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Conserved domains on  [gi|47087642|ref|NP_998173|]
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clusterin-associated protein 1 homolog [Danio rerio]

Protein Classification

clusterin-associated protein 1( domain architecture ID 12104052)

clusterin-associated protein 1 is required for cilia biogenesis, and appears to function within the multiple intraflagellar transport complex B (IFT-B)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cluap1 pfam10234
Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of ...
 14-283 7.17e-160

Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of 413 amino acids contains a central coiled-coil domain, possibly the region that binds to clusterin. Cluap1 expression is highest in the nucleus and gradually increases during late S to G2/M phases of the cell cycle and returns to the basal level in the G0/G1 phases. In addition, it is upregulated in colon cancer tissues compared to corresponding non-cancerous mucosa. It thus plays a crucial role in the life of the cell.


:

Pssm-ID: 463013 [Multi-domain]  Cd Length: 268  Bit Score: 451.26  E-value: 7.17e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642    14 RALGYPRLISMENFRSPNFPLVAEILIWLVKRYEPQMEIPSDVDTESDRVFFIKAVAQFMATKAHVKLNLKRLYQADGYA 93
Cdd:pfam10234   1 RALGYPRLISMENFRTPNFPLVAEILRWLAKRYDPNADIPGDIDTEQDRVIFIKSVAEFMATKAHIKLNTKKLYQADGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642    94 VKEMLKITSILYNAMKTkeNAGGDQNNDENSKFKFDLGSKIADLKLARQLGSEITAKGAALFDLLGQEEDLRESRTAAIA 173
Cdd:pfam10234  81 VKELLKITSLLYNAMKS--ADKEAEEEEDSTSSQFDLSSKLSDLKAARQLASEITTKGASLYDLLGKEVDLREIRQQALS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642   174 RPLEITETERAMRVAVKDVTESIQMTKDLLNNVSSDEASLEAKIEKKKQDLERNQKRLQTLQSVRPAFMDEYEKIEEDLE 253
Cdd:pfam10234 159 RPLEIAEIEKALKEAIKNVAAEIEQTQKQLENLASDEANLEAKIEKKKQELERNQKRLQTLQSVRPAFMDEYEKLEEELQ 238

                         250       260       270
                  ....*....|....*....|....*....|
gi 47087642   254 KQYQTYVEKYRNLSFLEQQLDDYHRVEQER 283
Cdd:pfam10234 239 KLYEEYVEKFRNLSYLEHQLEKYNKAEQER 268
 
Name Accession Description Interval E-value
Cluap1 pfam10234
Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of ...
 14-283 7.17e-160

Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of 413 amino acids contains a central coiled-coil domain, possibly the region that binds to clusterin. Cluap1 expression is highest in the nucleus and gradually increases during late S to G2/M phases of the cell cycle and returns to the basal level in the G0/G1 phases. In addition, it is upregulated in colon cancer tissues compared to corresponding non-cancerous mucosa. It thus plays a crucial role in the life of the cell.


Pssm-ID: 463013 [Multi-domain]  Cd Length: 268  Bit Score: 451.26  E-value: 7.17e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642    14 RALGYPRLISMENFRSPNFPLVAEILIWLVKRYEPQMEIPSDVDTESDRVFFIKAVAQFMATKAHVKLNLKRLYQADGYA 93
Cdd:pfam10234   1 RALGYPRLISMENFRTPNFPLVAEILRWLAKRYDPNADIPGDIDTEQDRVIFIKSVAEFMATKAHIKLNTKKLYQADGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642    94 VKEMLKITSILYNAMKTkeNAGGDQNNDENSKFKFDLGSKIADLKLARQLGSEITAKGAALFDLLGQEEDLRESRTAAIA 173
Cdd:pfam10234  81 VKELLKITSLLYNAMKS--ADKEAEEEEDSTSSQFDLSSKLSDLKAARQLASEITTKGASLYDLLGKEVDLREIRQQALS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642   174 RPLEITETERAMRVAVKDVTESIQMTKDLLNNVSSDEASLEAKIEKKKQDLERNQKRLQTLQSVRPAFMDEYEKIEEDLE 253
Cdd:pfam10234 159 RPLEIAEIEKALKEAIKNVAAEIEQTQKQLENLASDEANLEAKIEKKKQELERNQKRLQTLQSVRPAFMDEYEKLEEELQ 238

                         250       260       270
                  ....*....|....*....|....*....|
gi 47087642   254 KQYQTYVEKYRNLSFLEQQLDDYHRVEQER 283
Cdd:pfam10234 239 KLYEEYVEKFRNLSYLEHQLEKYNKAEQER 268
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 161-278 4.02e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 38.87  E-value: 4.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642 161 EEDLRESRTAAIARPLEITETERAMRVAVKDvtESIQMTKDL-----LNNVSSDEASLEAKIEKKKQDLERNQKR----L 231
Cdd:cd07680 118 EDGFRKAQKPWAKKMKELEAAKKAYHLACKE--EKLAMTREAnskaeQSVTPEQQKKLQDKVDKCKQDVQKTQEKyekvL 195

