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Database: UniProt
Entry: A0A137P1X4_CONC2
LinkDB: A0A137P1X4_CONC2
Original site: A0A137P1X4_CONC2 
ID   A0A137P1X4_CONC2        Unreviewed;       730 AA.
AC   A0A137P1X4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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_41124 {ECO:0000313|EMBL:KXN69037.1};
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:KXN69037.1, ECO:0000313|Proteomes:UP000070444};
RN   [1] {ECO:0000313|EMBL:KXN69037.1, ECO:0000313|Proteomes:UP000070444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN69037.1,
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; KQ964551; KXN69037.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137P1X4; -.
DR   STRING; 796925.A0A137P1X4; -.
DR   EnsemblFungi; KXN69037; KXN69037; CONCODRAFT_41124.
DR   OMA; LWGGPQF; -.
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   SMART; SM00360; RRM; 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"
FT   REGION          692..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  83756 MW;  C434E13685032D0D CRC64;
     MAPAIDFKNI ASEADLDFSS LDEKYSLELD TNFDNIAIVD NIPVIDESKE EKLGNVLRKI
     FKASGTIKEN GIYMPKEEVN GKLTSKGFAF LEFETPEQVA AAIKNVNNYA MDKKHVLLVN
     KINDIEKYTS LEDKYVEPHF EEFQPKEHLL GHLKDPSGRD QYATLIKNMC TIEWNNKSNP
     PEKIESRPNW TESYVLWSPK GTYLTTVHRQ GIALWGGPSW KQIVKFSHPG VSLIDYSPNE
     NYVVTWSNQP IVAGTGATPN QPSPFGADEE GHHFCIWDIK TGLLLRTFPN LPANDDGPVR
     ISWPAFKWSP SDKYFARIHP KQQISIYEAP SMSLLGKKSH KVDGVVDFSW APATHSIKGK
     AFDEMMVYWT PEIGNQPARV SLLRVPDKEV LRNKTLFNVS DCYFHWHPLG ELLAVRVNRH
     AKNKKSQFSN LEIFRVREKD IPVEVIELKD VAIQFSWEPT YHYRFVILTS SDPNPAPSAS
     GAAPQPVKTT IHFYKRERAV NGSIGASKDV FRHLATFDKK TANTVLWSPR GRHLVFATLK
     TQSIFDIEFW DVELPAKYPA DKKNSETSVH LVNTVEHYGL TQLEWDPSGR YVISSASVWQ
     HGMEHGYTLW DMNGNQLIKK VIEDFRQILW RPRPKSLLDE KQKREIEKKL DTYSVEFDKE
     DYYSRNAASA ALLKKRNQLY AEWNEFRSKV EAERQQNATE SKANVSDSTL NEEIEEWVEE
     VVEETEEILE
//
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