cct2

Thermosome subunit 2

557 amino acids

Molecular chaperone that assists in the folding or refolding of nascent or denatured proteins along with ATP hydrolysis (Probable). ATPase activity is highest in thermosome assemblies containing CCT1:CCT2, followed by assemblies containing CCT1:CCT2:CCT3. Seems to contribute to thermosome ATPase activity. Not required for growth.

Belongs to the TCP-1 chaperonin family.

59.298 kDa

MSQRMQQGQPMIIMGEDAQRVKDRDAQEYNIRAARAVAEAVRSTLGPKGMDKMLVDSMGDVTITNDGVTILKEMDIDNPTAEMIVEVAETQEDEAGDGTTTAVAIAGELLKNAEDLLEQDIHPTAIIRGFNLASEKAREEIDDIAERVDPDDEELLKKVAETSMTGKSSELNKELLADLIVRAVRQVTVEANDGSHVVDLENVSIETQTGRSASESELLTGAVIDKDPVHDDMPVQFDEADVLLLNEPVEVEETDIDTNVSIESPDQLQKFLDQEEAQLKQKVDQIVDSGADVVFCQKGIDDLAQHYLAKQGILAVRRTKKSDIRFLKNITGAAVVSDLDSIEAAVLGRASVRRDEAGELFYVEGIGDDVHGVTLLLRGSTDHVVDELERGVQDALDVVASTVADGRVLAGGGAIEVELASRLRNYADSVSGREQLAVEAYADALELVPRVLAENAGLDSIDTLVDLRAAHEDGQVRAGLNVFTGEVEDAFDAGVVETAHAKEQAVASASEAANLVLKIDDIIAAGDLSTGGDDDEEGGAPGGMGGMGGMGGMGGAM

CCT2

T-complex protein 1 subunit beta

535 amino acids

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).

Belongs to the TCP-1 chaperonin family.

57.488 kDa

MASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC

CCT2

T-complex protein 1 subunit beta

535 amino acids

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.

Belongs to the TCP-1 chaperonin family.

57.488 kDa

MASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC

Cct2

T-complex protein 1 subunit beta

535 amino acids

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.

Belongs to the TCP-1 chaperonin family.

57.477 kDa

MASLSLAPVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDAALMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFWQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC

Cct2

T-complex protein 1 subunit beta

535 amino acids

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.

Belongs to the TCP-1 chaperonin family.

57.458 kDa

MASLSLAPVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFWQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTMLASRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGRITAGLDMKEGSIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC

CCT2

T-complex protein 1 subunit beta

535 amino acids

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.

Belongs to the TCP-1 chaperonin family.

57.475 kDa

MASLSLAPVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAARQALLNSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFVGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLASRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGKTTAGLDMKEGTIGDMSVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC

cct2

T-complex protein 1 subunit beta

532 amino acids

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).

Belongs to the TCP-1 chaperonin family.

57.955 kDa

MSSQLAPIPILNQNASEERGEIARLSSFVGAIAITDLVKTTLGPKGMDKILISASNPNELIITNDGATILTKIYIDNPAAKILVDISRTQDDEVGDGTTSVCVLAGELLREGERLVQQKVHPQTIISGWRLALETARAALQSSTQDHSSDKVKFREDLLNIARTTLSSKILHTEKDHFANMVVDAVLRLNGNTNLDNIHIIKKSGGSLRESYLDEGFILEKKIGVGCPKRLENPKILIANTAMDTDKIKIFGGKVVVDSMTELAKMEDAEKEKMLNKCKKIVDHGINCFVNRQLVYNLPEQYFAEHGVMSIEHADFDGIERLALVTGAEIVSTFDHPELVKIGTCKLIEEVMIGEDKVIRFSGIPSGEACTIVLRGATSHILEEAERSIHDALCVLAVTVAETRTVLGAGCSEMIMSKAVDELAAITPGKKAMAIESFAKALRQIPTIIANNAGYDSSELVSQLKAAHHQGDKKAGLNMRDGCIGNAEELGVIESFKVKQQVLVSAHEAAEMIMRVDDILRAAPRQRSNLQH

cct2

Probable T-complex protein 1 subunit beta

527 amino acids

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).

Belongs to the TCP-1 chaperonin family.

56.677 kDa

MSLNPHQIFNESGIQERGENARLSSFVGAIAVGDLVKSTLGPKGMDKILQSNSSGDIVVTNDGATILKSIALDNAAAKVLVNISKVQDDEVGDGTTSVCVFAAELLRQAEIMVNAKIHPQVIIDGYRIATKTAIDALRASSIDNSSDPAKFRSDLENIARTTLSSKILSQNKNHFAQLAVDAVLRLKGSTNLDNIQIIKILGGKLDDSFLDEGFILNKTIGVNCPKVMENANILIANTAMDTDKVKVFGARVRVDTTGKLAELERAEREKMKAKVEKIKSHNINCFINRQLIYNWPEQLFADAGIMSIEHADFDGIERLSLVTGGEIASTFDHPELVKLGHCKKIEEIIIGEDKMIKFSGVEAGEACTIVLRGATHQLLDESERAIHDALAVLSQTVAESRVTLGGGCAEMLMAKAVEEAATHEPGKKAVAVSAFAKALSQLPTILADNAGFDSSELVAQLKAAHYDGNDTMGLDMDEGEIADMRAKGILEALKLKQAVVSSGSEGAQLLLRVDTILKAAPRPRERM

CCT2

T-complex protein 1 subunit beta

527 amino acids

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.

