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Database: UniProt
Entry: H2APS4_KAZAF
LinkDB: H2APS4_KAZAF
Original site: H2APS4_KAZAF 
ID   H2APS4_KAZAF            Unreviewed;       395 AA.
AC   H2APS4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=W2 domain-containing protein {ECO:0000259|PROSITE:PS51363};
GN   Name=KAFR0B00760 {ECO:0000313|EMBL:CCF56374.1};
GN   ORFNames=KAFR_0B00760 {ECO:0000313|EMBL:CCF56374.1};
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:CCF56374.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF56374.1, 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   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC       {ECO:0000256|ARBA:ARBA00010397}.
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DR   EMBL; HE650822; CCF56374.1; -; Genomic_DNA.
DR   RefSeq; XP_003955509.1; XM_003955460.1.
DR   AlphaFoldDB; H2APS4; -.
DR   STRING; 1071382.H2APS4; -.
DR   GeneID; 13882598; -.
DR   KEGG; kaf:KAFR_0B00760; -.
DR   eggNOG; KOG2767; Eukaryota.
DR   HOGENOM; CLU_026663_1_0_1; -.
DR   InParanoid; H2APS4; -.
DR   OrthoDB; 5475947at2759; -.
DR   Proteomes; UP000005220; Chromosome 2.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd11561; W2_eIF5; 1.
DR   Gene3D; 1.25.40.180; -; 1.
DR   Gene3D; 2.20.25.350; -; 1.
DR   Gene3D; 3.30.30.170; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045196; IF2/IF5.
DR   InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR   InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR   InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR   InterPro; IPR003307; W2_domain.
DR   PANTHER; PTHR23001; EUKARYOTIC TRANSLATION INITIATION FACTOR; 1.
DR   PANTHER; PTHR23001:SF7; EUKARYOTIC TRANSLATION INITIATION FACTOR 5; 1.
DR   Pfam; PF01873; eIF-5_eIF-2B; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF100966; Translation initiation factor 2 beta, aIF2beta, N-terminal domain; 1.
DR   SUPFAM; SSF75689; Zinc-binding domain of translation initiation factor 2 beta; 1.
DR   PROSITE; PS51363; W2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220}.
FT   DOMAIN          239..395
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          147..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  44176 MW;  84A324C47FB688AF CRC64;
     MSINICRDNH DPFYRYKMPP IQAKVEGRGN GIKTALLNVS DVARALNRPT AYLVKYFGFE
     LGTQTSISVD KDRYLVNGVH EPAKLQDVLD GFINKFVLCG SCKNPETEII ITKSSDLVRD
     CKACGKRTPM DLRHKLSSFI LKNPPASIDT GSKKKKKAAT ASANVRGGGV SISDIAQGKQ
     KEESSQNDEE DDDELARQIN AAASTLEQIE VKDDEWAVDM SEEAIRKRAK ELQVSSSTLS
     PELTKLDEFG EWMLKDDELP SDVELYKKAS ELEILNEPKL GCVLAQCLFT EDIVSEVSEH
     TAFLTKVLAN EDFEKNFLGG IERFLGLDHK DLIPQLPKIL VQLYNNDIVS EEVIINFGTK
     VSKKFVPKEV SKKVRRAAKP FITWLENAES DDDEE
//
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