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Conserved domains on  [gi|71987805|ref|NP_501397|]
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Spindle and kinetochore-associated protein 2 [Caenorhabditis elegans]

Protein Classification

prefoldin subunit alpha family protein( domain architecture ID 10503232)

prefoldin subunit alpha is an alpha subunit of prefoldin, a hexameric co-chaperone prefoldin complex that binds and stabilizes newly synthesized polypeptides, allowing them to fold correctly

Gene Ontology:  GO:0016272|GO:0006457|GO:0051082
PubMed:  9630229|33137104

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 23-143 4.60e-27

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: 98.09  E-value: 4.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805    23 IHPKIATEEKEFKKLQKQCEEYAKLKFTCQRLLNEaPKTTEGKTELGQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAI 102
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKE-DEGKEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 71987805   103 KTCDRKMDSLKNMMEKLQKSTNKLKTDLTMLLATMDMPYVE 143
Cdd:pfam02996  80 EILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
 
Name Accession Description Interval E-value
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 23-143 4.60e-27

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: 98.09  E-value: 4.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805    23 IHPKIATEEKEFKKLQKQCEEYAKLKFTCQRLLNEaPKTTEGKTELGQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAI 102
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKE-DEGKEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 71987805   103 KTCDRKMDSLKNMMEKLQKSTNKLKTDLTMLLATMDMPYVE 143
Cdd:pfam02996  80 EILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
Prefoldin_UXT cd23158
protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in ...
 15-138 7.86e-26

protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in the cytoplasmic assembly of RNA polymerase I and can interact with other chaperone complexes, like R2TP, to form the PAQosome. UXT has an important role in the activation of the NF-kappaB pathway. UXT is also a component of the centrosome and is associated with gamma-tubulin. 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: 467474  Cd Length: 128  Bit Score: 94.87  E-value: 7.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805  15 LEDLSENVIHPKIATEEKEFKKLQKQCEEYAKLKFTCQRLL-NEAPKTTEGKTELGQRVFMNIEVRDTKHVVVKLCDDVY 93
Cdd:cd23158   1 YEAFLNEVLKPDLKKVLEERDKLYEEISEYEQLKNTIETLQeNDGLKPLKTLVDLGCNFYVQAKVPDTSKIFVDVGLGFY 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71987805  94 VEMKLQDAIKTCDRKMDSLKNMMEKLQKSTNKLKTDLTMLLATMD 138
Cdd:cd23158  81 VEMTLDEALKFIDKKEKLLEKKADKLTKKAAKIKAHIKLVLEAIR 125
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 37-127 2.79e-06

prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich in coiled coil regions, are molecular chaperones in the class of the prefoldin (GimC) alpha subunit. Prefoldin is a hexamer of two alpha and four beta subunits. This protein appears universal in the archaea but is restricted to Aquifex aeolicus among bacteria so far. Eukaryotes have several related proteins; only prefoldin subunit 5, which appeared the most similar to archaeal prefoldin alpha, is included in this model. This model finds a set of small proteins from the Archaea and from Aquifex aeolicus that may represent two orthologous groups. The proteins are predicted to be mostly coiled coil, and the model may have a significant number of hits to proteins that contain coiled coil regions. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129394 [Multi-domain]  Cd Length: 126  Bit Score: 44.19  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805    37 LQKQCEEYAKLKFTCQRLLN--EAPKTTEGKTEL---GQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAIKTCDRKMDS 111
Cdd:TIGR00293  18 LQAQIAALRALIAELETAIEtlEDLKGAEGKETLvpvGAGSFVKAKVKDTDKVLVSIGSGYYVEKDAEEAIEFLKKRIEE 97

                          90
                  ....*....|....*.
gi 71987805   112 LKNMMEKLQKSTNKLK 127
Cdd:TIGR00293  98 LEKAIEKLQEALAELA 113
GIM5 COG1730
Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];
68-126 5.03e-04

Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441336 [Multi-domain]  Cd Length: 145  Bit Score: 38.35  E-value: 5.03e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71987805  68 LGQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAIKTCDRK----MDSLKNMMEKLQKSTNKL 126
Cdd:COG1730  63 LGGGAFVKAKVKDKDKVIVSLGAGVAVEKDLDEAIEYLEKRikelEKALEKLEEELQELEEEY 125
 
Name Accession Description Interval E-value
Prefoldin pfam02996
Prefoldin subunit; This family comprises of several prefoldin subunits. The biogenesis of the ...
 23-143 4.60e-27

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: 98.09  E-value: 4.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805    23 IHPKIATEEKEFKKLQKQCEEYAKLKFTCQRLLNEaPKTTEGKTELGQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAI 102
Cdd:pfam02996   1 YKQEIESLQAELARLREAIEELEKSLETLKTLKKE-DEGKEVLVPLGAGLYVKAEVIDTDKVLVDLGAGYYVEKSLEEAI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 71987805   103 KTCDRKMDSLKNMMEKLQKSTNKLKTDLTMLLATMDMPYVE 143
Cdd:pfam02996  80 EILDKRIEELEKQLEKLEEELEKLKDQITTLEANLQQVQQK 120
Prefoldin_UXT cd23158
protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in ...
 15-138 7.86e-26

protein UXT; UXT is an alpha subunit of the prefoldin-like complex (PFDL). PFDL is involved in the cytoplasmic assembly of RNA polymerase I and can interact with other chaperone complexes, like R2TP, to form the PAQosome. UXT has an important role in the activation of the NF-kappaB pathway. UXT is also a component of the centrosome and is associated with gamma-tubulin. 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: 467474  Cd Length: 128  Bit Score: 94.87  E-value: 7.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805  15 LEDLSENVIHPKIATEEKEFKKLQKQCEEYAKLKFTCQRLL-NEAPKTTEGKTELGQRVFMNIEVRDTKHVVVKLCDDVY 93
Cdd:cd23158   1 YEAFLNEVLKPDLKKVLEERDKLYEEISEYEQLKNTIETLQeNDGLKPLKTLVDLGCNFYVQAKVPDTSKIFVDVGLGFY 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71987805  94 VEMKLQDAIKTCDRKMDSLKNMMEKLQKSTNKLKTDLTMLLATMD 138
Cdd:cd23158  81 VEMTLDEALKFIDKKEKLLEKKADKLTKKAAKIKAHIKLVLEAIR 125
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 68-137 5.86e-07

Prefoldin alpha subunit; Alpha 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: 467468 [Multi-domain]  Cd Length: 121  Bit Score: 45.68  E-value: 5.86e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805  68 LGQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAIKTCDRKMDSLKNMMEKLQKSTNKLKTDLTMLLATM 137
Cdd:cd00584  50 LGGNAYVRAEVVDIDKVIVHLGLGYYAERDPDGAIEILEKKEDELDKRIEELQAELAELEDEYDQLEQQA 119
Prefoldin_5 cd23157
Prefoldin subunit 5; Prefoldin subunit 5 is one of the alpha subunits of the eukaryotic ...
 45-139 1.85e-06

Prefoldin subunit 5; Prefoldin subunit 5 is one of the alpha 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: 467473  Cd Length: 124  Bit Score: 44.40  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805  45 AKLKFT-CQRLLNEAPKTTEGKT---ELGQRVFMNIEVRDTKHVVVklcdDV----YVEMKLQDAIKTCDRKMDSLKNMM 116
Cdd:cd23157  26 AQAKFKeSKEALEQLKKENEGKEilvPLTSSLYVPGKLSDVDKVLV----DIgtgyYVEKSVEDAKDYFKRKIEFLNEQI 101

