EIF3A_BRUMA
ID EIF3A_BRUMA Reviewed; 1096 AA.
AC A8PKH2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
GN ORFNames=Bm1_29045;
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; DS239377; EDP33905.1; -; Genomic_DNA.
DR RefSeq; XP_001897252.1; XM_001897217.1.
DR AlphaFoldDB; A8PKH2; -.
DR SMR; A8PKH2; -.
DR STRING; 6279.A8PKH2; -.
DR GeneID; 6100703; -.
DR CTD; 6100703; -.
DR WormBase; Bm2433; BM42517; WBGene00222694; Bma-egl-45.
DR InParanoid; A8PKH2; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1096
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366347"
FT DOMAIN 323..502
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 808..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 591..643
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 677..761
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 811..839
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 808..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 126535 MW; 8DD27DB5A3E2967F CRC64;
MPPNFFQKPE TALKRAHELI SVGKEMDALE TLHDTIKSKR HKQWTKTHEA IMLKHMELCV
SLRRPHMAKD ALFQYKTLTQ QVAIKSLETV IQRFLELAQQ KTEEAQKTSI EKVEEIDDLD
QADAPENLLL SAVSGDAAQD RMDRTVLSPW LRFLWDSYRN CLDLLRNTAV VEQLYHRIAR
QSFEFCAKYQ RRTEFRKLCD NLRLHLTQIQ KHQHLAHVVK LTSAESLTLM QDTRLIQLDT
AIQMELWQEA YRSAEDVHGM MQLSKDKDER MVKPASYVNY YDKLALVFWK AGNRLFHAAA
LLQKYIIYKD MKKTFSMEEA MDQATRVLLA TLAIPDGADN PSDLTRHLDI EEQHIANMRL
LSNLLRLPVA PTRAGILKEI TRLNLPDVAV ESARTLYRLL ECNFAPLRLA SQIQAELTKV
TELNRAEYNQ YVEALKGVTA TKIIKQISVI YDTLSIGRIQ KVIPFYNGDE LERFLVDIAK
HRYVKARIDH RGGSIHFGAA DAALSGFFDL EVSDGFGGEA EQVAVEDIRN HLQSMYNNLR
DAVQVLDYEK IKRAATDDLK RHAEIYLYHK DADYERILLR RKKIESYKET SERQKLEKCQ
QAQAEANRKE EQRRAEEMRR LEQENIEKEK LRRLAEQEEI DRKVRAEKMK KIQATPIYQA
IVKDHGEEAF QNMDPDSVLR EQRDRLDEQR REQQARLQQQ EKKFDHLIRA YHLQEMVARK
AISDNFAVKA PQNHDSYEKR RVENAIKDHE NAVAVYERMQ KVRKDPDAAA FLESVKKARA
DDFNKKIRGF GRRNCVMRNE NVLKNRHELP KEGAEERMAS AREVAEQTRR DEQEKERRAV
RESQRPSKRE IVENSEMDSD WRKSAQPTQP RTISSKPFGE RFVEGERYRE SGAVTASEAD
SGPWVRGNVT GSQRQQDVPI RNIERPAVPS RFSNREQARG EADSTTNWRK GQVAQRDRDQ
SVGKQPLMEK RGEPSGAQLH DVKAVATPSP ADAGPWRRGM IVARDQADSS QRTSAATPTT
QPWRPSRLRQ ADGAPVNGAP SGRILEGSGS NEPSIGKWNR SIQRTGDSHG AQSFRGISQH
QQRRGAADDD RNWRQK