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 47087642 232 QTLQSVRPAFMDEYEKIEEdlekQYQTYVEKyrNLSFLEQQLDDYHR 278
Cdd:cd07680 196 DDVGKTTPQYMENMEQVFE----QCQQFEEK--RLVFLKEVLLDIKR 236
PRK11637 PRK11637
AmiB activator; Provisional
 194-309 8.20e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 38.14  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642  194 ESIQMTKDLLNNVSSDEASLEAKIEKKKQDLERNQKRLQTLQSVRPAFMDEYEKIEEDLEKQYQTYVEKYRNLSFLEQQL 273
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSI 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 47087642  274 DDYHRVEQERFE-EAEMAMKMRQN-----------KLKEEEKRLM-RSG 309
Cdd:PRK11637 250 ARAEREAKARAErEAREAARVRDKqkqakrkgstyKPTESERSLMsRTG 298
 
Name Accession Description Interval E-value
Cluap1 pfam10234
Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of ...
 14-283 7.17e-160

Clusterin-associated protein-1; This protein is conserved from worms to humans. The protein of 413 amino acids contains a central coiled-coil domain, possibly the region that binds to clusterin. Cluap1 expression is highest in the nucleus and gradually increases during late S to G2/M phases of the cell cycle and returns to the basal level in the G0/G1 phases. In addition, it is upregulated in colon cancer tissues compared to corresponding non-cancerous mucosa. It thus plays a crucial role in the life of the cell.


Pssm-ID: 463013 [Multi-domain]  Cd Length: 268  Bit Score: 451.26  E-value: 7.17e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642    14 RALGYPRLISMENFRSPNFPLVAEILIWLVKRYEPQMEIPSDVDTESDRVFFIKAVAQFMATKAHVKLNLKRLYQADGYA 93
Cdd:pfam10234   1 RALGYPRLISMENFRTPNFPLVAEILRWLAKRYDPNADIPGDIDTEQDRVIFIKSVAEFMATKAHIKLNTKKLYQADGYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642    94 VKEMLKITSILYNAMKTkeNAGGDQNNDENSKFKFDLGSKIADLKLARQLGSEITAKGAALFDLLGQEEDLRESRTAAIA 173
Cdd:pfam10234  81 VKELLKITSLLYNAMKS--ADKEAEEEEDSTSSQFDLSSKLSDLKAARQLASEITTKGASLYDLLGKEVDLREIRQQALS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642   174 RPLEITETERAMRVAVKDVTESIQMTKDLLNNVSSDEASLEAKIEKKKQDLERNQKRLQTLQSVRPAFMDEYEKIEEDLE 253
Cdd:pfam10234 159 RPLEIAEIEKALKEAIKNVAAEIEQTQKQLENLASDEANLEAKIEKKKQELERNQKRLQTLQSVRPAFMDEYEKLEEELQ 238

                         250       260       270
                  ....*....|....*....|....*....|
gi 47087642   254 KQYQTYVEKYRNLSFLEQQLDDYHRVEQER 283
Cdd:pfam10234 239 KLYEEYVEKFRNLSYLEHQLEKYNKAEQER 268
MRP-S27 pfam10037
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins ...
 143-306 3.74e-03

Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins possess one of three conserved blocks of sequence found in proteins that stimulate the dissociation of guanine nucleotides from G-proteins, leaving open the possibility that MRP-S27 might be a functional partner of GTP-binding ribosomal proteins.


Pssm-ID: 462947 [Multi-domain]  Cd Length: 395  Bit Score: 39.35  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642   143 LGSEITAKGAALFdllGQEEDLresrtaaiARPLEITETERAMRVAVKDVTESIQMTKDLLNNVSSDEaslEAKIEKKKQ 222
Cdd:pfam10037 247 LGLSSQLLGYALL---GKVGYL--------DRALSVMEKVASSPGDLKLHKEVLDVLQDILETLDELE---ESEQSKLPE 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642   223 DLERNQKRLQTLQSVRPAfmdEYEKIEEDLEKQYQTYVEKY-RNLsfLEQQLDDYHRVEQERFEEAEMAMKMRQNKLKEE 301
Cdd:pfam10037 313 YVKSFQELLSKLQSLGKV---ESESLLTLLENLVKESLPACeEKD--LANYEQLYQEWEEERRQLIQREKEMREKAERED 387


                  ....*
gi 47087642   302 EKRLM 306
Cdd:pfam10037 388 EARKA 392
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 161-278 4.02e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 38.87  E-value: 4.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642 161 EEDLRESRTAAIARPLEITETERAMRVAVKDvtESIQMTKDL-----LNNVSSDEASLEAKIEKKKQDLERNQKR----L 231
Cdd:cd07680 118 EDGFRKAQKPWAKKMKELEAAKKAYHLACKE--EKLAMTREAnskaeQSVTPEQQKKLQDKVDKCKQDVQKTQEKyekvL 195

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 47087642 232 QTLQSVRPAFMDEYEKIEEdlekQYQTYVEKyrNLSFLEQQLDDYHR 278
Cdd:cd07680 196 DDVGKTTPQYMENMEQVFE----QCQQFEEK--RLVFLKEVLLDIKR 236
PRK11637 PRK11637
AmiB activator; Provisional
 194-309 8.20e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 38.14  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087642  194 ESIQMTKDLLNNVSSDEASLEAKIEKKKQDLERNQKRLQTLQSVRPAFMDEYEKIEEDLEKQYQTYVEKYRNLSFLEQQL 273
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSI 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 47087642  274 DDYHRVEQERFE-EAEMAMKMRQN-----------KLKEEEKRLM-RSG 309
Cdd:PRK11637 250 ARAEREAKARAErEAREAARVRDKqkqakrkgstyKPTESERSLMsRTG 298
 
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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