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Conserved domains on  [gi|2462580496|ref|XP_054179482|]
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prefoldin subunit 4 isoform X1 [Homo sapiens]

Protein Classification

prefoldin subunit( domain architecture ID 10487305)

prefoldin subunit works as a transfer protein in conjunction with a chaperonin molecule to form a chaperone complex and correctly fold other nascent proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
 101-204 1.30e-50

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


:

Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 159.63  E-value: 1.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 101 DQQKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDcLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEI 180
Cdd:cd23165     1 DQQKINKFSRLNARLHELKEELKAKKKELENLEDASDELELADDD-EPVPYKIGEVFVHLSLEEAQERLEKAKEELEEEI 79

                          90       100
                  ....*....|....*....|....
gi 2462580496 181 DALESRVESIQRVLADLKVQLYAK 204
Cdd:cd23165    80 EKLEEEIDEIEEEMKELKVQLYAK 103
 
Name Accession Description Interval E-value
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
 101-204 1.30e-50

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 159.63  E-value: 1.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 101 DQQKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDcLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEI 180
Cdd:cd23165     1 DQQKINKFSRLNARLHELKEELKAKKKELENLEDASDELELADDD-EPVPYKIGEVFVHLSLEEAQERLEKAKEELEEEI 79

                          90       100
                  ....*....|....*....|....
gi 2462580496 181 DALESRVESIQRVLADLKVQLYAK 204
Cdd:cd23165    80 EKLEEEIDEIEEEMKELKVQLYAK 103
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 105-207 9.64e-27

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 98.45  E-value: 9.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 105 INKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDcLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEIDALE 184
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDED-TKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLE 79

                          90       100
                  ....*....|....*....|...
gi 2462580496 185 SRVESIQRVLADLKVQLYAKFGS 207
Cdd:pfam01920  80 KQLEKLEKELEELKEELYKKFGQ 102
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
84-201 1.88e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496  84 REPRRTQAAEDVNVTFEDQ---QKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDImladddclmipyqigdvfish 160
Cdd:COG2433   395 PEAEREKEHEERELTEEEEeirRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA--------------------- 453

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462580496 161 SQEETQEMLEEAK-KNLQEEIDALESRVESIQRVLADLKVQL 201
Cdd:COG2433   454 RSEERREIRKDREiSRLDREIERLERELEEERERIEELKRKL 495
46 PHA02562
endonuclease subunit; Provisional
 100-202 3.96e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 37.69  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 100 EDQQKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDImladddclmipyqigdvfishsQEETQEmLEEAKKNLQEE 179
Cdd:PHA02562  324 ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV----------------------KAAIEE-LQAEFVDNAEE 380

                          90       100
                  ....*....|....*....|...
gi 2462580496 180 IDALESRVESIQRVLADLKVQLY 202
Cdd:PHA02562  381 LAKLQDELDKIVKTKSELVKEKY 403
 
Name Accession Description Interval E-value
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
 101-204 1.30e-50

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 159.63  E-value: 1.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 101 DQQKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDcLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEI 180
Cdd:cd23165     1 DQQKINKFSRLNARLHELKEELKAKKKELENLEDASDELELADDD-EPVPYKIGEVFVHLSLEEAQERLEKAKEELEEEI 79

                          90       100
                  ....*....|....*....|....
gi 2462580496 181 DALESRVESIQRVLADLKVQLYAK 204
Cdd:cd23165    80 EKLEEEIDEIEEEMKELKVQLYAK 103
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 105-207 9.64e-27

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 98.45  E-value: 9.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 105 INKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDcLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEIDALE 184
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDED-TKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLE 79

                          90       100
                  ....*....|....*....|...
gi 2462580496 185 SRVESIQRVLADLKVQLYAKFGS 207
Cdd:pfam01920  80 KQLEKLEKELEELKEELYKKFGQ 102
Prefoldin cd00890
prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and ...
 114-192 4.11e-23

prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits; the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes, there are two or more paralogous genes encoding each subunit, adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467470  Cd Length: 79  Bit Score: 88.55  E-value: 4.11e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580496 114 RITELKEEIEVKKKQLQNLEDACDDIMLADDDCLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEIDALESRVESIQR 192
Cdd:cd00890     1 QVQALSQQIEQLNRQINELEEALDELSNLDKDTEEVYRSVGGVFIEKSKEETKEELEEKLDELQKEIKKLEQQLEAKTK 79
Prefoldin_beta cd00632
Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, ...
 114-192 5.74e-22

Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467469  Cd Length: 78  Bit Score: 85.47  E-value: 5.74e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462580496 114 RITELKEEIEVKKKQLQNLEDACDDIMLADDdCLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEIDALESRVESIQR 192
Cdd:cd00632     1 EVLALKSQKEELERKINEQKVVLDELSNLKK-NRKVYRQQGNIFILASKEETLSELKKTLDHLQKEIKELEQQLKAKEK 78
FAM76 pfam16046
FAM76 protein; This family of proteins is functionally uncharacterized. This family of ...
 115-198 1.02e-03

FAM76 protein; This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 233 and 341 amino acids in length.


