ID   K1X2T5_MARBU            Unreviewed;       741 AA.
AC   K1X2T5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=MBM_06819 {ECO:0000313|EMBL:EKD15058.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15058.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD15058.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15058.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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}.
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DR   EMBL; JH921443; EKD15058.1; -; Genomic_DNA.
DR   RefSeq; XP_007294708.1; XM_007294646.1.
DR   AlphaFoldDB; K1X2T5; -.
DR   STRING; 1072389.K1X2T5; -.
DR   GeneID; 18762754; -.
DR   KEGG; mbe:MBM_06819; -.
DR   eggNOG; KOG1461; Eukaryota.
DR   HOGENOM; CLU_012507_1_0_1; -.
DR   InParanoid; K1X2T5; -.
DR   OMA; LAQSCKI; -.
DR   OrthoDB; 5474157at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
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; 1.
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:EKD15058.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:EKD15058.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT   DOMAIN          552..731
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  80716 MW;  2F53662F9AA226F0 CRC64;
     MAQAQKSAKG AGGGGGRAAK GGKKAAPGKK VEDERDETLQ AVVLADSFET RFSPFTLQTP
     RCLLPLANTP LIEYTLEFLA MSGVADIYIY CGAHTADVER YIQASKWHPD CPASPFAKLE
     IVRTTARSVG DAMRDLDSRD LITGDFLLVH GDLVSNLPID AALAAHRARR LADKNAIMTM
     VLRAGGLETH RTKSKGITPV FVVDPTKSRC LHYEEINPLQ ANRYVNLDPE LISAHTELEI
     RTDLIDCGID ICTPDVLALW AESFDYEVPR RHFLHGVLKD YELNGKTIHT EVVDDHYAAR
     VFNLQSYEAV SKDILGRWTY PLVPDSNLLA GQSYKFERGG LCKENGVILA RTCKVGKRTV
     VGKDTSIGDG SVVSNSIIGR RCKIGKNVTI QNAYIWDDVA VGDGSVVDRA IIASEAVVGK
     NCKIQPGALL SYGVRIADGK EVKEASRITR AKRRQGDDDS DSDSLSAAVI PSDLSIVGEG
     GSGYLFEDSD EDEDEATIFH SNLIYSTSHL NISSESISTI TSEPSISPPD EGRSRHSSFA
     GSISEDGEPG SSSNENFHHD AVAGLLDALK EGGDFGAARL EFMGLRLGND ATDHQMRRAI
     AVAFTKRITQ LIETSKIEAS KAAGIAFSSP GAESFLKEVA VGTDRLEEDQ VDFIGCLQKD
     LVHRSNGAVI LAAVSQKLYQ LEVLEEEAFL AWWKASENLG DKEDGEMRRV REKTGVFVQW
     LKEAEVEEES SEEEGSEEES E
//