd:cd04145   128 ----EEGQELARQLKIPYIETSAKDRVNVDKAFHDLVRV 162
BTB_POZ_KLHL7 cd18237
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
481-569 6.80e-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: 6.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 481 KGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDLDPLELI 560
Cdd:cd18237    18 QKTLCDVILIVEGREIKAHRVVLAAASHFFHLMFTSNMTESKSSEVELKDAEPDIIELLVEFAYTARISVN-SNNVQSLL 96

                  ....*....
gi 1622963184 561 ALANRFCLP 569
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 ...
480-585 8.98e-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: 8.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 480 SKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQ--LSPNLDLDpl 557
Cdd:cd18261    24 NDGILCDITLVAEEQKFHAHKAVLAACSDYFRAMFSLCMVESEADEVNLHGVTSLGLKQALDFAYTGQilLEPGVIQD-- 101
                          90       100
                  ....*....|....*....|....*...
gi 1622963184 558 eLIALANRFCLPHLVALAEQHAVQELTK 585
Cdd:cd18261   102 -VLAAGSHLQLLELLSLCSHYLIQELNS 128
RabL2 cd04124
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ...
15-208 1.34e-07

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: 51.78  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLIcaracnttltQYQLLATHVPTvwaidQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHhkdrR 94
Cdd:cd04124     1 VKIILLGDSAVGKSKLV----------ERFLMDGYEPQ-----QLSTYALTLYKHNAKFEGKTILVDFWDTAGQE----R 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FA------YGRSDVVVLCFSIANPNSLNHVKSmWYPEIKHFCPRTPVVLVGCQLDLryadleavnrarrplarpikrgDI 168
Cdd:cd04124    62 FQtmhasyYHKAHACILVFDVTRKITYKNLSK-WYEELREYRPEIPCIVVANKIDL----------------------DP 118
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622963184 169 LPPEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAAL 208
Cdd:cd04124   119 SVTQKKFNFAEKHNLPLYYVSAADGTNVVKLFQDAIKLAV 158
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
15-189 2.32e-07

Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly homologous isoform, Rab27b. Unlike most Rab proteins whose functions remain poorly defined, Rab27a has many known functions. Rab27a has multiple effector proteins, and depending on which effector it binds, Rab27a has different functions as well as tissue distribution and/or cellular localization. Putative functions have been assigned to Rab27a when associated with the effector proteins Slp1, Slp2, Slp3, Slp4, Slp5, DmSlp, rabphilin, Dm/Ce-rabphilin, Slac2-a, Slac2-b, Slac2-c, Noc2, JFC1, and Munc13-4. Rab27a has been associated with several human diseases, including hemophagocytic syndrome (Griscelli syndrome or GS), Hermansky-Pudlak syndrome, and choroidermia. In the case of GS, a rare, autosomal recessive disease, a Rab27a mutation is directly responsible for the disorder. When Rab27a is localized to the secretory granules of pancreatic beta cells, it is believed to mediate glucose-stimulated insulin secretion, making it a potential target for diabetes therapy. When bound to JFC1 in prostate cells, Rab27a is believed to regulate the exocytosis of prostate- specific markers. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206700 [Multi-domain]  Cd Length: 180  Bit Score: 51.35  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQYqllathVPTVwAID--QYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHhkd 92
Cdd:cd04127     5 IKLLALGDSGVGKTTFLYRYTDNKFNPKF------ITTV-GIDfrEKRVVYNSQGPDGTSGKAFRVHLQLWDTAGQE--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  93 rRF-----AYGRSDV-VVLCFSIANPNSLNHVKSmWYPEIKH--FCPRTPVVLVGCQLDLryADLEAVNRARrplarpik 164
Cdd:cd04127    75 -RFrslttAFFRDAMgFLLMFDLTSEQSFLNVRN-WMSQLQAhaYCENPDIVLIGNKADL--PDQREVSERQ-------- 142
                         170       180
                  ....*....|....*....|....*
gi 1622963184 165 rgdilppekGREVAKELGIPYYETS 189
Cdd:cd04127   143 ---------ARELADKYGIPYFETS 158
BTB_POZ_Rank-5 cd18303
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
475-577 2.63e-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: 49.63  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 475 IKECLSKGTFSDVTFKLDDGAISAHKPLLIC-SCEWmaamfggSFVESAN-SEVYLPNINKISMQAVLDYLYTKQLSPNL 552
Cdd:cd18303     9 VASLFDKELYSDITIKLADKSIPAHKFVLAArSEKW-------SNENLAStNELDLSDISYEVVLALLRWLYTDELDLTL 81
                          90       100
                  ....*....|....*....|....*.
gi 1622963184 553 DLDPL-ELIALANRFCLPHLVALAEQ 577
Cdd:cd18303    82 DDEFLlELMKAAKRFQLTDLVERCER 107
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
15-200 3.26e-07

Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206659 [Multi-domain]  Cd Length: 167  Bit Score: 50.73  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLIcARACNTTLTQyqllaTHVPTVwAIDqYRVcqevleRSRDVvDEVSVSLRLWDTFGDHhkdrR 94
Cdd:cd01867     4 FKLLLIGDSGVGKSCLL-LRFSEDSFNP-----SFISTI-GID-FKI------RTIEL-DGKKIKLQIWDTAGQE----R 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 F-----AYGR-SDVVVLCFSIANPNSLNHVKsMWYPEI-KHFCPRTPVVLVGCQLDLryadleavnrarrplarPIKRgd 167
Cdd:cd01867    65 FrtittSYYRgAMGIILVYDITDEKSFENIK-NWMRNIdEHASEDVERMLVGNKCDM-----------------EEKR-- 124
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622963184 168 ILPPEKGREVAKELGIPYYETSVFDQFGIKDVF 200
Cdd:cd01867   125 VVSKEEGEALAREYGIKFLETSAKANINVEEAF 157
BTB_POZ_KLHL28_BTBD5 cd18257
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
486-545 3.91e-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: 49.07  E-value: 3.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 486 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYT 545
Cdd:cd18257    20 DVVLRVGDVKIHAHKVVLASCSPYFKAMFTGNLSEKENSEVEFQCIDETALQAIVEYAYT 79
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
14-200 6.41e-07

Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The Rab5-related subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206653 [Multi-domain]  Cd Length: 163  Bit Score: 49.86  E-value: 6.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  14 TIKCVVVGDNAVGKTRLICaRACNTTLTQYQLlathvPTVWAIDQYRVCQevlersrdvVDEVSVSLRLWDTFGDHhkdr 93
Cdd:cd01860     1 QFKLVLLGDSSVGKSSIVL-RFVKNEFSENQE-----STIGAAFLTQTVN---------LDDTTVKFEIWDTAGQE---- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  94 RFA-----YGR-SDVVVLCFSIANPNSLNHVKSmWYPEIK-HFCPRTPVVLVGCQLDLryADLEAVnrarrplarpikrg 166
Cdd:cd01860    62 RYRslapmYYRgAAAAIVVYDITSEESFEKAKS-WVKELQeHGPPNIVIALAGNKADL--ESKRQV-------------- 124
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622963184 167 dilPPEKGREVAKELGIPYYETSVFDQFGIKDVF 200
Cdd:cd01860   125 ---STEEAQEYADENGLLFMETSAKTGENVNELF 155
BTB_POZ cd01165
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
487-566 7.08e-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: 47.28  E-value: 7.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 487 VTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDlDPLELIALANRF 566
Cdd:cd01165     1 VVLVVEGEKFHVNKELLAQSSEYFRALFRGGFRESGQAEINLRDISPEDFRALLEFLYGGKRDLDAS-NLLELLEAANFL 79
BTB_POZ_KLHL36 cd18266
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
474-549 7.25e-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: 7.25e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622963184 474 RIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLS 549
Cdd:cd18266    15 GLNEQRQRGLFCDVVLVADEQRVPAHRNLLAVCSDYFNSMFTIGMREAHQKEVELVGASYIGLKAVIDFLYSSELP 90
BTB_POZ_KLHL18 cd18247
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
474-548 1.05e-06

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: 1.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622963184 474 RIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQL 548
Cdd:cd18247     9 VMEEIRRQGKLCDVTLKVGDQKFSAHRIVLAATIPYFHAMFTHDMVESKQDEITMQGIEPSALEALINFAYSGRI 83
BTB_POZ_roadkill-like cd18345
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
468-577 1.61e-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: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 468 HVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQ 547
Cdd:cd18345     2 ECRLSDDLGLLFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEERKQNRVEITDVDHEVMREMLRFIYTGK 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1622963184 548 lSPNLDLDPLELIALANRFCLPHLVALAEQ 577
Cdd:cd18345    82 -APNLDKMADDLLAAADKYALERLKVMCEE 110
BTB_POZ_KLHL41_KBTBD10 cd18341
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
475-569 1.74e-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: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 475 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDL 554
Cdd:cd18341    18 LKELLDENKFVDCTLKAGDKSLPCHRLILAACSPYFREYFLSEESEEKKKEVVLDNVDPNIMDMILKYLYSAEIDLN-DG 96
                          90
                  ....*....|....*
gi 1622963184 555 DPLELIALANRFCLP 569
Cdd:cd18341    97 NVQDIFALASRFQIP 111
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
16-189 1.75e-06

Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206695 [Multi-domain]  Cd Length: 191  Bit Score: 49.09  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLicaracnttLTQYQ----LLATHVPTVwaidqyrvcQEVLERSRDVVDEVSVSLRLWDTFGDhhk 91
Cdd:cd04112     2 KVMLVGDSGVGKTCL---------LVRFKdgafLAGSFIATV---------GIQFTNKVVTVDGVKVKLQIWDTAGQ--- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  92 dRRF-----AYGR-SDVVVLCFSIANPNSLNHVKSmWYPEIKHFCPRTPVVLVgcqldlryadleAVNRARRPLARPIKR 165
Cdd:cd04112    61 -ERFrsvthAYYRdAHALLLLYDVTNKSSFDNIRA-WLTEILEYAQSDVVIML------------LGNKADMSGERVVKR 126
                         170       180
                  ....*....|....*....|....
gi 1622963184 166 gdilppEKGREVAKELGIPYYETS 189
Cdd:cd04112   127 ------EDGERLAKEYGVPFMETS 144
BTB_POZ_KLHL12_C3IP1_DKIR cd18242
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
481-547 1.77e-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: 47.44  E-value: 1.77e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622963184 481 KGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQ 547
Cdd:cd18242    18 SNTLCDVTLRVEGKEFPAHRIVLAACSDYFCAMFTSEMSEKGKSEVELQGLTASTMEILLDFVYTET 84
BTB2_POZ_IBtk cd18302
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
484-584 2.77e-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: 46.59  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDG-AISAHKPLLICSCEWMAAMFGGSFVE-SANSEVYLPnINKISMQAVLDYLYTKQLSP---NLDLDPL- 557
Cdd:cd18302     5 LYDVTIVSEDGkEFPCHKCVLVARLEYFHSMLSSSWIEaSSCSALTMP-IPSDILEIILDYLYTDEASAvkeSQNVEFLc 83
                          90       100
                  ....*....|....*....|....*..
gi 1622963184 558 ELIALANRFCLPHLVALAEQHAVQELT 584
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 ...
484-574 3.00e-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: 3.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDlDPLELIALA 563
Cdd:cd18256    20 FCDVQLQVGMELFSVHRLVLAASSPYFAALFAGGMSESSKDVVQIHGVEPDIFHILLDFIYTGVVEVTVS-NVQELLVAA 98
                          90
                  ....*....|.
gi 1622963184 564 NRFCLPHLVAL 574
Cdd:cd18256    99 DMLQLTEVVEI 109
BTB1_POZ_RhoBTB cd18299
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
479-574 4.10e-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: 45.67  E-value: 4.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 479 LSKGTFSDVTFKLDDG-AISAHKPLLICSCEWMAAMFGgsfvesANSEVYL-PNINKISMQAVLDYLYTKQLspNLDLDP 556
Cdd:cd18299     7 LHSPSCADVVFILQGGvRIFAHRIVLAAASSVFADLFL------MMTVVTLdSDITPEAFRRVLEFLYTGVL--DENEDD 78
                          90
                  ....*....|....*....
gi 1622963184 557 L-ELIALANRFCLPHLVAL 574
Cdd:cd18299    79 LkELKDAAELLELFDLVMM 97
BTB_POZ_KLHL30 cd18259
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
484-551 4.16e-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: 4.16e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622963184 484 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPN 551
Cdd:cd18259    32 LSDVTLLVGGREFPCHRSVLALCSHYFNAMFTGDFVESISARVEIKDVDPAVMESLIDFAYTGKLTIN 99
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
406-455 5.52e-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: 5.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622963184  406 VQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNK 455
Cdd:smart00225  46 VSPEDFRALLNFLYTGKLDLPEENVEELLELADYLQIPGLVELCEEFLLK 95
BTB_POZ_BPM_plant cd18280
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
485-578 7.00e-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: 45.78  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 485 SDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQL--------SPNLDLDP 556
Cdd:cd18280    15 ADVTFNVDGEKFRAHKLVLAARSPVFRSMLFGPMREENEGEIVIEDVEPPVFKALLHFIYKDELpddvepagSDSSSLDT 94
                          90       100
                  ....*....|....*....|....*
gi 1622963184 557 L---ELIALANRFCLPHLVALAEQH 578
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 ...
475-569 8.75e-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: 8.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 475 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDL 554
Cdd:cd18269    18 LKDLLDENKFVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYTSEIDLN-DQ 96
                          90
                  ....*....|....*
gi 1622963184 555 DPLELIALANRFCLP 569
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 ...
478-563 1.04e-05

