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Conserved domains on  [gi|71992990|ref|NP_001021702|]
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Exocyst component Exo84 C-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

Vps51 and PH-like domain-containing protein( domain architecture ID 11179653)

protein containing domains Vps51, PH-like, and Exo84_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
140-252 6.35e-19

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01226:

Pssm-ID: 473070  Cd Length: 115  Bit Score: 82.70  E-value: 6.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990 140 MSTSEKVILY-GEMEQFDVETKKPVQKCMLILLSHRLIIGNINA----AGKYVMESTLSLNSVAPVNVKDREsgaaNAGK 214
Cdd:cd01226   1 VEVPGRYLLHeGDLLELDPDDYKPIQKVHLFLLNDVLLIASWLPnrrgPVRYKFQALYPLEDLAVVNVKDLG----PVKN 76
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 71992990 215 VLKLLIFPESRCYLCESARIRTLWFDELEQAKREILHK 252
Cdd:cd01226  77 AFKLLTFPETRVFQCENAKIKKEWLEKFEQAKRAKLAK 114
Vps51 pfam08700
Vps51/Vps67; This family includes a presumed domain found in a number of components of ...
9-98 2.28e-15

Vps51/Vps67; This family includes a presumed domain found in a number of components of vesicular transport. The VFT tethering complex (also known as GARP complex, Golgi associated retrograde protein complex, Vps53 tethering complex) is a conserved eukaryotic docking complex which is involved recycling of proteins from endosomes to the late Golgi. Vps51 (also known as Vps67) is a subunit of VFT and interacts with the SNARE Tlg1. Cog1_N is the N-terminus of the Cog1 subunit of the eight-unit Conserved Oligomeric Golgi (COG) complex that participates in retrograde vesicular transport and is required to maintain normal Golgi structure and function. The subunits are located in two lobes and Cog1 serves to bind the two lobes together probably via the highly conserved N-terminal domain of approximately 85 residues.


:

Pssm-ID: 462568  Cd Length: 86  Bit Score: 71.54  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990     9 FQTDAFSPSDYIRDRLKGVKIGDetrkLRHLRSEMGALNHASQETLKNNVFRNYQQFIDASKEISHLEREIYQLTHSLIE 88
Cdd:pfam08700   1 LDSPSFDADRYVSELLSKATLEE----LLQFESSLRSEIERLDSELKQLVYDNYRDLIKAADTISKMKSEMEQLSQKLSE 76
                          90
                  ....*....|
gi 71992990    89 QKQVIENLIM 98
Cdd:pfam08700  77 LKQALSKIAS 86
Exo84_C super family cl24934
Exocyst component 84 C-terminal; Exo84_C is the C-terminal helical region of the exocyst ...
306-467 2.09e-14

Exocyst component 84 C-terminal; Exo84_C is the C-terminal helical region of the exocyst component Exo84. This region resembles a cullin-repeat, a multi-helical bundle. The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Exocyst subunits are composed of mostly helical modules strung together into long rods.


The actual alignment was detected with superfamily member pfam16528:

Pssm-ID: 465161  Cd Length: 203  Bit Score: 72.25  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990   306 WLSELPAELDDCIAHRDLDQAVELIHEWK-------QCPTKD-----AVIDIQLQMRENTIVQLLSDDVSRpgavHGGPR 373
Cdd:pfam16528   2 WVDDLPEELDIDIARRNFEEAVDLLEKLEsklkdlaDGLKDNeailhDLINLKVDQRREKLASKLSRSLLS----TNEVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990   374 AMKKARTLLTQLGRGTYATDVYLRRRSAMQRSAMRDVTVSEEPISYVKQLCTLYGNAVSDIANEFRSM---PQYYCQVLQ 450
Cdd:pfam16528  78 KLKRNVSWLIRLGLEDRARELFLENRSNLIQKRIRQIGFEGDLTLYITQLAVVRFTLIKNTVQEFQECfpdNKMSSALVK 157
                         170
                  ....*....|....*..
gi 71992990   451 WCSYELSTLLNLIRRHV 467
Cdd:pfam16528 158 WAKEEVDKFFDLLSRQL 174
 
Name Accession Description Interval E-value
PH_RalBD_exo84 cd01226
Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 ...
140-252 6.35e-19

Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 complex, also called the exocyst complex, forms an octameric protein (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84) involved in the tethering of secretory vesicles to specific regions on the plasma membrane. The regulation of Sec6/8 complex differs between mammals and yeast. Mamalian Exo84 and Sec5 are effector targets for active Ral GTPases which are not present in yeast. Ral GTPases are members of the Ras superfamily, and as such cycle between an active GTP-bound state and an inactive GDP-bound state. The Exo84 Ral-binding domain adopts a PH domain fold. Mammalian Exo84 and Sec5 competitively bind to active RalA. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269933  Cd Length: 115  Bit Score: 82.70  E-value: 6.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990 140 MSTSEKVILY-GEMEQFDVETKKPVQKCMLILLSHRLIIGNINA----AGKYVMESTLSLNSVAPVNVKDREsgaaNAGK 214
Cdd:cd01226   1 VEVPGRYLLHeGDLLELDPDDYKPIQKVHLFLLNDVLLIASWLPnrrgPVRYKFQALYPLEDLAVVNVKDLG----PVKN 76
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 71992990 215 VLKLLIFPESRCYLCESARIRTLWFDELEQAKREILHK 252
Cdd:cd01226  77 AFKLLTFPETRVFQCENAKIKKEWLEKFEQAKRAKLAK 114
Vps51 pfam08700
Vps51/Vps67; This family includes a presumed domain found in a number of components of ...
9-98 2.28e-15

Vps51/Vps67; This family includes a presumed domain found in a number of components of vesicular transport. The VFT tethering complex (also known as GARP complex, Golgi associated retrograde protein complex, Vps53 tethering complex) is a conserved eukaryotic docking complex which is involved recycling of proteins from endosomes to the late Golgi. Vps51 (also known as Vps67) is a subunit of VFT and interacts with the SNARE Tlg1. Cog1_N is the N-terminus of the Cog1 subunit of the eight-unit Conserved Oligomeric Golgi (COG) complex that participates in retrograde vesicular transport and is required to maintain normal Golgi structure and function. The subunits are located in two lobes and Cog1 serves to bind the two lobes together probably via the highly conserved N-terminal domain of approximately 85 residues.


Pssm-ID: 462568  Cd Length: 86  Bit Score: 71.54  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990     9 FQTDAFSPSDYIRDRLKGVKIGDetrkLRHLRSEMGALNHASQETLKNNVFRNYQQFIDASKEISHLEREIYQLTHSLIE 88
Cdd:pfam08700   1 LDSPSFDADRYVSELLSKATLEE----LLQFESSLRSEIERLDSELKQLVYDNYRDLIKAADTISKMKSEMEQLSQKLSE 76
                          90
                  ....*....|
gi 71992990    89 QKQVIENLIM 98
Cdd:pfam08700  77 LKQALSKIAS 86
Exo84_C pfam16528
Exocyst component 84 C-terminal; Exo84_C is the C-terminal helical region of the exocyst ...
306-467 2.09e-14

Exocyst component 84 C-terminal; Exo84_C is the C-terminal helical region of the exocyst component Exo84. This region resembles a cullin-repeat, a multi-helical bundle. The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Exocyst subunits are composed of mostly helical modules strung together into long rods.


Pssm-ID: 465161  Cd Length: 203  Bit Score: 72.25  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990   306 WLSELPAELDDCIAHRDLDQAVELIHEWK-------QCPTKD-----AVIDIQLQMRENTIVQLLSDDVSRpgavHGGPR 373
Cdd:pfam16528   2 WVDDLPEELDIDIARRNFEEAVDLLEKLEsklkdlaDGLKDNeailhDLINLKVDQRREKLASKLSRSLLS----TNEVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990   374 AMKKARTLLTQLGRGTYATDVYLRRRSAMQRSAMRDVTVSEEPISYVKQLCTLYGNAVSDIANEFRSM---PQYYCQVLQ 450
Cdd:pfam16528  78 KLKRNVSWLIRLGLEDRARELFLENRSNLIQKRIRQIGFEGDLTLYITQLAVVRFTLIKNTVQEFQECfpdNKMSSALVK 157
                         170
                  ....*....|....*..
gi 71992990   451 WCSYELSTLLNLIRRHV 467
Cdd:pfam16528 158 WAKEEVDKFFDLLSRQL 174
 
Name Accession Description Interval E-value
PH_RalBD_exo84 cd01226
Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 ...
140-252 6.35e-19

Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 complex, also called the exocyst complex, forms an octameric protein (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84) involved in the tethering of secretory vesicles to specific regions on the plasma membrane. The regulation of Sec6/8 complex differs between mammals and yeast. Mamalian Exo84 and Sec5 are effector targets for active Ral GTPases which are not present in yeast. Ral GTPases are members of the Ras superfamily, and as such cycle between an active GTP-bound state and an inactive GDP-bound state. The Exo84 Ral-binding domain adopts a PH domain fold. Mammalian Exo84 and Sec5 competitively bind to active RalA. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269933  Cd Length: 115  Bit Score: 82.70  E-value: 6.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990 140 MSTSEKVILY-GEMEQFDVETKKPVQKCMLILLSHRLIIGNINA----AGKYVMESTLSLNSVAPVNVKDREsgaaNAGK 214
Cdd:cd01226   1 VEVPGRYLLHeGDLLELDPDDYKPIQKVHLFLLNDVLLIASWLPnrrgPVRYKFQALYPLEDLAVVNVKDLG----PVKN 76
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 71992990 215 VLKLLIFPESRCYLCESARIRTLWFDELEQAKREILHK 252
Cdd:cd01226  77 AFKLLTFPETRVFQCENAKIKKEWLEKFEQAKRAKLAK 114
Vps51 pfam08700
Vps51/Vps67; This family includes a presumed domain found in a number of components of ...
9-98 2.28e-15

Vps51/Vps67; This family includes a presumed domain found in a number of components of vesicular transport. The VFT tethering complex (also known as GARP complex, Golgi associated retrograde protein complex, Vps53 tethering complex) is a conserved eukaryotic docking complex which is involved recycling of proteins from endosomes to the late Golgi. Vps51 (also known as Vps67) is a subunit of VFT and interacts with the SNARE Tlg1. Cog1_N is the N-terminus of the Cog1 subunit of the eight-unit Conserved Oligomeric Golgi (COG) complex that participates in retrograde vesicular transport and is required to maintain normal Golgi structure and function. The subunits are located in two lobes and Cog1 serves to bind the two lobes together probably via the highly conserved N-terminal domain of approximately 85 residues.


Pssm-ID: 462568  Cd Length: 86  Bit Score: 71.54  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990     9 FQTDAFSPSDYIRDRLKGVKIGDetrkLRHLRSEMGALNHASQETLKNNVFRNYQQFIDASKEISHLEREIYQLTHSLIE 88
Cdd:pfam08700   1 LDSPSFDADRYVSELLSKATLEE----LLQFESSLRSEIERLDSELKQLVYDNYRDLIKAADTISKMKSEMEQLSQKLSE 76
                          90
                  ....*....|
gi 71992990    89 QKQVIENLIM 98
Cdd:pfam08700  77 LKQALSKIAS 86
Exo84_C pfam16528
Exocyst component 84 C-terminal; Exo84_C is the C-terminal helical region of the exocyst ...
306-467 2.09e-14

Exocyst component 84 C-terminal; Exo84_C is the C-terminal helical region of the exocyst component Exo84. This region resembles a cullin-repeat, a multi-helical bundle. The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Exocyst subunits are composed of mostly helical modules strung together into long rods.


Pssm-ID: 465161  Cd Length: 203  Bit Score: 72.25  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990   306 WLSELPAELDDCIAHRDLDQAVELIHEWK-------QCPTKD-----AVIDIQLQMRENTIVQLLSDDVSRpgavHGGPR 373
Cdd:pfam16528   2 WVDDLPEELDIDIARRNFEEAVDLLEKLEsklkdlaDGLKDNeailhDLINLKVDQRREKLASKLSRSLLS----TNEVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992990   374 AMKKARTLLTQLGRGTYATDVYLRRRSAMQRSAMRDVTVSEEPISYVKQLCTLYGNAVSDIANEFRSM---PQYYCQVLQ 450
Cdd:pfam16528  78 KLKRNVSWLIRLGLEDRARELFLENRSNLIQKRIRQIGFEGDLTLYITQLAVVRFTLIKNTVQEFQECfpdNKMSSALVK 157
                         170
                  ....*....|....*..
gi 71992990   451 WCSYELSTLLNLIRRHV 467
Cdd:pfam16528 158 WAKEEVDKFFDLLSRQL 174
 
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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