ID B2B1V8_PODAN Unreviewed; 579 AA.
AC B2B1V8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Translation initiation factor eIF2B subunit gamma {ECO:0000256|ARBA:ARBA00044196};
DE AltName: Full=eIF2B GDP-GTP exchange factor subunit gamma {ECO:0000256|ARBA:ARBA00044229};
GN ORFNames=PODANS_6_4610 {ECO:0000313|EMBL:CAP71093.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP71093.1};
RN [1] {ECO:0000313|EMBL:CAP71093.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP71093.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP71093.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP71093.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP30492.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-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}.
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DR EMBL; CU638744; CAP71093.1; -; Genomic_DNA.
DR EMBL; FO904941; CDP30492.1; -; Genomic_DNA.
DR RefSeq; XP_001909959.1; XM_001909924.1.
DR AlphaFoldDB; B2B1V8; -.
DR STRING; 515849.B2B1V8; -.
DR GeneID; 6194953; -.
DR KEGG; pan:PODANSg6996; -.
DR VEuPathDB; FungiDB:PODANS_6_4610; -.
DR eggNOG; KOG1462; Eukaryota.
DR HOGENOM; CLU_016743_1_0_1; -.
DR OrthoDB; 161736at2759; -.
DR Proteomes; UP000001197; Chromosome 6.
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 CDD; cd04652; LbH_eIF2B_gamma_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR45989; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT GAMMA; 1.
DR PANTHER; PTHR45989:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT GAMMA; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:CDP30492.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 34..149
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT REGION 308..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 62541 MW; 6DF77698354C42DE CRC64;
MPHAVTIATP GLQALILCGP GSSFPTFTAN PDENPKALLP IANRPMVWYP LEFCYRAGIT
NITLICPPSA KEAIDSALKT NPFLTGLPLP RPDLLAPEDL NQNTGTAEIL RLPELQSLVT
SDFLVLPCDL VCELGPEKLL QAWMVKSASL GDVLGDSRAS QGKHSGGLSV YYQTKSETPI
KGEETEFIAT VPLPSSSVLP ASGSLFPHLS KLVCSMPTDT LKDTLEDKKG FPSRHDLVEQ
HPKIKMHTTH RDAHIYIFPQ WVMKFVKEND RLETIGEDVI GWWAKASWQK GLSSKLGFDE
FLALPVDDSS SQHGGTNSPR GETTTTNTTS LETATQKLSL NSTPAEEPNQ VVTFKTPKVE
EPNPMESASK SVEVPPLLAY IHPTSTGTPA KPTPIIRRVD TAQLLLQISL QLAKLPSLEE
IHDTTNPPSP YCHARKVAYP EGVKPRTTIS KSDSLVADNV TVSEKTSIKE SVIGANCQIG
EGAKLQGCLL MDGVVVGKNC KLTKCIIGKR AELGEGCSLS GCEVQENLLV EAKTEAKEEK
FMSSSGLEAT KEELDDAYDE GDDDEEGSVD GEGSGSDEE
//