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: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 478 CLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFveSANSEVYL--PNINKISMQAVLDYLYTKQLspNLDLD 555
Cdd:cd18295    13 LLEQGSYSDVTFNVHGESFPAHRCILSARSPYFAEMFETKW--KDKREINLkhPLVNPDAFRALLQYLYTGRL--EIHVD 88

                  ....*....
gi 1622963184 556 PLE-LIALA 563
Cdd:cd18295    89 DVEdCKRLA 97
BTB_POZ_KLHL35 cd18265
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
482-571 1.38e-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: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 482 GTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSpnLDLDPLE-LI 560
Cdd:cd18265    21 GTFTDVVLLVDGKDFPCHRATLSANSAYFRAMFGGHLKESRQAVVEIQKVSAAAMEVLLDYMYGGGLR--IQEDNVEsVL 98
                          90
                  ....*....|.
gi 1622963184 561 ALANRFCLPHL 571
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 ...
475-553 1.48e-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: 44.59  E-value: 1.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622963184 475 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLD 553
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 ...
480-558 1.70e-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: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 480 SKGTFSDVTFKLDDG--AISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLD--LD 555
Cdd:cd18239    19 GEGLLCDVTLVPGDGdeTFPVHRAMMASASDYFKAMFTGGMKEQELMCIKLHGVSKIGLKNIIDFIYTAKLSLNMDnlQD 98

                  ...
gi 1622963184 556 PLE 558
Cdd:cd18239    99 TLE 101
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
16-205 2.14e-05

Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (>80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. Most Ras 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 Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206710 [Multi-domain]  Cd Length: 163  Bit Score: 45.11  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLicaracnTTLTQYQ-LLATHVPTVwaIDQYRvcqEVLersrdVVDEVSVSLRLWDTFG-DHHKDR 93
Cdd:cd04139     2 KVIMVGSGGVGKSAL-------TLQFMYDeFVEDYEPTK--ADSYR---KKV-----VLDGEEVQLNILDTAGqEDYAAI 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  94 RFAYGRSDVVVLC-FSIANPNSLNHVKSMWYPEIKH-FCPRTPVVLVGCQLDLryadleaVNRARRPLarpikrgdilpp 171
Cdd:cd04139    65 RDNYFRSGEGFLLvFSITDMESFTALAEFREQILRVkEDDNVPLLLVGNKCDL-------EDKRQVSV------------ 125
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622963184 172 EKGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:cd04139   126 EEAANLAEQWGVNYVETSAKTRANVDKVFFDLVR 159
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
16-205 2.18e-05

RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that is found in fungi. In budding yeasts, RSR1 is involved in selecting a site for bud growth on the cell cortex, which directs the establishment of cell polarization. The Rho family GTPase cdc42 and its GEF, cdc24, then establish an axis of polarized growth by organizing the actin cytoskeleton and secretory apparatus at the bud site. It is believed that cdc42 interacts directly with RSR1 in vivo. In filamentous fungi, polar growth occurs at the tips of hypha and at novel growth sites along the extending hypha. In Ashbya gossypii, RSR1 is a key regulator of hyphal growth, localizing at the tip region and regulating in apical polarization of the actin cytoskeleton. Most Ras 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 Ras proteins.


