ID A0A151JB07_9HYME Unreviewed; 1981 AA.
AC A0A151JB07;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Eukaryotic translation initiation factor 4 gamma 3 {ECO:0000313|EMBL:KYN22331.1};
GN ORFNames=ALC57_05285 {ECO:0000313|EMBL:KYN22331.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN22331.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN22331.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN22331.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN22331.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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DR EMBL; KQ979182; KYN22331.1; -; Genomic_DNA.
DR STRING; 471704.A0A151JB07; -.
DR Proteomes; UP000078492; 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; IPR049485; eIF4G1-like_eIF4E-bd.
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:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1.
DR Pfam; PF21140; eIF4G1-like_eIF4E-bd; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 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|EMBL:KYN22331.1};
KW Protein biosynthesis {ECO:0000313|EMBL:KYN22331.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078492}.
FT DOMAIN 1608..1730
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 1804..1971
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 36..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1981 AA; 217727 MW; 55919979089026C7 CRC64;
MVSRYGVSKD GAVGVAVGAL GPMHCLLPHC GGPHHHHPLT ASHPQNPQPG HNHHVHPGHQ
PPPPPSPSPH LNQLTHPQLT VNISHLGHHH HQHHQQQPQQ QQQPPQQQQQ TQMPPQYRVA
ANRSEFHGNY SAQPGSQVGG NAASNVGVPT GRGPPPLGGI QTIGQSAAGI PPGGPAGGQA
PSQAPTPGVQ SQPPQGPAPT TTPPVHTPSP QEMGKQAHLQ TQQPSLQQVY VPTQNRPASQ
GYYQTGPRPQ QPRGLSHRGG QGASGTPVVG MAGVGGGGGQ PPAIYSHPAG LPVQASSAMY
LSQSQVHGLH TGPHQQSVYP MNSQIPIHQF SGPPQRHQPQ NQSYYQTFQA PPPILPNVFA
GYAHPPAQHG YFYAASNTMS LTRASTSAVS GGAQHVAGPL AGTQGAPVVP QGTLQQPTQQ
AQPLPPMGIP LSQTDVYSGH NGGVTNTNST TRSRKPRGQN AILDIVNPLT GKNISDEIYK
DNETTQSGES SNRETPQPQN NGAEVIADFA ARVAKAATEG SETVSTSASE TAPNTIQTTA
QTSLSNIHTN SANDTNNRCS SSPPMAKNIA GAGASKTVPT INSQSSLGTC SNATQSDSNV
AKTESKVLQL PVKEFQPRSE IKSVAIEESS PVVSSVIAVA NKDTISVQLT APIVNTETTA
VTATVMAEVE SETVGTTGAV TATGEIPKPS ATASSANPVP TREPFPNLAS KTSSNSPPRR
KPNATELPSN TKEQKERKTR EKSLGSRGAT PTPVVHNQAA DHHHQKTNGD AAGDKSEAEV
VHPRNEIQQK PSDGKAMQKQ KSKNKVKLRE LNRKGAEKEG TDMDAFVNTV STAKTAEIKQ
DNKEQHAPAP KDSNKEPSRE ISKDIKEKDN YESKKEKEIL PVHVKTEKHV STEVSKDSTP
AQQASHVVEK PPTSKESSTK SEDSTFNALP ATNPNDVVDH AAVIEEMHLE AMVAQKNEEN
FKVSALHASN DEKATTIPSV NTEKKQEVEV SSDSGNAPAE IAAPSVNKAA PPLLKYLYKE
GQWSPVNMTG RKSYDREFLL RLQFDPNSKQ KPANLPNLQA VLKDSLQNTH NTMDLRAFKD
ANITRHDSLM PGFAKANIST RPPPTSRKSE SRGKPKPNKP NVITFSLSLR EDVKLRETEN
AWKPARLKQI NQTEEEAKTE ALYKRVRSVL NKLTPQKFNT LVEQVRSLPI DTQERLQGVI
NLVFEKAVDE PSFSVEYALL CKELAQMEVA GYEGQDSSVS FKKLIITRCQ KEFEKNPIDD
VARNRKLKEI DDCNDPEKKK ELQLALEEEE RRIRIKSVGN IRFIGELYRQ QILTTKIMHR
CIRHLLDQND EDNLECLCKL LTTIGKDLEL KGQQANTDEM QEYFNRMQEI VARKGHSKIS
SRIRFMLQDV IDLRANKWIP RRNDNNPKTI DQIQKEAESE RLDMQVNSVP LNTARKDDRN
NDRKRNRGLG GPTDDGWSQP VGRVRPATYS VETAKLKNKP PPMDDMQLGN RASYLWRATN
PSNNSKTISS NKFACLENMS NLDQDKRMPP LPLSGSRSTG PRECSRDYKY DGRNSRNGTH
QSSSASSRES HSLLDNSQSR KVSMLPPVLK SASQSGAISH KAPMSEQEFT KAYNSILKHY
MEEPIIENTA LEIQQKFDNA TFAKLTRECI NHVLEKSPIE RELISKLLSH LLRQNILPME
CFKNGLGEVL EIVDDLVIDI PKIWTYIAEI LSHSIEDGAI ALSELESICI SLRRQGFVGK
FLGELLMKVS RNKGPKWLAD KWDQNNLQLH TLIDPERENA EKIIQEYNLE FLTGDYNSAK
DSIAIEQLSL EKIQENLVRL MKENTSFDEI CSWITANVGD REKDPMFIRH LMTAILETTL
ERHHGTWKLN LESFASLQTL IQRFVDADEL LELQCLYAIQ RYIKLIEFPP GALVSIMNRL
WMDNVISSDA FLTWQQKPPE GADVEGHSVS LVTLTSFFTD LQEPDDNSSV EELSTSANQG
C
//
