GenomeNet

Database: UniProt
Entry: A0A182RCZ2_ANOFN
LinkDB: A0A182RCZ2_ANOFN
Original site: A0A182RCZ2_ANOFN 
ID   A0A182RCZ2_ANOFN        Unreviewed;       464 AA.
AC   A0A182RCZ2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Eukaryotic translation initiation factor 5 {ECO:0000256|ARBA:ARBA00018059};
OS   Anopheles funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN004061-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN004061-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN004061-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC       {ECO:0000256|ARBA:ARBA00010397}.
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DR   AlphaFoldDB; A0A182RCZ2; -.
DR   STRING; 62324.A0A182RCZ2; -.
DR   EnsemblMetazoa; AFUN004061-RA; AFUN004061-PA; AFUN004061.
DR   VEuPathDB; VectorBase:AFUN004061; -.
DR   VEuPathDB; VectorBase:AFUN2_004708; -.
DR   OrthoDB; 5475947at2759; -.
DR   Proteomes; UP000075900; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd11561; W2_eIF5; 1.
DR   Gene3D; 1.25.40.180; -; 1.
DR   Gene3D; 2.20.25.350; -; 1.
DR   Gene3D; 3.30.30.170; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045196; IF2/IF5.
DR   InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR   InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR   InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR   InterPro; IPR003307; W2_domain.
DR   PANTHER; PTHR23001; EUKARYOTIC TRANSLATION INITIATION FACTOR; 1.
DR   PANTHER; PTHR23001:SF7; EUKARYOTIC TRANSLATION INITIATION FACTOR 5; 1.
DR   Pfam; PF01873; eIF-5_eIF-2B; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF100966; Translation initiation factor 2 beta, aIF2beta, N-terminal domain; 1.
DR   SUPFAM; SSF75689; Zinc-binding domain of translation initiation factor 2 beta; 1.
DR   PROSITE; PS51363; W2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          251..412
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          145..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..421
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  51729 MW;  4D1918FA85EDE500 CRC64;
     MATVNVNRNV TDIFYRYKMP RINAKVEGKG NGIKTVIVNM AEVARAIGRP ATYPTKYFGC
     ELGAQTQFDH KNERFIVNGS HDAAKLQDLL DGFIRKFVLC PECDNPETDL LVSSKKGTIS
     QGCKACGFHG PLDVNHKVNT FIIKNPPNVN PASQGASLTE GKRSKRTKKG ENGDDSTVGL
     NTTNGGSTTE NGGAETNGDE SPNGSIAGGA VGENGEDDVN WTVDTSEEAV RARMQDLTDG
     AKNMTVSDDF DKTEKERINI FYELVKKKRD ANELDNVQVH KELVTEASRL DIQSKATLVL
     VELLFTANIT QEARKYRNLL LRFTHEDKKA QKYFMGGLEQ MISLHADKLM DKVPGILKLF
     YDSDVLDEKI ILDWSQKVSK KYVSKEIAAQ IHERAKPFIQ WLQEAEEEES SEEDDDSDLE
     IEYDDRAKVD SLRKEPAKPD PKKLAKASLE EDDEDGDDLN IDDI
//
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