Pssm-ID: 133377 [Multi-domain]  Cd Length: 168  Bit Score: 45.55  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLicaracNTTLTQYQLLATHVPTVWaiDQYRvcqevlerSRDVVDEVSVSLRLWDTFG-DHHKDRR 94
Cdd:cd04177     3 KIVVLGAGGVGKSAL------TVQFVQNVFIESYDPTIE--DSYR--------KQVEIDGRQCDLEILDTAGtEQFTAMR 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FAYGRSDV-VVLCFSIANPNSLNHVKSMWYP--EIKHfCPRTPVVLVGCQLDLRyadleavnrARRplarpikrgdILPP 171
Cdd:cd04177    67 ELYIKSGQgFLLVYSVTSEASLNELGELREQvlRIKD-SDNVPMVLVGNKADLE---------DDR----------QVSR 126
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622963184 172 EKGREVAKELG-IPYYETSVFDQFGIKDVFDNAIR 205
Cdd:cd04177   127 EDGVSLSQQWGnVPFYETSARKRTNVDEVFIDLVR 161
BTB_POZ_KBTBD8 cd18274
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
474-591 2.55e-05

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: 44.21  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 474 RIKECLSKGTFSDVTFKLDDG-AISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNl 552
Cdd:cd18274    12 QLKAMYDEGQLTDIVVEVDHGkTFSCHRNVLAAISPYFRSMFTSGLTESTQKEVRIVGVEAESMHLVLDYAYTSRVTLT- 90
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622963184 553 DLDPLELIALANRFCLPHLVALAEQHAVQELTKAAMSGV 591
Cdd:cd18274    91 EANVQALFTAASIFQIPSLQDQCAQFMISRLDPQNSIGV 129
Rit_Rin_Ric cd04141
Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related ...
16-205 2.78e-05

Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related protein which interacts with calmodulin (Ric); Rit (Ras-like protein in all tissues), Rin (Ras-like protein in neurons) and Ric (Ras-related protein which interacts with calmodulin) form a subfamily with several unique structural and functional characteristics. These proteins all lack a the C-terminal CaaX lipid-binding motif typical of Ras family proteins, and Rin and Ric contain calmodulin-binding domains. Rin, which is expressed only in neurons, induces neurite outgrowth in rat pheochromocytoma cells through its association with calmodulin and its activation of endogenous Rac/cdc42. Rit, which is ubiquitously expressed in mammals, inhibits growth-factor withdrawl-mediated apoptosis and induces neurite extension in pheochromocytoma cells. Rit and Rin are both able to form a ternary complex with PAR6, a cell polarity-regulating protein, and Rac/cdc42. This ternary complex is proposed to have physiological function in processes such as tumorigenesis. Activated Ric is likely to signal in parallel with the Ras pathway or stimulate the Ras pathway at some upstream point, and binding of calmodulin to Ric may negatively regulate Ric activity.


Pssm-ID: 206712 [Multi-domain]  Cd Length: 172  Bit Score: 45.23  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTrlicarACNTTLTQYQLLATHVPTVWaiDQYRVcqevlersRDVVDEVSVSLRLWDTFGD-HHKDRR 94
Cdd:cd04141     4 KIVMLGAGGVGKS------AVTMQFISHSFPDYHDPTIE--DAYKT--------QARIDNEPALLDILDTAGQaEFTAMR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FAYGRS-DVVVLCFSIANPNSLNHVKsmwypEIKHFCPR------TPVVLVGCQLDLRyadleavnRARRplarpikrgd 167
Cdd:cd04141    68 DQYMRCgEGFIICYSVTDRHSFQEAS-----EFKELITRvrltedIPLVLVGNKVDLE--------QQRQ---------- 124
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622963184 168 iLPPEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:cd04141   125 -VTTEEGRNLAREFNCPFFETSAALRFYIDDAFHGLVR 161
PTZ00369 PTZ00369
Ras-like protein; Provisional
16-205 2.86e-05

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 45.24  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICaracnttltqyQLLATHVptvwaIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFG-DHHKDRR 94
Cdd:PTZ00369    7 KLVVVGGGGVGKSALTI-----------QFIQNHF-----IDEYDPTIEDSYRKQCVIDEETCLLDILDTAGqEEYSAMR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FAYGRSDVVVLC-FSIANPNSLNHVKSMWYPEIK-HFCPRTPVVLVGCQLDLRYAdleavnrarrplaRPIKRGDilppe 172
Cdd:PTZ00369   71 DQYMRTGQGFLCvYSITSRSSFEEIASFREQILRvKDKDRVPMILVGNKCDLDSE-------------RQVSTGE----- 132
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622963184 173 kGREVAKELGIPYYETSVFDQFGIKDVFDNAIR 205
Cdd:PTZ00369  133 -GQELAKSFGIPFLETSAKQRVNVDEAFYELVR 164
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
64-209 4.07e-05

Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like families; RERG (Ras-related and Estrogen- Regulated Growth inhibitor) and Ras-like 11 are members of a novel subfamily of Ras that were identified based on their behavior in breast and prostate tumors, respectively. RERG expression was decreased or lost in a significant fraction of primary human breast tumors that lack estrogen receptor and are correlated with poor clinical prognosis. Elevated RERG expression correlated with favorable patient outcome in a breast tumor subtype that is positive for estrogen receptor expression. In contrast to most Ras proteins, RERG overexpression inhibited the growth of breast tumor cells in vitro and in vivo. RasL11 was found to be ubiquitously expressed in human tissue, but down-regulated in prostate tumors. Both RERG and RasL11 lack the C-terminal CaaX prenylation motif, where a = an aliphatic amino acid and X = any amino acid, and are localized primarily in the cytoplasm. Both are believed to have tumor suppressor activity.


