ID A0A168QF99_ABSGL Unreviewed; 642 AA.
AC A0A168QF99;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Translation initiation factor eIF2B subunit alpha {ECO:0000256|ARBA:ARBA00044208};
DE AltName: Full=eIF2B GDP-GTP exchange factor subunit alpha {ECO:0000256|ARBA:ARBA00044236};
DE Flags: Fragment;
GN Name=ABSGL_10413.1 scaffold 12013 {ECO:0000313|EMBL:SAM04548.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM04548.1};
RN [1] {ECO:0000313|EMBL:SAM04548.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM04548.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000256|ARBA:ARBA00007251, ECO:0000256|RuleBase:RU003814}.
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DR EMBL; LT554405; SAM04548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168QF99; -.
DR STRING; 4829.A0A168QF99; -.
DR InParanoid; A0A168QF99; -.
DR OrthoDB; 2729759at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1070; Translation initiation factor eIF-2B, N-terminal domain; 1.
DR InterPro; IPR042528; elF-2B_alpha_N.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR013889; Karyogamy_KAR9.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR45860; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT ALPHA; 1.
DR PANTHER; PTHR45860:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT ALPHA; 1.
DR Pfam; PF01008; IF-2B; 1.
DR Pfam; PF08580; KAR9; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT REGION 224..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 642
FT /evidence="ECO:0000313|EMBL:SAM04548.1"
SQ SEQUENCE 642 AA; 71801 MW; BD64B6577147FCBB CRC64;
MTMTYNDKTD FDVVSSYHTY LEDREISTPV AIFKALTDFV RQSTDIDTRG WILTLPWRFI
ALSLAPTMSE FMQTLEKAAK ALRDASEKTG HHLAEKQQYQ HHKATIATLA GLDLFMRFVT
RNSHDFSLSA EARTFDDFKT NLLSRATLIL DKASLARLRA AEIGAQFIHD NAVILVQAYS
RVIMGVLYHA ANVQNKRFKV LVAEGRPNSE GLKAVEELKE AGIPCRAEQR SGGPATTVAA
LDPKDPKDST HDSTHDSTHD SDSTTSTTAS TTATSTLAPD DILVDIDKRV GPVYGDVNKI
YTRMMVDTPP PTDVTGILGR RHRMIQERWE GLRVEIDELK ADLKEDRWLT VFKQVADQVE
TMMDGLDKMV EQCQTMVQQV REWQGIQQLS CSSSSSTVTP QLQQQQQQYP VPPKGILRSS
KSHHSSASVS SNSSSGSSGP PPPPVDHIKL RSLEKNFEAK YKYCTPLITK MLSMLGENIA
TRAAENNATV ARHQHMVQRW QQLKSNMDDL RIRDLPDIDR LLLFERPISP AWSKVSDRSD
KSGGSHRYKS PEPSSYDMFD YRSSSNNLGS MGGRARSPLS TQQHQLQQLQ QLQHHGNNGY
MSPTAQLYGM QEEMRRGRSV TPSSGTGSRD QISLWRSANG GS
//
