ID A0A0V1CZN6_TRIBR Unreviewed; 1753 AA.
AC A0A0V1CZN6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Eukaryotic translation initiation factor 4 gamma 3 {ECO:0000313|EMBL:KRY54679.1};
DE Flags: Fragment;
GN Name=EIF4G3 {ECO:0000313|EMBL:KRY54679.1};
GN ORFNames=T03_12047 {ECO:0000313|EMBL:KRY54679.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY54679.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY54679.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY54679.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRY54679.1}.
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DR EMBL; JYDI01000066; KRY54679.1; -; Genomic_DNA.
DR Proteomes; UP000054653; 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 Gene3D; 1.25.40.180; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000313|EMBL:KRY54679.1};
KW Protein biosynthesis {ECO:0000313|EMBL:KRY54679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 1456..1699
FT /note="MIF4G"
FT /evidence="ECO:0000259|SMART:SM00543"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1554..1581
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 114..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..205
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1721..1745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY54679.1"
SQ SEQUENCE 1753 AA; 199939 MW; 6F760E0448E219D8 CRC64;
LAMEPSSSNV SSDDSKVSST QQPKRFSKLL STLRFSGVPK LTGPSDGKLL DLDDWRSPKP
SLAERLFPKL FRKNAAAKES PKKIFRRSDL KKQIQESLTA RRRADLQRRY EQYALDQEQR
RDKHQSRKSL QPFVDVDLEE SFRKDKINDE DKEQLQEIEN EQQEEEEEEE EEDDDDDDED
EDDDQGKQTE EEDNAENENA EEDDEEEIAS RHKRPLKMES ESEDEDEDQK WNDETDNEKV
PSRPPKASIK SDNGFTENQT TVQERITVGT DDDCKVDDQA SPTCSNLLQR RNGKSLRDLS
MENIFFHDDS KLNLDDTFSF VEADAAPIKA QDSFFNPDGL LSSDECKKED ELCSSSLSYP
ELLPSSEKLT GSGEMVLTPR SESNSTTSCT QSKLLFAESP SVSGRLNVAT PKCRFDADTS
LEFFCSAPFA SSPIVAANYS LASGLPRRRP LPAAPSRLVF DEDAQDGFDA ERMPVNFESP
FQADTNRNSD ILGKIESNEF RIEENVKQDL PDDAENCEQN IFGNQVLEEL KKVKRSKFLD
SRKKIRKEFL DTEAVLSSSD EEEDSGDDEV DEYEAEAGDA DVVKSENDLR VEIGKIHLKQ
MLDDDRQLVE MYKEALIDSR KQRKSIRERR FAWKRNAAKD EEEGQARNAD HDNSDDEENE
ANTTFEKWQQ ERLERMRLMM EMNDSAEEEI LFGNDTNSRI YQFGMQALRA DDSQGIFLKE
NYISFHIPQW VLSELLGVGE ASRKSGQVEI TSFWSSIADD DGATAAHSVI FSQSMDYHSS
ESLLRRSQSA LETAYKCSAD SNSCHDFSKN IFFPITPPKD DTPRNFDTLT PSTRKRRRLL
KEQGTSTTIF DGVFIPRHNR VNNCFHLFSS LKLSSVYKRA VVLSISSVSG RLVVAYAAFN
CALISTCFDF LYNSWLCRKM SDERSNLNVS NGASDNGNGE AKSVDSTEQF VPSVGVDHHN
GTMGNSFTIF RNVKNDSPRE FSNNSVENDL KLDSNEVEEQ LPKSPADEKA SVEVKSLLSS
DVESLTRPKE FDSENERPFR LSKAQLKQLL DEPNGIYLLV HYLRSNFYEG YENGLGECDA
WNKFSSLSND LAPFQQGIVS RSGVVVAYNF PERQTSPADD STVAPQKENG QENKPKEVTE
AASTETMKIP LLRLNGMKMS IPDSSSNEWK EIEMVPILIP MQFVAGDNAE ASIFISKGEL
TVSSNVASAN GISGSRREEC AAAGNVSSEQ GHVEQWLGKG QSTVATKRFV RMVVDDEEEE
RRPGNNVGGH LENGYTKENA EQGGEEDEAP IVSRLSTGAR LNLENNLGKR QDESLEVDQL
GRRLESIELF ELANEVFRKR IIRYSSTEML EIGKLKCCFV QPQGSLILNL QAFNDIIPPE
KPYFRDDELE NNKSTKSSSI EMAPKRQSGI SPDIVIEHRI PNAEVHLHQD SNAWVPSWKR
NNAELTAEQL ETQDLMNDAR MILNKMTEQT FEELAVQFFG ISIRCTTAER AKMLARLMFD
KAVQEPGFSE IYVKLCCRIC SEDFKKKTSE EQKSCPKNTR MELLNLCQTH FCSIRRVHCE
LQEKEELLKR VKDQNVRKEL EAEFEDESAS TKRHTIGVVR LIGKLFLWKM ITLTIVQQCL
MSMMIEEEDI LVEHVCVLLS TMGREFELRI SQQMEREPKR RFMSVDGIYE YLLTIARKGD
TAVRIRFLIE ELIKNREKWN STVEAQKEEE VEDKKDDEKE DAEWEEIKQR GVVKQRRMKD
NGKTQFYKRR QRR
//