Pssm-ID: 206713 [Multi-domain]  Cd Length: 166  Bit Score: 44.58  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  64 EVLERSRDVVDEVSVSLRLWDTFGDHHKDRRFAYGRS----DVVVLCFSIANPNSLNHVKSMWY--PEIKHFCPRTPVVL 137
Cdd:cd04146    33 ESLYSRQVTIDGEQVSLEIQDTPGQQQNEDPESLERSlrwaDGFVLVYSITDRSSFDVVSQLLQliREIKKRDGEIPVIL 112
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622963184 138 VGCQLDLryadleavNRARRplarpikrgdiLPPEKGREVAKELGIPYYETSVFDQF-GIKDVFDNAIRAALI 209
Cdd:cd04146   113 VGNKADL--------LHSRQ-----------VSTEEGQKLALELGCLFFEVSAAENYlEVQNVFHELCREVRR 166
BTB_POZ_KBTBD2_BKLHD1 cd18270
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
461-551 4.45e-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: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 461 QEITKAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVL 540
Cdd:cd18270     3 RQINTEYAVSLLEQLKFFYEQQLLTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAATLQIII 82
                          90
                  ....*....|.
gi 1622963184 541 DYLYTKQLSPN 551
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 ...
484-561 4.74e-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: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDGAISAHKPLLI-CSCeWMAAMFGgSFVESANSEVYLPNINKISMQAVLDYLYTKQLS-PNLDLDPLELIA 561
Cdd:cd18315     1 LVDVTLACEGGSLKAHKLVLAaASP-YFAALLK-ETPPDEHPVIILPDVPYSELKALLDFIYTGEVNvSQEQLESLLKLA 78
BTB_POZ_KLHL38 cd18268
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
484-554 7.75e-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: 7.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622963184 484 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDL 554
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 ...
484-584 8.22e-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: 8.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQlSPNLDLDPLELIALA 563
Cdd:cd18343    21 FTDCSLFVGGQEFKAHKSILAARSPVFNAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTGK-APNLDKMADNLLAAA 99
                          90       100
                  ....*....|....*....|.
gi 1622963184 564 NRFCLPHLVALAEQHAVQELT 584
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 ...
486-544 1.09e-04

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: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 486 DVTFKLDDGA-ISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 544
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 ...
474-585 1.78e-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: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 474 RIKECLSKGTFSDVTFKLDDGA----ISAHKPLLICSCEWMAAMFGGSFVeSANSEVYLPNINKISMQAVLDYLYTKQls 549
Cdd:cd18281    12 RFAFLFNNETLSDVHFIVGKGDneqrIPAHKFVLSIGSAVFDAMFNGGMA-TTSAEIELPDVEPAAFLALLRFLYSDE-- 88
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622963184 550 pnLDLDPLELIAL---ANRFCLPHLvalaEQHAVQELTK 585
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 ...
468-577 2.21e-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: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 468 HVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKq 547
Cdd:cd18353     4 FLTVAESLKKEFDSPETSDLKFRVDGKYIHVHKAVLKIRCEHFRTMFQSHWNEDMKEVIEIDQFSYPVYRAFLEYLYTD- 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622963184 548 lspNLDLDP---LELIALANRFCLPHLVALAEQ 577
Cdd:cd18353    83 ---SVDLPPedaIGLLDLATSYCENRLKKLCQH 112
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
15-144 2.48e-04

Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown to be a late embryogenesis-abundant (Lea) protein that is regulated by the plant hormone abcisic acid (ABA). In Arabidopsis, Rab28 is expressed during embryo development and is generally restricted to provascular tissues in mature embryos. Unlike maize Rab28, it is not ABA-inducible. Characterization of the human Rab28 homolog revealed two isoforms, which differ by a 95-base pair insertion, producing an alternative sequence for the 30 amino acids at the C-terminus. The two human isoforms are presumably the result of alternative splicing. Since they differ at the C-terminus but not in the GTP-binding region, they are predicted to be targeted to different cellular locations. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206694 [Multi-domain]  Cd Length: 213  Bit Score: 42.86  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLiCARACNTTLTQyqllathvptvwaidQYRVCQEVLERSRDVV--DEVSVSLRLWD----TFGD 88
Cdd:cd04109     1 IKIVVLGDGASGKTSL-IRRFAQEGFGK---------------SYKQTIGLDFFSRRITlpGSLNVTLQVWDiggqQIGG 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  89 HHKDrRFAYGrSDVVVLCFSIANPNSLNHVKSmWYPEIKHF---CPRTP-VVLVGCQLDL 144
Cdd:cd04109    65 KMLD-KYIYG-AQAVCLVYDITNSQSFENLED-WLSVVKKVneeSETKPkMVLVGNKTDL 121
BTB_POZ_KLHL40_KBTBD5 cd18340
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
475-569 2.53e-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: 41.74  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 475 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDL 554
Cdd:cd18340    18 LKDLLDHNKFVDCVLKIKEKEFPCHRLVLAACSPYFRAMFLSDLEESKKREIVLEDVDPDVMGKILHYIYTSEIEIT-EQ 96
                          90
                  ....*....|....*
gi 1622963184 555 DPLELIALANRFCLP 569
Cdd:cd18340    97 NVQDIFAAANMFQIP 111
BTB2_POZ_KLHL33 cd18263
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
475-549 2.55e-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: 2.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622963184 475 IKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLS 549
Cdd:cd18263     4 IEGLWEKGVGCDVQLEADGSIFRVHRVILAAGSDYFRAMFTSGMKESTQSVVQLPTIPAKDLRLLISFAYSGILH 78
BTB_POZ_KLHL10 cd18240
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
482-566 2.58e-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: 41.16  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 482 GTFSDVTFKLDDGAISAHKPLLiCSCE-WMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDlDPLELI 560
Cdd:cd18240    15 GKLCDVVIRVNGVEFPAHRNIL-CACSpYFRALFTNGWNETEKKVYKIPGVSPEMMELIIEYAYTRTVPITAE-NVEELL 92

                  ....*.
gi 1622963184 561 ALANRF 566
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 ...
482-548 2.66e-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: 2.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622963184 482 GTFSDVTFKLDDGAI-SAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQL 548
Cdd:cd18252    19 GLFTDITLQCASGQIfHCHKAALAACSSYFKVMFTADMKEKSNNVIKLSGIDHDILEALVNYVYTSQI 86
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
265-305 3.79e-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: 39.46  E-value: 3.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622963184 265 CADVLFILQDQEhIFAHRIYLATSSSKFYDLFLMECEESPN 305
Cdd:cd18186     1 LCDVTLVVGGRE-FPAHRAVLAARSPYFRAMFSSGMKESSS 40
BTB_POZ_KLHL20_KLEIP cd18249
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
486-549 3.90e-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: 3.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622963184 486 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLS 549
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 ...
470-584 4.11e-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: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 470 RKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQlS 549
Cdd:cd18279     4 RLAEDLGNLWENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVDPEVFKEMMRFIYTGK-A 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622963184 550 PNLDLDPLELIALANRFCLPHLVALAEQHAVQELT 584
Cdd:cd18279    83 PNLDKMADDLLAAADKYALERLKVMCEDALCSNLS 117
BTB_POZ_BTBD3_6 cd18282
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
485-572 5.15e-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: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 485 SDVTFKL--DDGA--ISAHKPLLICSCEWMAAMFGGSFVESANsEVYLPNINKISMQAVLDYLYTKQlspnLDLDP---L 557
Cdd:cd18282     8 ADVHFIVgpPGGTqrIPAHKYVLATGSSVFYAMFYGGLAENKN-EIEIPDVEPAAFLNLLRYLYCDE----IDLEPdtvL 82
                          90
                  ....*....|....*
gi 1622963184 558 ELIALANRFCLPHLV 572
Cdd:cd18282    83 ATLYAAKKYLVPHLA 97
Rab9 cd04116
Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate ...
15-205 5.22e-04

Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate receptors (MPRs) and the tail-interacting protein of 47 kD (TIP47). Rab9 is a key mediator of vesicular transport from late endosomes to the trans-Golgi network (TGN) by redirecting the MPRs. Rab9 has been identified as a key component for the replication of several viruses, including HIV1, Ebola, Marburg, and measles, making it a potential target for inhibiting a variety of viruses. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206697 [Multi-domain]  Cd Length: 170  Bit Score: 41.40  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLICARACNTTLTQyqllATHVPTVwaidqyrvcqEVLERSRdVVDEVSVSLRLWDTFG-DHHKDR 93
Cdd:cd04116     6 LKVILLGDGGVGKSSLMNRYVTNKFDTQ----LFHTIGV----------EFLNKDL-EVDGHFVTLQIWDTAGqERFRSL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  94 RFAYGR-SDVVVLCFSIANPNSLNHVKS-----MWYPEIKHfCPRTPVVLVGCQLDLryadleavnrARRPLARpikrgd 167
Cdd:cd04116    71 RTPFYRgSDCCLLTFSVDDSQSFQNLSNwkkefIYYADVKE-PESFPFVILGNKIDI----------PERQVST------ 133
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622963184 168 ilppEKGREVAKELGI-PYYETSVFDQFGIKDVFDNAIR 205
Cdd:cd04116   134 ----EEAQAWCRDNGDyPYFETSAKDATNVAAAFEEAVR 168
BTB_POZ_KLHL1-like cd18234
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
485-548 5.99e-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: 39.66  E-value: 5.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622963184 485 SDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQL 548
Cdd:cd18234     2 CDVILIAGDRRIPAHRLVLSAVSDYFAAMFTNDVREATEEEIKLKDVDPDALWTLVQYCYTGRL 65
Ras2 cd04144
Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, ...
16-211 1.04e-03

Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, found exclusively in fungi, was first identified in Ustilago maydis. In U. maydis, Ras2 is regulated by Sql2, a protein that is homologous to GEFs (guanine nucleotide exchange factors) of the CDC25 family. Ras2 has been shown to induce filamentous growth, but the signaling cascade through which Ras2 and Sql2 regulate cell morphology is not known. Most Ras 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 Ras proteins.


Pssm-ID: 133344 [Multi-domain]  Cd Length: 190  Bit Score: 40.60  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTrlicarACNTTLTQYQLLATHVPTVWaiDQYRvcqevlerSRDVVDEVSVSLRLWDTFGDHH----K 91
Cdd:cd04144     1 KLVVLGDGGVGKT------ALTIQLCLNHFVETYDPTIE--DSYR--------KQVVVDGQPCMLEVLDTAGQEEytalR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  92 DRRFAYGRSDVVVlcFSIANPNSLNHVKSMWYP--EIKHFCP-RTPVVLVGcqldlryadleavNRARRPLARPIKRgdi 168
Cdd:cd04144    65 DQWIREGEGFILV--YSITSRSTFERVERFREQiqRVKDESAaDVPIMIVG-------------NKCDKVYEREVST--- 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622963184 169 lppEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAALISR 211
Cdd:cd04144   127 ---EEGAALARRLGCEFIEASAKTNVNVERAFYTLVRALRQQR 166
BTB_POZ_KLHL25 cd18254
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
476-551 1.07e-03

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: 1.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622963184 476 KECLskgtFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEV-YLPNINKISMQAVLDYLYTKQLSPN 551
Cdd:cd18254    18 KQCM----FTDVTLWAGNRSFPCHRAVLAACSRYFEAMFSNGLRESLDSTVnFHDSLHPEVLELLLDFAYSSRIIIN 90
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
16-214 1.20e-03

Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with N|PM-ALK, it may provide a target for cancer treatments. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133310 [Multi-domain]  Cd Length: 199  Bit Score: 40.61  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICARACNTTLTQYqllathvPTVWAIDqYRVCQEVLERSRdvvdevsVSLRLWDTFGdhhkDRRF 95
Cdd:cd04110     8 KLLIIGDSGVGKSSLLLRFADNTFSGSY-------ITTIGVD-FKIRTVEINGER-------VKLQIWDTAG----QERF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  96 A------YGRSDVVVLCFSIANPNSLNHVKSmWYPEIKHFCPRTPVVLVGCQLDlryadleavNRARRplarpikrgdIL 169
Cdd:cd04110    69 RtitstyYRGTHGVIVVYDVTNGESFVNVKR-WLQEIEQNCDDVCKVLVGNKND---------DPERK----------VV 128
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622963184 170 PPEKGREVAKELGIPYYETSVFDQFGIKDVFDNAIRAALisRRHL 214
Cdd:cd04110   129 ETEDAYKFAGQMGISLFETSAKENINVEEMFNCITELVL--RAKK 171
BTB_POZ_KLHL24_KRIP6 cd18253
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
473-553 1.21e-03

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: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 473 NRIKEclsKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNL 552
Cdd:cd18253    10 NEFRD---SRLFTDVIICVEGREFPCHRAILSACSSYFRAMFCNDHRESREMLVEINGILAEAMDCFLQYVYTGKVKITT 86

