ID J4G0L1_9APHY Unreviewed; 349 AA.
AC J4G0L1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN ORFNames=FIBRA_00758 {ECO:0000313|EMBL:CCL98753.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCL98753.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCL98753.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCL98753.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC {ECO:0000256|ARBA:ARBA00007223}.
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DR EMBL; HE796898; CCL98753.1; -; Genomic_DNA.
DR RefSeq; XP_012178036.1; XM_012322646.1.
DR AlphaFoldDB; J4G0L1; -.
DR STRING; 599839.J4G0L1; -.
DR GeneID; 24093664; -.
DR HOGENOM; CLU_033458_0_1_1; -.
DR InParanoid; J4G0L1; -.
DR OrthoDB; 4371132at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd04452; S1_IF2_alpha; 1.
DR Gene3D; 3.30.70.1130; EIF_2_alpha; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044126; S1_IF2_alpha.
DR InterPro; IPR024055; TIF2_asu_C.
DR InterPro; IPR024054; TIF2_asu_middle_sf.
DR InterPro; IPR011488; TIF_2_asu.
DR PANTHER; PTHR10602; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR PANTHER; PTHR10602:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; eIF-2-alpha, C-terminal domain; 1.
DR SUPFAM; SSF116742; eIF2alpha middle domain-like; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 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:UP000006352}.
FT DOMAIN 12..83
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 125..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 39054 MW; 33C3857CE05BBC01 CRC64;
MRYYEQRYPE VDELVMVQVR QIAEMGAYVK LLEYDNIEGM ILLSELSRRR IRSIQKLIRV
GRNEVVVVLR VDKEKGYIDL SKRRVSPEDI TKCEERYMKS KTVASIMRHV ASKLPSVGAD
GVEQVSEVQD AEAKEAKKSR RAARKEGNED EAAEDMVIPG SNEEDRLEQL YDQIAWPLGK
KYGHPYDAFK LALTEQETVF SSLSSPVQPS TLNILTATIA RRLTPQPIKL RADIELTCYT
PAGIDAIKKA LRAGERESSE AVPIKAKLVA PPLYVLSTNA TDKYAAVDRL ERAIESIQST
IENSGGSLVV KMKPKAISET EEHDLAQLMA KAGEENAEVS GDEDDEEVL
//
