ID G3AFG7_SPAPN Unreviewed; 258 AA.
AC G3AFG7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Protein BMH2 {ECO:0000313|EMBL:EGW34956.1};
GN ORFNames=SPAPADRAFT_58080 {ECO:0000313|EMBL:EGW34956.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW34956.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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DR EMBL; GL996499; EGW34956.1; -; Genomic_DNA.
DR RefSeq; XP_007372368.1; XM_007372306.1.
DR AlphaFoldDB; G3AFG7; -.
DR STRING; 619300.G3AFG7; -.
DR GeneID; 18872311; -.
DR KEGG; spaa:SPAPADRAFT_58080; -.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; G3AFG7; -.
DR OMA; KGCQLAR; -.
DR OrthoDB; 920089at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
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.
DR PROSITE; PS00797; 1433_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT DOMAIN 5..245
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT REGION 236..258
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 131
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ SEQUENCE 258 AA; 28943 MW; D4A2D7D6A7BE1CAE CRC64;
MPASREDSVY LAKLAEQAER YEEMVENMKA VASSGQELSV EERNLLSVAY KNVIGARRAS
WRIVSSIEQK EESKGNENQV SLIREYRAKI EAELSKICED ILSVLTDHLI SSAQTGESKV
FYYKMKGDYH RYLAEFAVAD KRKEAADLSL EAYKAASDVA VTELPPTHPI RLGLALNFSV
FYYEILNSPD RACHLAKQAF DDAVADLETL SEDSYKDSTL IMQLLRDNLT LWTDLSEAPA
ATEEQPAQQS SEAKADEE
//