                  .
gi 1622963184 553 D 553
Cdd:cd18253    87 E 87
BTB_POZ_KLHL19_KEAP1 cd18248
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
486-572 1.23e-03

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: 39.28  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 486 DVTFKLDDGA----ISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNlDLDPLELIA 561
Cdd:cd18248    23 DVTLKVKYQDpkeeFMAHKVVLASSSPYFKAMFTSGLRECGMEVVPIEGVHPCVMSRLIEFAYTASISVG-EKCVLHVLP 101
                          90
                  ....*....|.
gi 1622963184 562 LANRFCLPHLV 572
Cdd:cd18248   102 GAVMYQMDSVV 112
BTB_POZ_ETO1-like cd18190
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
486-566 1.52e-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: 37.88  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 486 DVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNiNKIS---MQAVLDYLYTKQLSPNLDLDPLELIAL 562
Cdd:cd18190     1 DLVFCVGGEKFCCVRKKIASLSRPFKAMLYGNFRESTSDCIDFEE-NGISieaMRAVIDFSVTGRLDLFSVENVHEVLEL 79

                  ....
gi 1622963184 563 ANRF 566
Cdd:cd18190    80 ASKF 83
BTB_POZ_BTBD14B_NAC1 cd18290
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
473-552 2.01e-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: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 473 NRIKECLS----KGTFSDVTFKLDDGAISAHKPLLICScewmAAMFGGSFVESANSEVYLP-NINKISMQAVLDYLYTKQ 547
Cdd:cd18290    12 NSILECLNeqrlQGLYCDVSVVVKGHAFKAHRAVLAAS----SSYFRDLFNSSRSAVVELPaAVQPQSFQQILSFCYTGR 87

                  ....*
gi 1622963184 548 LSPNL 552
Cdd:cd18290    88 LSMNV 92
BTB2_POZ_ABTB1_BPOZ1 cd18296
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
483-571 2.08e-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: 38.43  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 483 TFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVES-----ANSEVYLPNINKISMQAVLDYLYTKqlspNLDLDP- 556
Cdd:cd18296    16 SFPDVCFQVEGHRFPCHKAFFCGRSDYFKALLRDHFAESeenngSIPVVTLHDVSPEVFAIVLYYIYTD----DTDLPPe 91
                          90
                  ....*....|....*..
gi 1622963184 557 --LELIALANRFCLPHL 571
Cdd:cd18296    92 naYDVLYVADMYLLPGL 108
BTB_POZ_BTBD1 cd18346
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
484-585 2.45e-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: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDGA----------ISAHKPLLICSCEWMAAMFGGSFVeSANSEVYLPNINKISMQAVLDYLYTK--QLSPN 551
Cdd:cd18346    22 LSDVRFVVGKGRprgpgpgaqrIPAHRFVLAAGSAVFDAMFNGGMA-TTSAEIELPDVEPAAFLALLRFLYSDevQIGPE 100
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622963184 552 LDLDPLeliALANRFCLPHLvalaEQHAVQELTK 585
Cdd:cd18346   101 TVMTTL---YTAKKYAVPAL----EAHCVEFLTK 127
BTB_POZ_NPR_plant cd18310
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
484-578 2.51e-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: 38.83  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 484 FSDVTFKLDDGA-ISAHKPLLICSCEWMAAMFGGSFVESANSEVYLP--------NINKISMQAVLDYLYTKQLSPNLD- 553
Cdd:cd18310    18 YSDAEIIVEGGRpVPVHRCILAARSPFFRDIFASAKAEGANTKPKLElrelipggIVGYDAFMLVLSYLYSGRLRLVPKe 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622963184 554 ----LDP--------------LELIALANRFCLPHLVALAEQH 578
Cdd:cd18310    98 gsacVDSdcwhvacrpavdfaLEVLYAASVFQIPELVSLFQRR 140
BTB_POZ_BTBD3_6 cd18282
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
259-296 2.71e-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: 2.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622963184 259 LLDNPLCADVLFIL---QDQEHIFAHRIYLATSSSKFYDLF 296
Cdd:cd18282     1 MFNNELMADVHFIVgppGGTQRIPAHKYVLATGSSVFYAMF 41
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
16-206 2.77e-03

Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL4 lacks a prenylation site at the C-terminus. The specific function of RabL4 remains unknown.


Pssm-ID: 206688 [Multi-domain]  Cd Length: 167  Bit Score: 39.05  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLICARACNTTLTQYQLLAThvptvwaidqyrVCQEVLERSRDV-VDEVSVSLRLWDTFGDHHKDRR 94
Cdd:cd04101     2 QCAVVGDPAVGKSALVQMFHSDGATFQKNYTMT------------TGCDLVVKTVPVpDTSDSVELFIFDSAGQELFSDM 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  95 FA--YGRSDVVVLCFSIANPNSLNHVkSMWYPEIKHFCPR--TPVVLVGCQLDLryADLEAVNRArrplarpikrgdilp 170
Cdd:cd04101    70 VEnvWEQPAVVCVVYDVTNEVSFNNC-SRWINRVRTHSHGlhTPGVLVGNKCDL--TDRREVDAA--------------- 131
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622963184 171 peKGREVAKELGIPYYETSVFDQFGIKDVFDNAIRA 206
Cdd:cd04101   132 --QAQALAQANTLKFYETSAKEGVGYEAPFLSLARA 165
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
15-214 2.86e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.19  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  15 IKCVVVGDNAVGKTRLIcARACNTTLTQYQLLATHVPTVWaidqyrvcqevleRSRDVVDEVSVSLRLWDT-----FGDH 89
Cdd:COG1100     4 KKIVVVGTGGVGKTSLV-NRLVGDIFSLEKYLSTNGVTID-------------KKELKLDGLDVDLVIWDTpgqdeFRET 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  90 HKDRRFAYGRSDVVVLCFSIANPNSLNHVKsMWYPEIKHFCPRTPVVLVGCQLDLryadleavnrarrplarpIKRGDIL 169
Cdd:COG1100    70 RQFYARQLTGASLYLFVVDGTREETLQSLY-ELLESLRRLGKKSPIILVLNKIDL------------------YDEEEIE 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622963184 170 PPEKGREVAKELGI-PYYETSVFDQFGIKDVFdNAIRAALISRRHL 214
Cdd:COG1100   131 DEERLKEALSEDNIvEVVATSAKTGEGVEELF-AALAEILRGEGDS 175
Rab2 cd01866
Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi ...
16-206 2.96e-03

