ID A0A384B733_BALAS Unreviewed; 1513 AA.
AC A0A384B733;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Eukaryotic translation initiation factor 4 gamma 1 isoform X7 {ECO:0000313|RefSeq:XP_007195363.1};
GN Name=EIF4G1 {ECO:0000313|RefSeq:XP_007195363.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007195363.1};
RN [1] {ECO:0000313|RefSeq:XP_007195363.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007195363.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007195363.1; XM_007195301.2.
DR CTD; 1981; -.
DR OrthoDB; 92033at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:SF10; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1; 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 Initiation factor {ECO:0000313|RefSeq:XP_007195363.1};
KW Protein biosynthesis {ECO:0000313|RefSeq:XP_007195363.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681}.
FT DOMAIN 1154..1276
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 1346..1512
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 166788 MW; A7442145BB02C247 CRC64;
MNKAPQPTGP PPAPSPGLPQ GRSTYVVPTQ QYPVQPGAPS FYPGASPTEF GTYAGAYYPA
QGVQQFPTGV APPPVLMSQP PQIAPKRERK TIRIRDPNQG GKDITEEIMS GARTASTPTP
SQTGGGLEPQ ANGETPQVAV VVRPDDRSQG AVIGERPGLP GPEHSPSESQ PSSPSPTPSP
PPVLEPGSEP NLTVLPIPGD SMTTGMIQTS VEESTPMPSE TGEPYCLSPE PTPLAEPILE
VEVTLSKPVP ESEFSSSPLQ VPTPLASHKV EILPEPNGTV LSENLEPELE SSLELAPLPP
PACPSESPMP IAPTAQPEEL LNGAPSPPAV DLSPVSEPEE QAKDATALVA PPTILSATPA
VAPPAASPAQ EEDMEEEEEE EEEGEAEGEK GGEEPLPLES TPVPAHLSQN LEVASVTQVA
VSVPKRRRKI KELNKKEAVG DLLDAFKEVN PGVSEVENQP PVGNNPSPEP EGSSVPPRPE
EADETWDSKE DKIQNAENIQ PGEQKYEYKS DQWKPLNLEE KKRYDREFLL GFQFIFASMQ
KPEGLPHISD VVLDKANKTP LRPLDPSRLQ GINCGPDFTP SFANLGRPAL SSRGPPRGGP
GGELPRGPQA GLGPRRSQQG PRKEPRKIIA TVSMTEDIKL NKAEKAWKPS SKRAVAEKDR
GEEDADGSKT QDLFRRVRSI LNKLTPQMFQ QLMKQVTQLA IDTEERLKGV IDLIFEKAIS
EPNFSVAYAN MCRCLMALKV PTTEKPTVTV NFRKLLLNRC QKEFEKDKDD DEVFEKKQKE
MDEAATAEER GRLKEELEEA RDIARRRSLG NIKFIGELFK LKMLTEAIMH DCVVKLLKNH
DEESLECLCR LLTTIGKDLD FEKAKPRMDQ YFNQMEKIIK EKKTSSRIRF MLQDVLDLRR
SNWVPRRGDQ GPKTIDQIHK EAELEEHREH IKVQQLMAKG SDKRRGGPPG PPISRGLPLV
DDGGWNTVPI SKGSRPIDTS RLTKITKPGS IDSNNQLFAP GGRLSWGKGS SGGSGAKPSD
AASEAARPAT STLNRFSALQ QAVPTESTDN RRVIQRSSLS RERGEKAGDR GDRLERSERG
GDRGDRLDRA RTPATKRSFS KEVEERSRER PSQPEGLRKA ASLTEDRDRG RDAVKREAAL
PPVSPPRAAL SEEELEKKSR AIIEEYLHLN DMKEAVQCVQ ELASPSLLFI FVRHGIESTL
ERSAIAREHM GRLLHQLLCA GHLSTAQYYQ GLYEILELAE DMEIDIPHVW LYLAELVTPI
LHEGGVPMGE LFREITKPLR PLGKAASLLL EILGLLCKSM GPKKVGTLWR EAGLSWKEFL
PEGQDVSAFV TAQKVEYTLG EESEAPGQRL LSSEELSKQL EKLLKEGSSN QRVFDWIEAN
VNEQQVASNT LVRALMTTVC YSAIIFETPL RVDVAVLKAR AKLLQKYLCD EQKELQALYA
LQALVVTLEQ PPNLLRMFFD ALYDEDVVKE DAFYSWESSK DPAEQQGKGV ALKSVTAFFK
WLREAEEEES ENN
//
