ID Q5CQQ0_CRYPI Unreviewed; 1040 AA.
AC Q5CQQ0;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000256|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=cgd4_3770 {ECO:0000313|EMBL:EAK87744.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK87744.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK87744.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC 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_03002}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAK87744.1}.
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DR EMBL; AAEE01000008; EAK87744.1; -; Genomic_DNA.
DR RefSeq; XP_625952.1; XM_625952.1.
DR AlphaFoldDB; Q5CQQ0; -.
DR STRING; 353152.Q5CQQ0; -.
DR EnsemblProtists; EAK87744; EAK87744; cgd4_3770.
DR GeneID; 3372916; -.
DR KEGG; cpv:cgd4_3770; -.
DR VEuPathDB; CryptoDB:cgd4_3770; -.
DR InParanoid; Q5CQQ0; -.
DR OMA; FRCGLIK; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000006726; Chromosome 4.
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:InterPro.
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 HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR Pfam; PF05470; eIF-3c_N; 2.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000006726}.
FT DOMAIN 734..917
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 116323 MW; 894B2D32B62D14B0 CRC64;
MQGKFWAEGS ESSSMDSSNS ESESSSDSEM EMQAARRRQR EMNNSRWAID SDSDSSEDDR
RVVRGAKEKF HDELRMIIRR VNNHVKVSDF SSLSDEYDKL LKCMQKSQNA IKNYGIPKFF
ISVLVELEAF LDEKFRDKEA IKKLSKAKAT SFNTLRAKFR KSVEEYRDQM DDCKNNPLAY
QDDNLSDDDS DSNSYSDSDS DSDSDSDSSS SSSGSDSRSV SGSDSDGNGS GSDESSSDSD
SSSSSSSSEW SSYEDEYEDR HASALAKWGT RTKSVKKKES GKKANRQKQV KKDLQDTTVS
GGANNNIPSG DLLSFEGEVT VDMIVEKVGE IVAARGKKGT DRQEQIRLLK KAAEISRPLS
LQAYADVLTH LISAQFDTIT GAFHCITSGI WSEICDNINI LLDLVLLNNK DKRVYISGFQ
SFISSKDKKK KASGDSSGAG ANSGMDAHGN SLDGENANTD ENSSLGDIVD LKEQDKSTVT
FLVSFIERLD GESLKALQLT DVHSSEYKDR LVQSLHLLAL LWRCYKICEE RGYYDLVSSL
SVHLINQLHF KNDSLAIKVW EFVRQILEKT VNSSLSSEEL SANSDSSNTD CAGKIPDIPV
PKKFKPSELI TELVGNVYKY GDSKDKLRVL IQHVYNMALH DNYNEAVTLF QSIGVYDMAL
GSDVNIQILY NRSLVQLGLS AFRLGQISEA QQLLSEICMP NRNRELLAQG MSNMKSQERT
PEQERAEKRR LLPYHMHLSL EVIDCIYLIC SMLLEVPYLA YHKSLIMQNE ASNSHIKLRP
ISKQFRRLLE QYERQAITGP PESLRDTIIA ATRSLQLGKW RECRDYVFSL SIWDYNQEDL
QQTQERLELN IKQEALRTYL FTYGHLYSSY SVNNLIEMFQ LPREKIHSLL SKMMLKNELQ
ALWDQTGEFV LLNHKQASKI QNDSLIVADK LLQFVDCNES MISSKGNASG GKNPNVINNR
NSAGVGNPNN QGGIGPGSVQ GGGPNNTSNT NSSGTGNQSF NSNYYSRKTN SGQYNKHKNT
SSSSSSVPSS SSMNLRPIRV
//