                        90       100
                ....*....|....*....|...
gi 71987805 117 EKLQKSTNKLKTDLTMLLATMDM 139
Cdd:cd23157 102 EKLQKILQEKQQNLQAVVEVLQQ 124
TIGR00293 TIGR00293
prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich ...
 37-127 2.79e-06

prefoldin, archaeal alpha subunit/eukaryotic subunit 5; Members of this protein family, rich in coiled coil regions, are molecular chaperones in the class of the prefoldin (GimC) alpha subunit. Prefoldin is a hexamer of two alpha and four beta subunits. This protein appears universal in the archaea but is restricted to Aquifex aeolicus among bacteria so far. Eukaryotes have several related proteins; only prefoldin subunit 5, which appeared the most similar to archaeal prefoldin alpha, is included in this model. This model finds a set of small proteins from the Archaea and from Aquifex aeolicus that may represent two orthologous groups. The proteins are predicted to be mostly coiled coil, and the model may have a significant number of hits to proteins that contain coiled coil regions. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129394 [Multi-domain]  Cd Length: 126  Bit Score: 44.19  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805    37 LQKQCEEYAKLKFTCQRLLN--EAPKTTEGKTEL---GQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAIKTCDRKMDS 111
Cdd:TIGR00293  18 LQAQIAALRALIAELETAIEtlEDLKGAEGKETLvpvGAGSFVKAKVKDTDKVLVSIGSGYYVEKDAEEAIEFLKKRIEE 97

                          90
                  ....*....|....*.
gi 71987805   112 LKNMMEKLQKSTNKLK 127
Cdd:TIGR00293  98 LEKAIEKLQEALAELA 113
Prefoldin_alpha_GimC cd23160
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ...
 60-126 3.28e-05

Prefoldin alpha subunit, archaeal; Archaeal alpha 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: 467476 [Multi-domain]  Cd Length: 127  Bit Score: 41.32  E-value: 3.28e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987805  60 KTTEGKTE----LGQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAIKTCDRKMDSLKNMMEKLQKSTNKL 126
Cdd:cd23160  44 KKLKEGTEilvpIGGGSFVKAKIKDTDKVLVNIGAGVVVEKTIDEAIEILEKRIKELEKALEKLQEQLQQI 114
Prefoldin_URI1 cd23159
RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II ...
 26-133 6.48e-05

RNA polymerase II subunit 5-mediating protein homolog; URI (also called RNA polymerase II fifth subunit regulatory protein or RMP) is an alpha subunit of prefoldin-like complex (PFDL). PFDL is involved in the cytoplasmic assembly of RNA polymerase II and can interact with other chaperone complexes, like R2TP to form the PAQosome. In the cytoplasm, URI acts as a chaperone protein; in the nucleus, URI acts as a transcription regulator and can interact with RPB5 (a subunit of eukaryotic RNA polymerases) and RNA polymerase II (pol II). 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: 467475  Cd Length: 124  Bit Score: 40.23  E-value: 6.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987805  26 KIATEEKEFKKLQKQCEEYAKLKftcqRLLNEAPKTTEGKT--ELGQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAIK 103
Cdd:cd23159  11 ALEETEEKIEQWEKYKKEYEALK----ERLETLPDKLSHDVmvPFGKLAFMPGKLVHTNEILVLLGDNYFVERSAKQAIE 86

                        90       100       110
                ....*....|....*....|....*....|
gi 71987805 104 TCDRKMDSLKNMMEKLQKSTNKLKTDLTML 133
Cdd:cd23159  87 IIERRIKFLEEKLEKLEKELKLLESRLELT 116
GIM5 COG1730
Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];
68-126 5.03e-04

Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441336 [Multi-domain]  Cd Length: 145  Bit Score: 38.35  E-value: 5.03e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71987805  68 LGQRVFMNIEVRDTKHVVVKLCDDVYVEMKLQDAIKTCDRK----MDSLKNMMEKLQKSTNKL 126
Cdd:COG1730  63 LGGGAFVKAKVKDKDKVIVSLGAGVAVEKDLDEAIEYLEKRikelEKALEKLEEELQELEEEY 125
 
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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