ID M7BIE4_CHEMY Unreviewed; 1071 AA.
AC M7BIE4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Eukaryotic translation initiation factor 4B {ECO:0000313|EMBL:EMP36964.1};
GN ORFNames=UY3_05861 {ECO:0000313|EMBL:EMP36964.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36964.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB523361; EMP36964.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BIE4; -.
DR STRING; 8469.M7BIE4; -.
DR eggNOG; KOG0118; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd12402; RRM_eIF4B; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR033107; EIF-4B_RRM.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1.
DR PANTHER; PTHR23239:SF349; KERATIN, TYPE I CYTOSKELETAL 18; 1.
DR Pfam; PF00038; Filament; 2.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000313|EMBL:EMP36964.1};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754};
KW Protein biosynthesis {ECO:0000313|EMBL:EMP36964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 77..408
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT DOMAIN 597..674
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 74..115
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 244..282
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 344..410
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 443..459
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 120464 MW; 99055D5B8A6BABD9 CRC64;
MSFSRSTSYS SNLRSPSIMG RRYAPNTSAA SVYAGAGGSG SRISVARTTS LGSSLPGSSS
GGSYGISLSG SGVVQNEKET MQDLNDRLAS YLERVRSLET DNRKLELQIR EFMDKKGPRS
QDWSRYFQII EDLRNQGGGG TCRTEIREFM DKKGPRSQDW SRYFQIIEDL RNQPAPALLS
APTDPPAMHL PPAQIFESAV GNARIVLQID NARLAADDFR VKFESELAIR QSVESDINGL
RKVLDDTNMS RLQLEGEIES LREELIFMKK NHQDEVDSLQ AQIANSGLTV EVDAAQPQDL
GKVMAEIRAQ YDTLAQKNMA DLDQQWNQMI TQSTAEITEN TKEIEVARSS VSELRRTCQT
LEIELESLRN LKASLEANLR DVEQHYVVQM EHLNGQLLRA EAELAQHSLA VAGQDIYAVI
RYWLEHRGVL FDSFNGDGGN TEAGFGDEED DDDDEVVDSS QQASGETGFP DSQELFLTLD
LEPVPPEPTQ GCLLDPAGGE GTSAKKKNKK GKTLTLTDFL AEDGGSGGGG GTTFIPKPVS
WADETDDLEG DVSTTWHSND DDMYRAAPID RSILPTAPRA AREPNIDRSR LPKSPPYTAF
LGNLPYDVSE ESIKDFFRGL NISAVRLPRE PTNPERLKGF GYAEFEDLDS LLRALSLNEE
SLGNRRIRVD VADQAQDKDR DDRSFGRDRD RNRDSERFET DWRARPATDS FDDYPPRRSE
DSFGDRYRDR DRYNDSDRYR DGPRRDMDRF GGRDRYDDRS RDYDRGGYDS RVGSGRRAFG
TGYRRDDDFR GGGDRYEDRY ERRDDRVDRW SSRDDYARDD IRRDDRGEER LQKEQEKLQR
QLEDDKPRLE RRPRERHPSW RSEENQERSR TGSESSQTGS TGPSVGTGPT GRTTRRRESE
KSLENETFSK EDDAPSPTSK TPKEEKLPLK VMPAPPPKEN AWVKRSSNPP ARSLSSDMEQ
HSPTSSSQGG PAQLSEDRAP PKSASRKGDE NKPDEGKESV PKARGGPGDG GSRDHWQDSD
RKESKNDHDS QSASEPKKPE ENTASKFSYV SKYAALSVDG EDEVEEDNYT D
//
