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Database: UniProt
Entry: A0A137NRH2_CONC2
LinkDB: A0A137NRH2_CONC2
Original site: A0A137NRH2_CONC2 
ID   A0A137NRH2_CONC2        Unreviewed;       730 AA.
AC   A0A137NRH2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000256|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000256|HAMAP-Rule:MF_03001};
DE   AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03001};
DE            Short=eIF3 p90 {ECO:0000256|HAMAP-Rule:MF_03001};
DE   AltName: Full=Translation initiation factor eIF3, p90 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03001};
GN   Name=PRT1 {ECO:0000256|HAMAP-Rule:MF_03001};
GN   ORFNames=CONCODRAFT_13113 {ECO:0000313|EMBL:KXN65335.1};
OS   Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS   (Delacroixia coronata).
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC   Ancylistaceae; Conidiobolus.
OX   NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN65335.1, ECO:0000313|Proteomes:UP000070444};
RN   [1] {ECO:0000313|EMBL:KXN65335.1, ECO:0000313|Proteomes:UP000070444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN65335.1,
RC   ECO:0000313|Proteomes:UP000070444};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA   Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA   Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT   Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis and, together
CC       with other initiation factors, stimulates binding of mRNA and
CC       methionyl-tRNAi to the 40S ribosome. {ECO:0000256|PIRNR:PIRNR036424}.
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:0000256|HAMAP-Rule:MF_03001}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03001,
CC       ECO:0000256|PIRNR:PIRNR036424}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001,
CC       ECO:0000256|PIRNR:PIRNR036424}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000256|HAMAP-
CC       Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424}.
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DR   EMBL; KQ964908; KXN65335.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137NRH2; -.
DR   STRING; 796925.A0A137NRH2; -.
DR   EnsemblFungi; KXN65335; KXN65335; CONCODRAFT_13113.
DR   OMA; HLFWAPR; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000070444; 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:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011400; EIF3B.
DR   InterPro; IPR034363; eIF3B_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR14068; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 EIF3 -RELATED; 1.
DR   PANTHER; PTHR14068:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
KW   Initiation factor {ECO:0000256|HAMAP-Rule:MF_03001,
KW   ECO:0000256|PIRNR:PIRNR036424};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03001,
KW   ECO:0000256|PIRNR:PIRNR036424};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070444};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}.
FT   DOMAIN          35..124
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
SQ   SEQUENCE   730 AA;  84029 MW;  0A6CDE1E43F2E34A CRC64;
     MAPAIDFKNI TSEADLDFSF LDEKYNLELD TNFDNIAIVD NIPVIDESRE ERLCNVLRKI
     FRASGTIKEN GIYMPKEEVN GTLISKGFAF LEFESSEQVT AAIRNVNNYA MDKKHTLLVN
     KISDIEKYTT LEENYVEPHF EEFQPKEHLL SHLKDPYGRD QYATLVKNIC TIEWNNKSNP
     AEKIKSVEDW TESYFLWSPK GTYLTTVHSQ GIALWGGPSW KKIVKFPHPG VSLIDYSPNE
     NYVVTWSNQP IIAGASATPS HPSPFGADEE GHHFCIWDVN TGLLLRTFPN LPANDDGPVR
     ISWPAFKWSP SEKYFARLHP KQQISIYEAP SMNLLGKKSH KVGGVVDFSW APATHSIKGK
     AFDEMMVYWT PEIGNQPARV SLLRVPDKEV LRNKTLFSVS DCHFHWHPLG ELLAVRVSRH
     AKNKKSQFSS LEIFRVREKG IPVEVVELKD VAIQFSWEPT YHYRFAIISS NDPNPVPSAS
     GAAPQPVKTT IHFYKRERTV NGNLGASKDV FRHLATFDKK TVNTVLWSPK GRNLVFATLR
     TQSIFDIEFW DVDLPDKYPA EKKNSETSIH LVNVVEQYGF TQLEWDPSGR YVISSASVWQ
     HSMEHGYALW DMNGNQLTKK VIEDFRQILW RPRPRSLLKE KQKREIESNL DTYSVDFDKE
     DYYSRNEAAA ALLKKRNQLY AEWKKFRSKI EAERQKNATK SKSNTYDSTL NEEIEEWVEE
     VVDETEEILV
//
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