ID G8BPS2_TETPH Unreviewed; 256 AA.
AC G8BPS2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=14-3-3 domain-containing protein {ECO:0000259|SMART:SM00101};
GN Name=TPHA0B03310 {ECO:0000313|EMBL:CCE62003.1};
GN OrderedLocusNames=TPHA_0B03310 {ECO:0000313|EMBL:CCE62003.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE62003.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE62003.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
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 -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141}.
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DR EMBL; HE612857; CCE62003.1; -; Genomic_DNA.
DR RefSeq; XP_003684437.1; XM_003684389.1.
DR AlphaFoldDB; G8BPS2; -.
DR STRING; 1071381.G8BPS2; -.
DR GeneID; 11534824; -.
DR KEGG; tpf:TPHA_0B03310; -.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR OMA; KGCQLAR; -.
DR OrthoDB; 920089at2759; -.
DR Proteomes; UP000005666; Chromosome 2.
DR Gene3D; 1.20.190.20; 14-3-3 domain; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; 14-3-3 PROTEIN; 1.
DR PANTHER; PTHR18860:SF17; 14-3-3 PROTEIN EPSILON; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; 14-3-3 protein; 1.
DR PROSITE; PS00796; 1433_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT DOMAIN 5..247
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT REGION 237..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 58
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT SITE 132
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ SEQUENCE 256 AA; 29000 MW; C3DEC2AE0F1A9D85 CRC64;
MSQSREDSVY LAKLAEQAER YEEMVENMKV VASSGQELSV EERNLLSVAY KNVIGARRAS
WRIVSSIEQK EESKEKSEHQ VSLIRTYRSK IETELTKISD DILSVLDSHL IPYATTGESK
VFYYKMKGDY YRYLAEFSSG DVRDKATDSS LEAYKTASEI ATTELPPTHP IRLGLALNFS
VFYYEIQNSP DKACHLAKQA FDDAIAELDT LSEESYKDSA LIMQLLRDNL TLWTSDMSES
NQAEQPSDEA QAQAPK
//
