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Database: UniProt
Entry: A0A1S3LW68_SALSA
LinkDB: A0A1S3LW68_SALSA
Original site: A0A1S3LW68_SALSA 
ID   A0A1S3LW68_SALSA        Unreviewed;      1756 AA.
AC   A0A1S3LW68;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Eukaryotic translation initiation factor 4 gamma 1-like isoform X6 {ECO:0000313|RefSeq:XP_013995091.1};
GN   Name=LOC106568864 {ECO:0000313|RefSeq:XP_013995091.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013995091.1};
RN   [1] {ECO:0000313|RefSeq:XP_013995091.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013995091.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000256|ARBA:ARBA00005775}.
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DR   RefSeq; XP_013995091.1; XM_014139616.1.
DR   GeneID; 106568864; -.
DR   OrthoDB; 92033at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa14.
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_013995091.1};
KW   Protein biosynthesis {ECO:0000313|RefSeq:XP_013995091.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          1397..1519
FT                   /note="MI"
FT                   /evidence="ECO:0000259|PROSITE:PS51366"
FT   DOMAIN          1590..1756
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1121..1399
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        35..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..193
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..351
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..639
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..659
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1177..1204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1263..1285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1286..1338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1345..1374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1756 AA;  190553 MW;  707D2C4C6886E783 CRC64;
     MNKPPQPITG PTSVPHPSPS PGLTQAAYAP GQPPSLVFAT PPPQQMNSSP QPRQPYYANR
     ATMPTSAPRV QTSSGPRPVG PTHVYQPGSQ MMMIPGQQLS FAGSPQGYFI PPGQYRAPYM
     PPSPQYPVTS GTAGFYPGTS PAEYSTYAGA YYPAQPQYSH TPTVQTAPVM ISPAQPQQQA
     LPPQPPPSQP PAPKRERIAI RIRDPNQGGR DITEEIMSGG RATSTPPSQS STTEGEGPSQ
     TNGEVTKPVT MMTRTDDIME PAVSKAMAAV TPPPALVTPE PATATVPAEA KQETDSQAAP
     PTEQVVSQSA VLTAEGKAEE AIPPEEDQAP PTSPSPPAAP TSPPPAEVQT PPPITTIAQV
     SDTVDAGVTL AGKAVTPEAP PIEEEPSAAP AAVEKPPALV AEKEEAENKK EEVVVEEEKV
     EKVKEEPVLT TKPEVVAPVT VAVAEEHTKP APRPLTPVAK ATIKHSAPAV KPVVSMEAPT
     KTESVVEPTA TKRETAAAVP ASAPVPAVTP SVPEAEPAMA QKSEAQTPLS NGLPQEYPDE
     VDAPVPAQER TAMPNTEPAA PTPQETATPA AAAVAEEGEK EEKEEDAATV PLASSPSEDT
     SMQAAVSVPK KKRNMKELNK KEAIGDMLDA FKEEKEAAAA PEPLSTPAEP SPVAPPPLAT
     ADAPDETWEE KEDKQNADTP PLKPGDLKYQ YKGEQWKPID PEDKKRYDRE FLLGFRYIGA
     SMNKPEGLPL ICDVVLDKAN KTPMRPAEPG RNMMNAGPDF TPAFMGNLGR QSSGGGGGGP
     RGPGRDHMGP PGPRRSQQGQ RKEPRKIIIS SSLGGDVELN KAEKAWKPAV KMAGSRGTGP
     DEEESDDPEQ AKTQELFKRV RSILNKLTPQ MFQQLMKQVT ELTIDTEERL KGVIDLIFEK
     AISEPNFSVA YANMCRCLMG LKVPTTDKPG VTVNFRKLLL NRCQKEFEKD QDDDVIFEAK
     QKEMEAAKEE EKAGLKAELE EAKDKARRRS LGNIKFIGEL FKLKMLTEAI MHDCIVKLLK
     NHDEESLECL CRLLSTIGKD LDFEKAKPRM DQYFAQMDKI IKEKKTSSRI RFMLQDVIDL
     RRSGWVPRRG EQGPKTIDQI HKDAEREEQM QLVKVQQQLM SRNDSGGGGG GGGGGGGGGG
     RGGGGGGGGG GRDGRGGDRD RGGRDQGGRG GQHGGQGARG SQPQDEGWNT VPISTKNRPI
     DTSRLSKITK PGALDFNNQL LAPQLGGKGM WGSWGKGSSG GTTGAKPAAG AEPAAETGRP
     ATGNRFSALQ QSAPPASSSD ADRRVPQRSS SSRDRGGDRD RFDRFERRDS SRDARPPVTK
     RSFSRETEER RSDSRTPTEP PVRRVASMSD DRNRGSRDRG GSGSRDRAPS KEAVVKRETN
     PTPPPAAPAK PAMTEEELDK KSSAIIEEYL HLNDMKEALQ CVAELNSAPL LFVFVRNGLE
     DTLERSAIAR ERMGLLLHQL LKAGTLPTTQ YYKGLQEILE VAEDMAIDIP HIWQYLAELI
     TPMLHDGGIP MGQLFREISK PLVPLGKAGL LLVQILNLLC KGMTHKKVGG LWTEAGLNWR
     DFLPEDEDVN KFVTEQKMEF TLGEESDETN QKKPMSGEEL SKHLDRLIQD KANNQRIRDW
     VEANLDQQQA AANQFVRALM TSICQSAVIC ENPYKVDVEQ ITQRAKLLQR YLSDEHRELQ
     ALYALQALMV HMEQPANLLR MFFDALYDED VIKEEAFYRW ESSKDPAEQT GKGVALKSVT
     AFFTWLREAE EESDKD
//
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