ID A0A1E1FD44_9AGAM Unreviewed; 66 AA. AC A0A1E1FD44; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 02-OCT-2024, entry version 26. DE RecName: Full=T-complex protein 1 subunit gamma {ECO:0000256|ARBA:ARBA00017187}; DE Flags: Fragment; GN Name=Cct3 {ECO:0000313|EMBL:BAV68448.1}; OS Strobilomyces annulatus. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Boletales; Boletineae; Boletaceae; Boletoideae; OC Strobilomyces. OX NCBI_TaxID=889414 {ECO:0000313|EMBL:BAV68448.1}; RN [1] {ECO:0000313|EMBL:BAV68448.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L26-fb1 {ECO:0000313|EMBL:BAV68448.1}; RC TISSUE=Fruit body {ECO:0000313|EMBL:BAV68448.1}; RA Sato H., Tanabe S.A., Toju H.; RT "Host shifts enhance diversification of ectomycorrhizal fungi: RT diversification rate analysis of the ectomycorrhizal fungal genera RT Strobilomyces and Afroboletus with 80-gene phylogeny."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. CC {ECO:0000256|RuleBase:RU004187}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LC083788; BAV68448.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1E1FD44; -. DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF24; T-COMPLEX PROTEIN 1 SUBUNIT GAMMA; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR PROSITE; PS00751; TCP1_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004187}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004187}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU004187}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAV68448.1" FT NON_TER 66 FT /evidence="ECO:0000313|EMBL:BAV68448.1" SQ SEQUENCE 66 AA; 7004 MW; 06C8CB8FD241C113 CRC64; LDPMGGILLT NDGNAILREI DVAHPAAKNM IELSRTQDEE CGDGTTSVIV LAGEILAQSL AQLERD //