ID A0A1D2M673_ORCCI Unreviewed; 973 AA.
AC A0A1D2M673;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
DE Flags: Fragment;
GN ORFNames=Ocin01_18207 {ECO:0000313|EMBL:ODM88475.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM88475.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM88475.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM88475.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
CC -!- FUNCTION: Appears to play a role in the switch from cap-dependent to
CC IRES-mediated translation during mitosis, apoptosis and viral
CC infection. Cleaved by some caspases and viral proteases.
CC {ECO:0000256|ARBA:ARBA00037759}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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:ODM88475.1}.
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DR EMBL; LJIJ01003549; ODM88475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2M673; -.
DR STRING; 48709.A0A1D2M673; -.
DR OMA; CAPLDIN; -.
DR OrthoDB; 92033at2759; -.
DR Proteomes; UP000094527; 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; cd11559; W2_eIF4G1_like; 1.
DR Gene3D; 1.25.40.180; -; 3.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR PANTHER; PTHR23253:SF82; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 2; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Initiation factor {ECO:0000313|EMBL:ODM88475.1};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Protein biosynthesis {ECO:0000313|EMBL:ODM88475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 609..732
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 786..969
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 50..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODM88475.1"
SQ SEQUENCE 973 AA; 111264 MW; 904381B3433D0606 CRC64;
VHRFSPQSPI FDEGATLSFI KITSAVAPFS PPLHFSKPFV QETTTEGPQV IGSASRNLGG
RDEIRSQSST SERWIPPSAI RRDALPHENS DDVKFRKVRG ILNKLTPQTF DRLTEELIRI
GLDSQVLLKG VILLIFEKAL QEPKYVSMYA QLCKKLSKKV PNFDPPNPDN TTTFRRLLLN
KCQDEYANRA RASAMYDQKS AIGNLTPEEE EEKLLAKRKM LGNIKFIGEL GKLEMLTHSI
LHKCCEELVK KTKAEDLECL CQIMSTCGHL LDNDKGKYLM DQYFDRMKEL SENEKLPARI
RFMLQDVIEL RENHWLPRKT ISLKESPKPI QEIRREAHDE LGISDGSRSP TEEFRYLQID
PRRNGRIFGP KKRTGLEDVF APVPIAMTSL GTGPGVITPG EKSLGMETNG FHTPPPMNNY
RPAGGMRGYN PPNNMAPNNM APNNPPYYQQ HKNNMKYHQN HNNMHHNHNH DNHHGQMNNM
HHNMRNNQNN MNNHVGYEKS PVAPRFMKQA QQANQGMVGA PPMPMSTMPM ANEELSFRPP
QNSMIKMIPQ PMKPPTFVPP IMDPRKSPVT AVLPPPVINN PPPVENPLMQ QGNKNTLERK
KNTAPTKEDI IKKVDDIIGE LIAKKSQEEA LEAMKELKMP DRLYCDIIVA ILNKAMDHNE
PDREAVYSFV VYLVEQEFIS VAQFQDSFRV MLDLMGDLEA DIPRIKSYVA AFAGRAICQG
QMTIVEVADL TENGKHYPFL LLVLQHMGKT MERTKLCKLF DESKVNLLTT LPKTDRTKDR
MAEILEEREL SFLFPLLKIQ AEMAKRLQIN SDPTDFLEWV KGQVDVTYQT SHGFIHALMT
VIFKFINGEG LQGIKGNPSQ APEKQMKEKE KALLLKYKPV ISTFLQDRVD LQVIAIYALQ
SAWFALECPK VMLLRWFMNT YELDLIEEDA FLKWKEDIRD DYPGKGKALF QVNQWLNWLE
EEEEEGEEGE GDE
//
