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Database: UniProt
Entry: A0A5C3Q1M3_9APHY
LinkDB: A0A5C3Q1M3_9APHY
Original site: A0A5C3Q1M3_9APHY 
ID   A0A5C3Q1M3_9APHY        Unreviewed;       111 AA.
AC   A0A5C3Q1M3;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   28-JUN-2023, entry version 10.
DE   RecName: Full=Tubulin-specific chaperone A {ECO:0000256|RuleBase:RU364030};
GN   ORFNames=K466DRAFT_579452 {ECO:0000313|EMBL:TFK94949.1};
OS   Polyporus arcularius HHB13444.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Polyporus.
OX   NCBI_TaxID=1314778 {ECO:0000313|EMBL:TFK94949.1, ECO:0000313|Proteomes:UP000308197};
RN   [1] {ECO:0000313|EMBL:TFK94949.1, ECO:0000313|Proteomes:UP000308197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB13444 {ECO:0000313|EMBL:TFK94949.1,
RC   ECO:0000313|Proteomes:UP000308197};
RX   PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA   Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA   Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA   Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA   Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA   Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA   Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA   LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA   Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA   Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA   Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA   Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA   Hibbett D.S., Nagy L.G.;
RT   "Megaphylogeny resolves global patterns of mushroom evolution.";
RL   Nat. Ecol. Evol. 3:668-678(2019).
CC   -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC       function by capturing and stabilizing tubulin in a quasi-native
CC       conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC       interaction with cofactor C then causes the release of tubulin
CC       polypeptides that are committed to the native state.
CC       {ECO:0000256|RuleBase:RU364030}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|RuleBase:RU364030}.
CC   -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000256|ARBA:ARBA00006806,
CC       ECO:0000256|RuleBase:RU364030}.
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DR   EMBL; ML210963; TFK94949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C3Q1M3; -.
DR   STRING; 1314778.A0A5C3Q1M3; -.
DR   InParanoid; A0A5C3Q1M3; -.
DR   Proteomes; UP000308197; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0007021; P:tubulin complex assembly; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.58.90; -; 1.
DR   InterPro; IPR004226; TBCA.
DR   InterPro; IPR036126; TBCA_sf.
DR   PANTHER; PTHR21500; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR   PANTHER; PTHR21500:SF0; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR   Pfam; PF02970; TBCA; 1.
DR   SUPFAM; SSF46988; Tubulin chaperone cofactor A; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364030};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364030};
KW   Cytoskeleton {ECO:0000256|RuleBase:RU364030};
KW   Microtubule {ECO:0000256|RuleBase:RU364030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000308197}.
FT   COILED          18..45
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   111 AA;  12870 MW;  259F6674A2E4752D CRC64;
     MSDAVALRKQ LKIKSGSAKR LYKEHKLYQK EEEDLKRKLD KYIADNAEDW DINNTRRMME
     ESGKMIADSA ERLGSVMQEL RDLLVSAERN PELSQDEVVL KAQETLEEVS I
//
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