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Conserved domains on  [gi|388240786|ref|NP_001252525|]
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prefoldin subunit 6 [Homo sapiens]

Protein Classification

prefoldin subunit 6( domain architecture ID 10089799)

prefoldin subunit 6 (PFDN6) is a beta subunit of prefoldin, a hexameric co-chaperone prefoldin complex that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly; similar to human PFDN6 (also known as Protein Ke2)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prefoldin_6 cd23161
Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic ...
 13-113 2.26e-36

Prefoldin subunit 6; Prefoldin subunit 6 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: 467477 [Multi-domain]  Cd Length: 101  Bit Score: 119.89  E-value: 2.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786  13 VEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYES 92
Cdd:cd23161    1 SKEFQKLQKELQKLVEARQQLEAQLNENEMVKKELDLLEDDAKVYKLIGPVLVKQDLDEAKSNVDKRLEFITGEIKRVEK 80

                         90       100
                 ....*....|....*....|.
gi 388240786  93 QLRDLERQSEQQRETLAQLQQ 113
Cdd:cd23161   81 QIKDLEKKQEKKREKIAKLQQ 101
 
Name Accession Description Interval E-value
Prefoldin_6 cd23161
Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic ...
 13-113 2.26e-36

Prefoldin subunit 6; Prefoldin subunit 6 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: 467477 [Multi-domain]  Cd Length: 101  Bit Score: 119.89  E-value: 2.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786  13 VEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYES 92
Cdd:cd23161    1 SKEFQKLQKELQKLVEARQQLEAQLNENEMVKKELDLLEDDAKVYKLIGPVLVKQDLDEAKSNVDKRLEFITGEIKRVEK 80

                         90       100
                 ....*....|....*....|.
gi 388240786  93 QLRDLERQSEQQRETLAQLQQ 113
Cdd:cd23161   81 QIKDLEKKQEKKREKIAKLQQ 101
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 13-114 3.24e-16

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 68.79  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786   13 VEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYES 92
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80

                          90       100
                  ....*....|....*....|..
gi 388240786   93 QLRDLERQSEQQRETLAQLQQE 114
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKFGQ 102
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
1-118 1.19e-06

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 44.11  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786   1 MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQElgeaRATVGKRL 80
Cdd:COG1382    1 MMQNLPPEVQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTD----KEEVIKEL 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 388240786  81 DyitAEIKRYESQLRDLERQSEQQRETLAQLQQEFQRA 118
Cdd:COG1382   77 E---EKKETLELRLKTLEKQEERLQKQLEELQEKLQEA 111
PRK09343 PRK09343
prefoldin subunit beta; Provisional
 1-118 6.87e-06

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 42.36  E-value: 6.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786   1 MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQelgearaTVGKRL 80
Cdd:PRK09343   1 MAENIPPEVQAQLAQLQQLQQQLERLLQQKSQIDLELREINKALEELEKLPDDTPIYKIVGNLLVKV-------DKTKVE 73

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 388240786  81 DYITAEIKRYESQLRDLERQSEQQRETLAQLQQEFQRA 118
Cdd:PRK09343  74 KELKERKELLELRSRTLEKQEKKLREKLKELQAKINEM 111
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
 5-118 3.54e-04

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 37.33  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786    5 IQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEAratvgkrLDYIT 84
Cdd:TIGR02338   1 IPPQVQNQLAQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERLPDDTPVYKSVGNLLVKTDKEEA-------IQELK 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 388240786   85 AEIKRYESQLRDLERQSEQQRETLAQLQQEFQRA 118
Cdd:TIGR02338  74 EKKETLELRVKTLQRQEERLREQLKELQEKIQEA 107
 
Name Accession Description Interval E-value
Prefoldin_6 cd23161
Prefoldin subunit 6; Prefoldin subunit 6 is one of the beta subunits of the eukaryotic ...
 13-113 2.26e-36

Prefoldin subunit 6; Prefoldin subunit 6 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: 467477 [Multi-domain]  Cd Length: 101  Bit Score: 119.89  E-value: 2.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786  13 VEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYES 92
Cdd:cd23161    1 SKEFQKLQKELQKLVEARQQLEAQLNENEMVKKELDLLEDDAKVYKLIGPVLVKQDLDEAKSNVDKRLEFITGEIKRVEK 80

                         90       100
                 ....*....|....*....|.
gi 388240786  93 QLRDLERQSEQQRETLAQLQQ 113
Cdd:cd23161   81 QIKDLEKKQEKKREKIAKLQQ 101
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 13-114 3.24e-16