Pssm-ID: 464993 [Multi-domain]  Cd Length: 303  Bit Score: 39.39  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 115 ITELKEEIEVKKKQLQnledACDDIMLADDDclmipyQIGDVFISHSQEET--QEMLEEAKKNLQEEIDALESRVESIQR 192
Cdd:pfam16046 224 ITQLKEQIASLQKQLA----QKDQQLLEKDK------QITELKAKHFTKERelRNKMKTMEKEHEDKVEQLQIKIRSLLK 293


                  ....*.
gi 2462580496 193 VLADLK 198
Cdd:pfam16046 294 EVATLS 299
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
84-201 1.88e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496  84 REPRRTQAAEDVNVTFEDQ---QKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDImladddclmipyqigdvfish 160
Cdd:COG2433   395 PEAEREKEHEERELTEEEEeirRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA--------------------- 453

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462580496 161 SQEETQEMLEEAK-KNLQEEIDALESRVESIQRVLADLKVQL 201
Cdd:COG2433   454 RSEERREIRKDREiSRLDREIERLERELEEERERIEELKRKL 495
PDRG1 cd22860
p53 and DNA damage-regulated protein 1; p53 and DNA damage-regulated protein 1 (PDRG1) is a ...
 153-197 2.62e-03

p53 and DNA damage-regulated protein 1; p53 and DNA damage-regulated protein 1 (PDRG1) is a beta-type subunit of the prefoldin-like complex that is part of the PAQosome (Particle for Arrangement of Quaternary structure) complex. The PAQosome is a cochaperone that assists the chaperone HSP90 in assembly of large protein complexes. PDRG1 acts as a tumor marker in multiple cancer types, including testicular cancer, lung cancer, colorectal cancer, liver cancer, etc. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related.


Pssm-ID: 467471  Cd Length: 103  Bit Score: 36.34  E-value: 2.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462580496 153 IGDVFISHSQEETQEMLEEAKKNLQEEIDALESRVESIQRVLADL 197
Cdd:cd22860    53 LGDMFIKLPKEKAKKMLEKDQKELDKEINKLRSELKEKVNKLRDL 97
Prefoldin_1 cd23164
prefoldin subunit 1; Prefoldin subunit 1 is one of the beta subunits of the eukaryotic ...
 107-201 3.74e-03

prefoldin subunit 1; Prefoldin subunit 1 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467480  Cd Length: 99  Bit Score: 35.64  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 107 KFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDCLMipYQ-IGDVFISHSQEETQEMLEEAKKNLQEEIDALES 185
Cdd:cd23164     5 KMIETQQQLKLADAQIEQLEREKRRAQLTAKELSSLPEDTRT--YEgVGRMFVLQPKATVKKELEEKQKEADEKIKKLEK 82

                          90
                  ....*....|....*.
gi 2462580496 186 RVESIQRVLADLKVQL 201
Cdd:cd23164    83 KKEYLERSLKESEDNL 98
46 PHA02562
endonuclease subunit; Provisional
 100-202 3.96e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 37.69  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 100 EDQQKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDImladddclmipyqigdvfishsQEETQEmLEEAKKNLQEE 179
Cdd:PHA02562  324 ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV----------------------KAAIEE-LQAEFVDNAEE 380

                          90       100
                  ....*....|....*....|...
gi 2462580496 180 IDALESRVESIQRVLADLKVQLY 202
Cdd:PHA02562  381 LAKLQDELDKIVKTKSELVKEKY 403
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
93-201 4.54e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496  93 EDVNVTFEDQQKI-NKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDCLMIPYQIGDVFISHSQEETQEM--- 168
Cdd:PRK03918  588 EELEERLKELEPFyNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELree 667

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462580496 169 ---LEEAKKNLQEEIDALESRVESIQRVLADLKVQL 201
Cdd:PRK03918  668 yleLSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 117-198 6.98e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 36.51  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 117 ELKEEIEVKKKQLQNLEDACDDImladDDCLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEIDALESRVESIQRVLAD 196
Cdd:pfam03961 153 ELKEKLEELEKELEELEEELEKL----KKRLKKLPKKARGQLPPEKREQLEKLLETKNKLSEELEELEEELKELKEELES 228


                  ..
gi 2462580496 197 LK 198
Cdd:pfam03961 229 LL 230
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 102-201 7.30e-03

Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent transfer to the cytosolic chaperonin CCT (chaperonin containing TCP-1). Electron microscopy shows that eukaryotic PFD, which has a similar structure to its archaeal counterpart, interacts with unfolded actin along the tips of its projecting arms. In its PFD-bound state, actin seems to acquire a conformation similar to that adopted when it is bound to CCT.


Pssm-ID: 427096 [Multi-domain]  Cd Length: 120  Bit Score: 35.31  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 102 QQKINKFARNTSRITELKEEIEvkkkqlqNLEDACDDIMLADDDCLMiPYQIGD-VFISHSQEETQEML----------- 169
Cdd:pfam02996   2 KQEIESLQAELARLREAIEELE-------KSLETLKTLKKEDEGKEV-LVPLGAgLYVKAEVIDTDKVLvdlgagyyvek 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462580496 170 --EEAKKNLQEEIDALESRVESIQRVLADLKVQL 201
Cdd:pfam02996  74 slEEAIEILDKRIEELEKQLEKLEEELEKLKDQI 107
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
100-201 9.17e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 36.67  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462580496 100 EDQQKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMlaDDDCLMIPYQIGDvfishsQEETQEMLEEAKKNLQEE 179
Cdd:COG4717   143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELL--EQLSLATEEELQD------LAEELEELQQRLAELEEE 214

                          90       100
                  ....*....|....*....|..
gi 2462580496 180 IDALESRVESIQRVLADLKVQL 201
Cdd:COG4717   215 LEEAQEELEELEEELEQLENEL 236
 
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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