RLI1_CHATD
ID RLI1_CHATD Reviewed; 611 AA.
AC G0SEV9;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Translation initiation factor RLI1;
DE AltName: Full=ATP-binding cassette sub-family E member RLI1;
GN Name=RLI1; ORFNames=CTHT_0059880;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- FUNCTION: Component of the multifactor complex (MFC) involved in
CC translation initiation. Required for the binding of MFC to the 40S
CC ribosome. Required for the processing and nuclear export of the 60S and
CC 40S ribosomal subunits. {ECO:0000250|UniProtKB:Q03195}.
CC -!- SUBUNIT: Component of the multifactor complex (MFC). The complex
CC associates with pre-initiation complexes.
CC {ECO:0000250|UniProtKB:Q03195}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03195}. Nucleus
CC {ECO:0000250|UniProtKB:Q03195}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:Q03195}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGS17975.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GL988046; EGS17975.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006696306.1; XM_006696243.1.
DR AlphaFoldDB; G0SEV9; -.
DR SMR; G0SEV9; -.
DR STRING; 759272.G0SEV9; -.
DR EnsemblFungi; EGS17975; EGS17975; CTHT_0059880.
DR GeneID; 18260026; -.
DR KEGG; cthr:CTHT_0059880; -.
DR eggNOG; KOG0063; Eukaryota.
DR HOGENOM; CLU_017344_4_1_1; -.
DR OrthoDB; 359213at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:EnsemblFungi.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0045727; P:positive regulation of translation; IEA:EnsemblFungi.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IEA:EnsemblFungi.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0032790; P:ribosome disassembly; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013283; RLI1.
DR InterPro; IPR034348; RLI_dom_1.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR PANTHER; PTHR19248; PTHR19248; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF04068; RLI; 1.
DR PRINTS; PR01868; ABCEFAMILY.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Cytoplasm; Initiation factor; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Nucleus; Protein biosynthesis;
KW Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW Transport.
FT CHAIN 1..611
FT /note="Translation initiation factor RLI1"
FT /id="PRO_0000435814"
FT DOMAIN 7..31
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 46..75
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 77..318
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 345..565
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 382..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 611 AA; 69009 MW; 17441F78E35A63FD CRC64;
MADKLTRVAI VNSDKCKPKK CRQECKKSCP VVRSGKLCIE VTPESRIAFI SEQLCIGCGI
CPKRCPFGAI TIINLPTNLE SMITHRYAAN SFKLHRLPMP RPGSVLGLVG TNGIGKSTAL
KILSGKLKPN LGRYDNPPDW EEVIKYFRGS ELQNYFTKIL EDDLRAVVKP QYVDQIPKAV
RTPDKTVKFL IESRKSMDNL DEVLDTLELR HIYDRDVTHL SGGELQRFAI GTVCVQKADV
YMFDEPSSYL DVKQRLAAAR IIRSLLRPDD YVIVVEHDLS VLDYLSDYVC VLYGQPAVYG
VVTLPHSVRE GINIFLDGHI PTENLRFREE SLTFRMVEGT EDFVAEKSRA FKYPAMEKTL
GNFKLRVDAG SFSDSEIIVM MGENGTGKTT FCRLLAGVLK PDGTTRVPEM RISMKPQTIT
PKFEGTVRQL FFKKIKAAFL SPQFQTDVVK PLKLDDFIDQ EVKNLSGGEL QRVAIVLALG
IPADIYVIDE PSAYLDSEQR IVASRVIKRF IMHAKKTAFI VEHDFIMATY LADRVIVFDG
KPGIDAHANK PESLLTGCNT FLKNLDVTFR RDPTNFRPRI NKLNSQLDQE QKLSGNYFFL
EEGPDKEKER S
