ID F0W176_9STRA Unreviewed; 1363 AA.
AC F0W176;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Eukaryotic translation initiation factor 3 subunit p {ECO:0000313|EMBL:CCA14802.1};
GN Name=AlNc14C6G853 {ECO:0000313|EMBL:CCA14802.1};
GN ORFNames=ALNC14_009450 {ECO:0000313|EMBL:CCA14802.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA14802.1};
RN [1] {ECO:0000313|EMBL:CCA14802.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA14802.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FR824051; CCA14802.1; -; Genomic_DNA.
DR EnsemblProtists; CCA14802; CCA14802; ALNC14_009450.
DR HOGENOM; CLU_003256_0_0_1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0051640; P:organelle localization; IEA:UniProt.
DR GO; GO:0006996; P:organelle organization; IEA:InterPro.
DR CDD; cd15466; CLU-central; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR033646; CLU-central.
DR InterPro; IPR025697; CLU_dom.
DR InterPro; IPR028275; CLU_N.
DR InterPro; IPR027523; CLU_prot.
DR InterPro; IPR023231; GSKIP_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12601:SF6; CLUSTERED MITOCHONDRIA PROTEIN HOMOLOG; 1.
DR PANTHER; PTHR12601; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT EIF-3; 1.
DR Pfam; PF13236; CLU; 1.
DR Pfam; PF15044; CLU_N; 1.
DR Pfam; PF12807; eIF3_p135; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF103107; Hypothetical protein c14orf129, hspc210; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51823; CLU; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Initiation factor {ECO:0000313|EMBL:CCA14802.1};
KW Protein biosynthesis {ECO:0000313|EMBL:CCA14802.1}.
FT DOMAIN 421..702
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1363 AA; 148942 MW; 315E3D581C3CC07C CRC64;
MGEAKTDALE SPPLAPLSTA SLPTEQNGLS PEDVDLHKTM EELDDPGFSL YVFPPNCTAQ
SDRILLEHVT AADTVLSLRQ LVAEYPQVAA YTCYHLEAEI NKDGKQQCVP LNDFVELGEY
PDIVDQVEIK MILEKYDARK ARQHVGRFRE LLVNPPIPQS VLAESSQAAM GKKTRTNSMR
SSRDGKLSTK KKKGTSKSED GNDTKSLTTS SSSNPDQKEC LVGGNGKPDL PGKVPPVSDK
VYSALDQIQI PVPNNLGDYY TMTTTGDDLK ESKLNALGQG NGGSGSTVEL PTCIRSIVFS
GFNPPPASRK LTGDLLYLEI QVEGEESVLH VTSHVDGFFI NRSSQGHFNP HVHEAHGHQD
HLLLNVLRNA SSVFETSYQS VLSRASMLAK EGPASIQWMI AAGNDIGGKL PWITPSNGSS
ESHKYDKNRA EDELCASYGM EERGILRDWN EEYQCCRELP ATTLKEKIVR ARVMYKIVTE
FVEAATQGAM AIVEGHIPPI NPMDEPNAHV YVFNNIFFSL PVDGKSSGKD ATNQNDEGGY
SAANRDLQGV KALNEADIAG LYTLATAVVD YLGIRVIAQS LIPGILQGEA ASKLIYGSVD
GGKTIAFNPK MHDLMLKAST KLHLAEREIQ PLGPESPETG SDQTSKAKSS SNNENEEINK
GQAGTDIVKL CGPVEAKGIL GSDGRMYALD LVRITPKDST YYEPQPLSNE NADGLHFQRE
DETYVALLRP ELINLYVLWR RNQIRRANRD ANNKSKELNS KASDNNNTLK KQIENSEEAP
TENADEPALK PEKVPSTSES TKDVSLVSTK EDESAPIQFN PNVFMKYDAC VDKEQVARDE
SLARDAADYL QRVVLPAFVA DLRRGSISPA DGYSLAELMH SCGINMRYLG RLASLIAKSE
DSPTNNTAYL SELLEAEMVA RATKHLLGNI LTSNPDVRAA LGQALLCILN GIFGGCMDAH
SNTIDQSEEL KLTQAQKNTG SSQTNPAAYA NGVGKHPSGQ SAQQLDPSSV WTKLKTHIKK
SFDYELFIWG SHSNAKVSKR VYPHVLLRRI CQRTGLRVCS RDYDFTIDAP FTIADITGVV
PIVKDSLPNH PLPLAKQLLE RGRFYLSTGS LASAYELLQE ASALLFQVCG AAHEDAALCS
SSLATVLYHA GDVAGAIAQQ QRALVLYTQL NGVDYHDTVF AHANLALFLH ANNQSDLAAL
HMRRSIYLLE LCAGANSPEL GSLYFKLGMI CQDAGHLTLA LECHQESLRR GNLDSLQSAT
TYHQMALACA LMGDFREALV HEKKVYSIYK EIFGEKDTHT LDSAKYMTRF TEKAVEGAKG
RREVDAAAAA DAIANQLLQE LEQGATTSKK KKSKKGKQAA TKC
//
