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Database: UniProt
Entry: A0A1J9Q478_9EURO
LinkDB: A0A1J9Q478_9EURO
Original site: A0A1J9Q478_9EURO 
ID   A0A1J9Q478_9EURO        Unreviewed;       729 AA.
AC   A0A1J9Q478;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000256|ARBA:ARBA00018601};
DE   AltName: Full=GDP-mannose pyrophosphorylase {ECO:0000256|ARBA:ARBA00031190};
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00030179};
DE   AltName: 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=ACJ73_05760 {ECO:0000313|EMBL:OJD22890.1};
OS   Blastomyces percursus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD22890.1, ECO:0000313|Proteomes:UP000242791};
RN   [1] {ECO:0000313|EMBL:OJD22890.1, ECO:0000313|Proteomes:UP000242791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI222 {ECO:0000313|EMBL:OJD22890.1,
RC   ECO:0000313|Proteomes:UP000242791};
RA   Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA   Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (AUG-2015) 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:OJD22890.1}.
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DR   EMBL; LGTZ01000931; OJD22890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9Q478; -.
DR   STRING; 1658174.A0A1J9Q478; -.
DR   VEuPathDB; FungiDB:ACJ73_05760; -.
DR   OrthoDB; 5474157at2759; -.
DR   Proteomes; UP000242791; 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:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
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; IPR001451; Hexapep.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
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; PF14602; Hexapep_2; 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   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS51363; W2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242791}.
FT   DOMAIN          531..716
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..729
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   729 AA;  81524 MW;  A3F80E777A7670A2 CRC64;
     MGPKSKSGGG AAAARQKSQA AEEERDEALQ AVVLADTFET RFEPFTLERP RCLLPLANTP
     IIEYTLEFLA NAGVEEVFLY GGAHSEQVER YINASKWKSP SSPFKSFVFL KSTSTSVGDV
     MRDLDGKHLI TRDFIIVSGD VVSNYPIEEA LSKHRARRQT DKNAIMTMIL RETNVSHRSN
     PSTAPVFFID PTKDRCLHYE EIESRPRRSS HSSSHPNPSN FLSVDPDMLK EFAEIDVRSD
     LIDTYIDICT PEVLGLWSDS FDYQTPRKQF LFGVLKDYEL NGKTIHTHII KDHYAARVRN
     LKTYDSVTKD TVSRYTYPLC LETNLVPDHT YTLKRGNIYQ EQGVRYAQSC VIGAKTVIGQ
     GTTLGDHTTV KNTVIGRRCR IGKNVVLDGA YLWDDVVVGD GTEVRHAIVA NEAVVGDNCR
     IENGALLSYG VKIANGTTIR EGMKITRAER EQGPVPSDPE IVGEGGVGYE FSREEDEDDE
     SDYESVASSG LLYNMASPSL STASISTLSS EFSDDDFSPL YRSGSFGTSV SDDDGDRAHF
     HHDAVNSIYD GLRDGLSADV VQLELVGLRM SANASEHQVR RAVVTAFLKR IQQLMDAPSP
     SQPSLSASDA VKQVLTKYKD ILERIVFDRD EPVRKPDQVD LLLLIQQELV ERSRGETVLL
     FMAKVLYDLE TVEEEAFEQW WADERGVASE GLKRVRRQTE PFIAWLANAD SEEDDDNDDD
     DDEEEDDNE
//
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