Rab GTPase family 2 (Rab2); Rab2 is localized on cis-Golgi membranes and interacts with Golgi matrix proteins. Rab2 is also implicated in the maturation of vesicular tubular clusters (VTCs), which are microtubule-associated intermediates in transport between the ER and Golgi apparatus. In plants, Rab2 regulates vesicle trafficking between the ER and the Golgi bodies and is important to pollen tube growth. 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. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206658 [Multi-domain]  Cd Length: 168  Bit Score: 38.94  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  16 KCVVVGDNAVGKTRLIcaracnTTLTQYQLLATHVPTVWAIDQYRVCQevlersrdvVDEVSVSLRLWDTFGDH--HKDR 93
Cdd:cd01866     6 KYIIIGDTGVGKSCLL------LQFTDKRFQPVHDLTIGVEFGARMIT---------IDGKQIKLQIWDTAGQEsfRSIT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184  94 RFAYGRSDVVVLCFSIANPNSLNHVKSmWYPEIK-HFCPRTPVVLVGCQLDLRyadleavnrARRPLARpikrgdilppE 172
Cdd:cd01866    71 RSYYRGAAGALLVYDITRRETFNHLTS-WLEDARqHSNSNMTIMLIGNKCDLE---------SRREVSY----------E 130
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622963184 173 KGREVAKELGIPYYETSVFDQFGIKDVFDNAIRA 206
Cdd:cd01866   131 EGEAFAREHGLIFMETSAKTASNVEEAFINTAKE 164
BTB_POZ_BTBD12_SLX4 cd18288
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
485-576 3.24e-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: 37.83  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 485 SDVTFKLDDG-AISAHKPLLICSCEWMAAMF--GGSFVESANS----EVYLPNINKISMQAVLDYLYTKQLSPNLDLDPl 557
Cdd:cd18288    19 SDVQFQTDSGeVLYAHSFVLYARCPLLIQMVhsEGFSVEEEGGvttrRVLLGDVSGEAARCFLQYLYTADTGLPPGLSP- 97
                          90
                  ....*....|....*....
gi 1622963184 558 ELIALANRFCLPHLVALAE 576
Cdd:cd18288    98 HVSELADRFGVSELVHLCE 116
BACK cd14733
BACK (BTB and C-terminal Kelch) domain; The BACK domain is found in architectures C-terminal ...
597-629 3.91e-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: 36.10  E-value: 3.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622963184 597 VLSYLELAQFHNAHQLAAWCLHHICTNYNSVCS 629
Cdd:cd14733     5 CLGILELADLYNLEELKEKALKFILENFEEVSK 37
BTB_POZ_KLHL2-like cd18235
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
465-548 4.64e-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: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 465 KAFHVRKANRIKECLSkgtfsDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLY 544
Cdd:cd18235     7 KAFDVMNELRKQNLLC-----DVILVADGVEIPAHRVVLASCSPYFHAMFTGDLSESRANRVTLQDVDGKALLLLIDYVY 81

                  ....
gi 1622963184 545 TKQL 548
Cdd:cd18235    82 TAEI 85
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
259-297 5.60e-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: 37.23  E-value: 5.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622963184 259 LLDNPLCADVLFIL-QDQEHIFAHRIYLATSSSKFYDLFL 297
Cdd:cd18294     8 LINNPEFSDVKFLVgPERQEIFAHKCILAARCEVFRAMFL 47
BTB2_POZ_LZTR1 cd18309
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
482-514 6.26e-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: 6.26e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622963184 482 GTFSDVTFKLDDGAISAHKPLLICSCEWMAAMF 514
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 ...
485-577 7.03e-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: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 485 SDVTFKLDDGAISAHKpLLICSCEWMAAMFGGSFVESANSEVYL----PNINKISMQAVLDYLYtkqlSPNLDLDPLELI 560
Cdd:cd18305    16 SDITICALGREWKLHK-IYLCQSGYFASMFSGSWKESKETVINLeipdDNITVEALNVVFGSLY----RDEIEIKPSRVV 90
                          90
                  ....*....|....*..
gi 1622963184 561 ALANRFCLPHLVALAEQ 577
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 ...
481-576 8.26e-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: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 481 KGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGsfVESANseVYLPNINKISMQAVLDYLYTKQL---SPNLDldpl 557
Cdd:cd18232    15 EGQYCDATLDVGGRVFKAHWSVLACCSHFFQSLYGD--GTSGS--VVLPESFAEVFGLLLDFFYTGELaltRENRD---- 86
                          90
                  ....*....|....*....
gi 1622963184 558 ELIALANRFCLPHLVALAE 576
Cdd:cd18232    87 RVLLAAKELRVPEAVELCQ 105
BTB_POZ_KLHL11 cd18241
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
472-571 9.18e-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: 37.14  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622963184 472 ANRIKECLSKGTFSDVTFKLDDGA---ISAHKPLLICSCEWMAAMFGGSFVESANSEVYL------PNINKISMQAVLDY 542
Cdd:cd18241    11 SWRQNEQRKQGLFCDITLAFGGAGgreFRAHRSVLAAATEYFTPLLSGQFSESRSGRVEMrkwssePGPDPDTVEAVIQY 90
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622963184 543 LYTKQL---SPNLDldplELIALANRFCLPHL 571
Cdd:cd18241    91 MYTGRIrvsTGNVH----EVLELADRFLLIRL 118
 
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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