Belongs to the TCP-1 chaperonin family.

57.203 kDa

MSVQIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSNTCMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAELLREAEKLIDQSKIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFREDLIHIAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGKLSDSFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKVDSTAKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLGINSIEHADFEGVERLALVTGGEVVSTFDEPSKCKLGECDVIEEIMLGEQPFLKFSGCKAGEACTIVLRGATDQTLDEAERSLHDALSVLSQTTKETRTVLGGGCAEMVMSKAVDTEAQNIDGKKSLAVEAFARALRQLPTILADNAGFDSSELVSKLRSSIYNGISTSGLDLNNGTIADMRQLGIVESYKLKRAVVSSASEAAEVLLRVDNIIRARPRTANRQHM

CCT2

T-complex protein 1 subunit beta

527 amino acids

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.

Belongs to the TCP-1 chaperonin family.

57.286 kDa

MPIDKIFKDDASEEKGERARMASFVGAMAISDLVKSTLGPKGMDKILQSTGRGHAVTVTNDGATILKSLHIDNPAAKVLVDISKVQDDEVGDGTTSVVVLAGELLREAEKLVASKIHPMTIIAGYRMASECARNALLKRVIDNKDNAEKFRSDLLKIAMTTLCSKILSQDKEHFAEMAVDAVFRLKGSTNLEAIQIIKKPGGSLKDSFLDEGFILDKKIGIGQPKRIENANILVANTAMDTDKVKIYGARVRVDSMTKVAEIEGAEKEKMKDKVKKIIGHGINCFVNRQLIYNFPEELFADAGILAIEHADFEGIERLGLVTGGEIASTFDNPESVKLGHCKLIEEIMIGEDKLIHFSGCEMGQACSIVLRGASHHVLDEAERSLHDALCVLSQTVNDTRVLLGGGWPEMVMAKEVDELARKTAGKKSHAIEAFSRALVAIPTTIADNAGLDSAELVAQLRAEHHTEGCNAGIDVITGAVGDMEERGIYEAFKVKQAVLLSATEASEMILRVDEIITCAPRRREDRM

CCT2

T-complex protein 1 subunit beta

508 amino acids

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis.

Belongs to the TCP-1 chaperonin family.

55.671 kDa

MNIFSHANLGTTEERGDDAKRTILAGTDIVGDILKTTLGPKGMLKMLKGQHVNVTNDGAFILNNLMIDSPSARILIGSSTGQDWEEGDGTTSVAILASLLVKEAGKLEMHPTKILRGYRMAQAKCEEILSSISFEATKEDLLKLVRTTLCSKVLRYDLERFCEICVNAVEKLEGRNDLNLIQIIKCSGKLEDSYLDDGFLLKKDIRIDDVVNPRVLIANTSMDQDKIKVFGAKINVNSVGELEEMEKAEKIKIKGKVERISQNGVNVFVNRQLVYDYPLQLLRMKGIQAIEHADFDGVERLNNVLGGKILSTFDNMDESCYGTCESIRNVHVGNERMIKFSGVRSGASTIVLCGSSKEMLDEAERSVHDALCVLAKIKEDPRVIYGGGSSEMAMAVGLNKYAMEVPGAESDAILAFSSALQQIPKILADNGGYNGESIKASLRAEHNSGRTSYGVNVRNGSIGCMKEAGVVDSLRIKHRVVTAASETAQMIIKCDAIVKCKPRERTRE

CCT2

Choline-phosphate cytidylyltransferase 2

304 amino acids

Plays an important role in the biosynthesis of the phospholipid phosphatidylcholine. Catalyzes the formation of CDP-choline.

Belongs to the cytidylyltransferase family.

34.983 kDa

MSVNGENKVSGGDSSSSDRPVRVYADGIFDLFHFGHARAIEQAKKSFPNTYLLVGCCNDEITNKFKGKTVMTESERYESLRHCKWVDEVIPDAPWVLTTEFLDKHKIDYVAHDALPYADTSGAGNDVYEFVKSIGKFKETKRTEGISTSDIIMRIVKDYNQYVLRNLDRGYSREELGVSFEEKRLRVNMRLKKLQEKVKEQQEKIQTVAKTAGMHHDEWLENADRWVAGFLEMFEEGCHKMGTAIRDGIQQRLMRQESEENRRLLQNGLTISKDNDDEQMSDDNEFAEEDCVNVSNKGIETVKK

CCT2

T-complex protein 1 subunit beta

150 amino acids

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.

Belongs to the TCP-1 chaperonin family.

15.887 kDa

multiple

AGADEERAETARLSSFIGAIAIGDLVKVQDDEVGDGTTSVTVLAAELLRLGGSLADSYLDEGFLLDKKQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKGATQQILDEAERQVLLSAAEAAEVILRVDNIIK