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Database: UniProt
Entry: A0A421JRA7_9ASCO
LinkDB: A0A421JRA7_9ASCO
Original site: A0A421JRA7_9ASCO 
ID   A0A421JRA7_9ASCO        Unreviewed;       741 AA.
AC   A0A421JRA7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Translation initiation factor eIF2B subunit epsilon {ECO:0000256|ARBA:ARBA00044144};
DE   AltName: Full=eIF2B GDP-GTP exchange factor subunit epsilon {ECO:0000256|ARBA:ARBA00044345};
GN   ORFNames=JA1_002082 {ECO:0000313|EMBL:RLV94040.1};
OS   Spathaspora sp. JA1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV94040.1, ECO:0000313|Proteomes:UP000285775};
RN   [1] {ECO:0000313|EMBL:RLV94040.1, ECO:0000313|Proteomes:UP000285775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA1 {ECO:0000313|EMBL:RLV94040.1,
RC   ECO:0000313|Proteomes:UP000285775};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC       {ECO:0000256|ARBA:ARBA00007878}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV94040.1}.
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DR   EMBL; NSGQ01000012; RLV94040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421JRA7; -.
DR   STRING; 2028339.A0A421JRA7; -.
DR   Proteomes; UP000285775; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   CDD; cd04197; eIF-2B_epsilon_N; 1.
DR   CDD; cd05787; LbH_eIF2B_epsilon; 1.
DR   CDD; cd11558; W2_eIF2B_epsilon; 1.
DR   Gene3D; 1.25.40.180; -; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 2.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035543; eIF-2B_epsilon_N.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR003307; W2_domain.
DR   InterPro; IPR044123; W2_eIF2B_epsilon.
DR   PANTHER; PTHR45887; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT EPSILON; 1.
DR   PANTHER; PTHR45887:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT EPSILON; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS51363; W2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Initiation factor {ECO:0000313|EMBL:RLV94040.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:RLV94040.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285775}.
FT   DOMAIN          569..737
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  83812 MW;  BA9E2C8ADAD0982A CRC64;
     MPPKGKKKDP SPAATKSKSK KEIVKDDRFQ AIVLTDSFQT RFMPLTAVKP RCLLPLANVP
     LIEYTLEFLA QAGVNEVYLM CSSHGDQIQT YIENSKWSNS KNSPFHIATI MSLESRSVGD
     AMRDLDNRGL ISGDFLLVSG DVVTNMDFNK CLNFHRAKKS VDKDHMVTMV LNQASPLHRT
     RSYIDPATFI LDKKTNRCLY YQGIPSVDGK KTSINIDPEL LEDIEDEFVI RNDLIDCHVD
     ICSPQVPQIF QENFDYQYLR SDFVKGVLTS DLLKKTIYGY ITEDSSEYVA RVESWGTYDA
     VSQDILARWC YPIVPDLNLI EDNSYNYEFN NIYKEDKVIL AQSCKIGTST SIGTNTVVGE
     GTSIKKSVIG RNCKIGNNVI INNSYIWDNT VIKDNSVLEH TIVAANAEIG TNVNLNPGSV
     IGFNVIIGDN KVIGNNVRIV ESQIVKEGDD GFNNSFSDSE DEEENDNKIH KPTIVVSPDF
     AVKDIDLVGE EGKGFMYISD GDEDEDYDES ESVADSYSGM VYQMKHLNVS DESIASISNR
     RGGKRRSHSR TRRYSANSMM SETGFITDEE EEEDFTKEGV ATVARAIENN HDIDTALLEL
     NTLRMSMNVS YHEVRSVTVQ ALVNKIVEFI STDTLNPQEA AVKIFKHWGP MFIRQVFSDQ
     EQVDLLNILQ TKIEILDTAY NQMVLFIAIK TLYDLDITEE ENILQWWNQG EQDVEVRTMT
     AKFIKWLEEA DEEESEESDD E
//
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