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Database: UniProt
Entry: A0A9W8M826_9FUNG
LinkDB: A0A9W8M826_9FUNG
Original site: A0A9W8M826_9FUNG 
ID   A0A9W8M826_9FUNG        Unreviewed;       600 AA.
AC   A0A9W8M826;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   RecName: Full=Translation initiation factor RLI1 {ECO:0000256|ARBA:ARBA00067238};
DE   AltName: Full=ATP-binding cassette sub-family E member RLI1 {ECO:0000256|ARBA:ARBA00082546};
GN   Name=RLI1 {ECO:0000313|EMBL:KAJ2866465.1};
GN   ORFNames=GGH94_001506 {ECO:0000313|EMBL:KAJ2866465.1};
OS   Coemansia aciculifera.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX   NCBI_TaxID=417176 {ECO:0000313|EMBL:KAJ2866465.1, ECO:0000313|Proteomes:UP001140074};
RN   [1] {ECO:0000313|EMBL:KAJ2866465.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RSA 476 {ECO:0000313|EMBL:KAJ2866465.1};
RA   Reynolds N.K., Stajich J.E., Barry K., Grigoriev I.V., Crous P.,
RA   Smith M.E.;
RT   "Phylogenomic reconstructions and comparative analyses of Kickxellomycotina
RT   fungi.";
RL   Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00056499}.
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:KAJ2866465.1}.
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DR   EMBL; JANBUY010000037; KAJ2866465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9W8M826; -.
DR   Proteomes; UP001140074; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-ARBA.
DR   CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR   FunFam; 3.40.50.300:FF:000144; ATP-binding cassette sub-family E member 1; 1.
DR   FunFam; 3.40.50.300:FF:000152; ATP-binding cassette, sub-family E, member 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; NF009945; PRK13409.1; 1.
DR   PANTHER; PTHR19248; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF04068; Fer4_RLI; 1.
DR   PRINTS; PR01868; ABCEFAMILY.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP001140074}.
FT   DOMAIN          46..75
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          70..315
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          344..563
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   600 AA;  67255 MW;  3B91AC8FA59A56FD CRC64;
     MSDSNSRIAI VNNDKCKPKK CKQECKRVCP VVKMGKQCIV AEVTSKIALI SEGLCIGCGM
     CVKRCPFGAI TIINLPANLE KETTHRYGAN SFKLHRLPMP RPGQVLGLVG ANGTGKSTAL
     KILAGRTKPN LGNFADPPEW TEIIRYFRGS ELQNYFTKIL EDDLKALIKP QSVDAIAKSV
     KMEVGVALDL KTQKDNLDYL IRELDLRDVM KRNVKDLSGG ELQRFAIAVT CVQKADVYMF
     DEPSSYLDVK QRLNAARVIR SLVESNNYVI AIEHDLAVLD YLSDFVCMLY GTPSVYGVVT
     MPFSVREGIN IFLSGMLPTE NMRFRKEELT FRMAEQAQEE EEIQRYRDYP YPTMTKTQGD
     FKLSVVGDMF SESEIIVLLG ENGTGKTTLI NLLAGNILTD KGEKLEDLKV SYKPQKIAPK
     FQGTVRMLMG KVIGDTFPKP TFQTQVAKPM QIDEILDNDV QNLSGGELQR VALVLALGKD
     ADVYLLDEPS AYLDSEQRIN ASKVIKRFIM GTKKTAFVVE HDFIMATYLA DRVIVMEGTP
     SVRATANAPQ SLLSGMNKFL KSLNITFRRD PTNYRPRINK LESAKDREQK STGNYFFLED
//
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