RLI1_SCHPO
ID RLI1_SCHPO Reviewed; 593 AA.
AC O60102;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Translation initiation factor rli1;
DE AltName: Full=ATP-binding cassette sub-family E member rli1;
DE AltName: Full=RNase L inhibitor;
GN Name=rli1; ORFNames=SPBC14F5.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the multifactor complex (MFC). The complex
CC associates with pre-initiation complexes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA19324.1; -; Genomic_DNA.
DR PIR; T39452; T39452.
DR RefSeq; NP_596732.1; NM_001022658.2.
DR AlphaFoldDB; O60102; -.
DR SMR; O60102; -.
DR BioGRID; 276305; 2.
DR STRING; 4896.SPBC14F5.06.1; -.
DR iPTMnet; O60102; -.
DR MaxQB; O60102; -.
DR PaxDb; O60102; -.
DR PRIDE; O60102; -.
DR EnsemblFungi; SPBC14F5.06.1; SPBC14F5.06.1:pep; SPBC14F5.06.
DR GeneID; 2539753; -.
DR KEGG; spo:SPBC14F5.06; -.
DR PomBase; SPBC14F5.06; rli1.
DR VEuPathDB; FungiDB:SPBC14F5.06; -.
DR eggNOG; KOG0063; Eukaryota.
DR HOGENOM; CLU_017344_4_1_1; -.
DR InParanoid; O60102; -.
DR OMA; VCVQQAD; -.
DR PhylomeDB; O60102; -.
DR PRO; PR:O60102; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0051536; F:iron-sulfur cluster binding; ISM:PomBase.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; ISS:PomBase.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0002183; P:cytoplasmic translational initiation; ISO:PomBase.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:PomBase.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Initiation factor; Nucleotide-binding; Nucleus;
KW Protein biosynthesis; Reference proteome; Repeat; Ribosome biogenesis;
KW rRNA processing; Transport.
FT CHAIN 1..593
FT /note="Translation initiation factor rli1"
FT /id="PRO_0000316194"
FT DOMAIN 7..39
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 70..318
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 334..556
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 593 AA; 66590 MW; 20F2DBB5C02BB4D4 CRC64;
MSESLTRIAI VSEDKCRPKK CRQECRRSCP VVRTGKLCIE VNPTDRIAFI SETLCIGCGI
CVKKCPFGAI NIINLPTNLE SEVTHRYSAN SFKLHRLPTP RPGQVLGLVG TNGIGKSTAL
KILSGKMKPN LGRYDNPPDW AEVVKYFRGS ELQNFFTKVV EDNIKALIKP QYVDHIPRAI
KTGDKTVSGL IKARANNNNF EEVMDHTDLQ NLLNREVGHL SGGELQRFAI AAVATQKADV
YMFDEPSSYL DIKQRLKAGR VIRSLLATTN YVIVVEHDLS VLDYLSDFVC VLYGVPSMYG
VVTLPYSVRE GINIFLDGHI PTENLRFRSE ALTFRLADAS DEITADRTAE YNYPDHVIEQ
GDFKLTIKSG GFSDAEIIVL LGENGTGKTT FCKWMAKNSD LKISMKPQTI APKFQGTVRM
LFLKKIRAAF LNGKFQSEVC KPLSIDNIID QEVLNLSGGE LQRVAICLAL GMPADVYLID
EPSAYLDSEQ RIIASKVIRR FIVNSRKTAF IVEHDFIMAT YLADRVILFE GQPSRDARCN
PPQSLLTGMN TFLKNLDVTF RRDPNTLRPR INKFDSQMDQ EQKNAGNYFF LEN
