ID A0A182WAQ6_9DIPT Unreviewed; 1173 AA.
AC A0A182WAQ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2 {ECO:0000256|ARBA:ARBA00040449};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN007434-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN007434-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN007434-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A182WAQ6; -.
DR STRING; 112268.A0A182WAQ6; -.
DR EnsemblMetazoa; AMIN007434-RA; AMIN007434-PA; AMIN007434.
DR VEuPathDB; VectorBase:AMIN007434; -.
DR OrthoDB; 92033at2759; -.
DR Proteomes; UP000075920; 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; PF02854; MIF4G; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 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 Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 816..941
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 991..1171
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 190..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 132125 MW; 1A463F17613C22F8 CRC64;
MYAQLCKRIQ KELENDIDKT KSSGFLQILL NVCRDKFENR VEYSEKIINS VSTLTDDLEE
KKNVAKQKIL GNVKFIGELY KLGMLREMHL HEMLRSLFIN KKFNSSTEKN CEDMECLAQL
IRTCGKNLDT ELGKQLMDQY FERLEKYSQS QSMFPPRIRF LLRDLIELRK NNWTPRKVAL
VEGPAPIQEL NHDDDVLPPG LNHLRNRDRD YRNNDRSEQR DWIGKLSFNL HNLNDGINLL
SVSSPSPLFP SSYNQSSNGY GGNRDHRDNG GGGGAGGGNY RMHNNRNNQN NYGNNNMRYN
KHNNHHHQGG TGGSMRDGGG NGSHASAYGG NSGMMINKDL APRFKRNLMT PPQNPVEELQ
MRPTPNSLLF KANMNIKPQM PMSSSMGGGN SGNMKPNFNG PPLNEFASPL TTRTLLSEQR
NAGQINSSAF SGGNNNSMGG NGNFGESGNS ASSTSSNINP RGGGMQSDSG VNMAAGRNSG
GSQQSSNQNT PSNMMNQRHQ HMSQGMNPRS MNPASDGSHM HLNKHHSDLN QHHHHYQPNK
QGPHVQVPEH HGGRDMNGDN RMNNSHYEAP HRQHNNEPIN LGLPNTATIG TGNNNVSLLN
GSKLIQKDQV VKQTSADKAE KKKKEKGLSK EYHMKRIATF VDDVLLENIK QQIEEEEQKA
NEGEAKDEKK GNEPNCGATV TEVVVEVVDN KEEKVETSST PPPTDEAIET ETPTPAVEET
PLIENVECIE QKLTEQDDLV EKVKKLDDDE NRAVDLLRGD EKLDVGSETQ KDENDVTTLE
TQQLEQQQES TTEIGGISDE VKTPEETKDS SPLVAASPEP SDVLDEKQVL KKSSLMEELV
NAFCELKIPE KLMRVAMIAI LNQVLDRNDA YHAKTIEFLQ ILNKESKLSD SAALESFKSI
VNGMNEKEKT IPKITSIVAS LLARAVAGNL CNLPDIANFT ENGQHYPLFL LVLQHLHKQL
GKQPLQELFN KSKVDLMSSL PECDRTKDRM AEILEDRNLN FLYPLLRVQA ELWKQIQTDA
NPQQFYKWIK ENVEPSCYAE QGFIVAILTV LFKYIHQETE NLKDDEERVE KETEILTKYC
PVLNAFLNGN NDLQLTAVYA IQVYWYNIGY PKGVLLRWFR AINELNVIED DAFLRYKEDL
TDIYPGKGTA LFQVSQWLKW LEEAEDVDDD EED
//