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 68.79  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786   13 VEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYES 92
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLDEDTKVYKLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80

                          90       100
                  ....*....|....*....|..
gi 388240786   93 QLRDLERQSEQQRETLAQLQQE 114
Cdd:pfam01920  81 QLEKLEKELEELKEELYKKFGQ 102
Prefoldin_beta cd00632
Prefoldin beta subunit; Beta subunits of prefoldin, a hexameric molecular chaperone complex, ...
 22-99 4.33e-12

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: 57.35  E-value: 4.33e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388240786  22 DLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYESQLRDLER 99
Cdd:cd00632    1 EVLALKSQKEELERKINEQKVVLDELSNLKKNRKVYRQQGNIFILASKEETLSELKKTLDHLQKEIKELEQQLKAKEK 78
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
1-118 1.19e-06

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 44.11  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786   1 MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQElgeaRATVGKRL 80
Cdd:COG1382    1 MMQNLPPEVQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKLPDDAEVYKSVGNLLVKTD----KEEVIKEL 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 388240786  81 DyitAEIKRYESQLRDLERQSEQQRETLAQLQQEFQRA 118
Cdd:COG1382   77 E---EKKETLELRLKTLEKQEERLQKQLEELQEKLQEA 111
PRK09343 PRK09343
prefoldin subunit beta; Provisional
 1-118 6.87e-06

prefoldin subunit beta; Provisional


Pssm-ID: 181787 [Multi-domain]  Cd Length: 121  Bit Score: 42.36  E-value: 6.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786   1 MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQelgearaTVGKRL 80
Cdd:PRK09343   1 MAENIPPEVQAQLAQLQQLQQQLERLLQQKSQIDLELREINKALEELEKLPDDTPIYKIVGNLLVKV-------DKTKVE 73

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 388240786  81 DYITAEIKRYESQLRDLERQSEQQRETLAQLQQEFQRA 118
Cdd:PRK09343  74 KELKERKELLELRSRTLEKQEKKLREKLKELQAKINEM 111
Prefoldin_2 cd23163
prefoldin subunit 2; Prefoldin subunit 2 is one of the beta subunits of the eukaryotic ...
 13-107 7.68e-05

prefoldin subunit 2; Prefoldin subunit 2 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: 467479  Cd Length: 100  Bit Score: 39.04  E-value: 7.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786  13 VEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYES 92
Cdd:cd23163    3 VAQYNQLRQEQQQLASKIAELEQELNEHKLVIDTLKPLDPDRKCFRLVGGVLVERTVGEVLPALEENKENLEEVIEQLNE 82

                         90
                 ....*....|....*
gi 388240786  93 QLRDLERQSEQQRET 107
Cdd:cd23163   83 QLEEKEKELNEFREK 97
Prefoldin_beta_GimC cd23162
Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), a hexameric ...
 12-118 8.78e-05

Prefoldin beta subunit, archaeal; Archaeal beta subunit of prefoldin (GimC), 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: 467478 [Multi-domain]  Cd Length: 102  Bit Score: 39.00  E-value: 8.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786  12 EVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDyiTAEIKrye 91
Cdd:cd23162    2 QLAQLQQLQQQLQAVLLQKQQLEAELREIERALEELEKLPDDAEVYKSVGTILVKVDKEEVIKELKERKE--TLELR--- 76

                         90       100
                 ....*....|....*....|....*..
gi 388240786  92 sqLRDLERQSEQQRETLAQLQQEFQRA 118
Cdd:cd23162   77 --LKTLEKQEERLRKQLEELQKKIQEA 101
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
 5-118 3.54e-04

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 37.33  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388240786    5 IQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEAratvgkrLDYIT 84
Cdd:TIGR02338   1 IPPQVQNQLAQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERLPDDTPVYKSVGNLLVKTDKEEA-------IQELK 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 388240786   85 AEIKRYESQLRDLERQSEQQRETLAQLQQEFQRA 118
Cdd:TIGR02338  74 EKKETLELRVKTLQRQEERLREQLKELQEKIQEA 107
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
 7-47 7.01e-03

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 35.17  E-value: 7.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 388240786   7 KKLQGEVEKYQQ-----LQKDLSKSmsgrqKLEAQLTENNIVKEEL 47
Cdd:cd07136   27 KKLKQAIKKYENeileaLKKDLGKS-----EFEAYMTEIGFVLSEI 67
 
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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