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Database: UniProt
Entry: H2AMY8_KAZAF
LinkDB: H2AMY8_KAZAF
Original site: H2AMY8_KAZAF 
ID   H2AMY8_KAZAF            Unreviewed;       168 AA.
AC   H2AMY8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Transcription initiation factor TFIID subunit 13 {ECO:0008006|Google:ProtNLM};
GN   Name=KAFR0A03030 {ECO:0000313|EMBL:CCF55738.1};
GN   ORFNames=KAFR_0A03030 {ECO:0000313|EMBL:CCF55738.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF55738.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF55738.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; HE650821; CCF55738.1; -; Genomic_DNA.
DR   RefSeq; XP_003954873.1; XM_003954824.1.
DR   AlphaFoldDB; H2AMY8; -.
DR   STRING; 1071382.H2AMY8; -.
DR   GeneID; 13887131; -.
DR   KEGG; kaf:KAFR_0A03030; -.
DR   eggNOG; KOG3901; Eukaryota.
DR   HOGENOM; CLU_076665_0_2_1; -.
DR   InParanoid; H2AMY8; -.
DR   OrthoDB; 1326266at2759; -.
DR   Proteomes; UP000005220; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd07978; TAF13; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR003195; TFIID_TAF13.
DR   PANTHER; PTHR11380; TRANSCRIPTION INITIATION FACTOR TFIID/SUPT3-RELATED; 1.
DR   PANTHER; PTHR11380:SF5; TRANSCRIPTION INITIATION PROTEIN SPT3 HOMOLOG; 1.
DR   Pfam; PF02269; TFIID-18kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220}.
FT   REGION          103..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..130
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   168 AA;  18950 MW;  23CAF6AEC2DA2692 CRC64;
     MSRRLKRTNL FSKDISSLLY AYGDVPQPLT ETVQCIDELV SQYLVDICAT ASQTSQNSSR
     NKIKLEDFRF AIRKDPIKLA RAEELIATNK VIIEAKKQFN ETDNQSLKRY RGQDNEFEDD
     DEDNDIEGAA NEEENASVRP KRKDAAKTGG KVKATAAKTS KNNKDDAE
//
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