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Database: UniProt
Entry: A0A0D2BIR4_9EURO
LinkDB: A0A0D2BIR4_9EURO
Original site: A0A0D2BIR4_9EURO 
ID   A0A0D2BIR4_9EURO        Unreviewed;       604 AA.
AC   A0A0D2BIR4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   SubName: Full=Translation initiation factor RLI1 {ECO:0000313|EMBL:KIW52261.1};
GN   ORFNames=PV05_07913 {ECO:0000313|EMBL:KIW52261.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW52261.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW52261.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW52261.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KN847321; KIW52261.1; -; Genomic_DNA.
DR   RefSeq; XP_013312845.1; XM_013457391.1.
DR   AlphaFoldDB; A0A0D2BIR4; -.
DR   STRING; 348802.A0A0D2BIR4; -.
DR   GeneID; 25329821; -.
DR   HOGENOM; CLU_017344_4_1_1; -.
DR   OrthoDB; 1110105at2759; -.
DR   Proteomes; UP000054342; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF16; ATP-BINDING CASSETTE SUB-FAMILY E MEMBER 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; 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; 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   Initiation factor {ECO:0000313|EMBL:KIW52261.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:KIW52261.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          46..75
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          70..318
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          327..565
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   604 AA;  68199 MW;  E3E3166745974868 CRC64;
     MADKLTRIAI VNSDKCKPKK CRQECKKSCP VVRTGKLCIE VTPESKIAYI SERLCIGCGI
     CPKKCPFGAI HIINLPTNLE TQVTHRYSAN SFKLHRLPMP RPGQVLGLVG TNGIGKSTAL
     KILSGKLKPN LGRYDNPPDW EEILKYFRGS ELQNYFTKVL EDDLKAIVKP QYVDQLPRAI
     KGPVKTVKPL IEAKSEMGNL KHIMDVLELN AVQDREISLL SGGELQRFAI ALVCVQKADV
     YMFDEPSSYL DVKQRLSAAK TIRELLRPDD YVIVVEHDLS VLDYLSDFIC VLYGRPAVYG
     VVTLPASVRE GINIFLDGHI PTENLRFREE SLTFRIAEAG EEYLLDKARG FEYPSMEKTL
     GNFHLKINSG TFTDSEIIVM MGENGTGKTT FCKMLAGIEK PDGTQKVPAM NISMKPQKIT
     PKFQGTVRQL FFKRIKASFL NPQFQTDVYK PLKLDDFIDQ EVQNLSGGEL QRVAIVLALG
     LPADIYLIDE PSAYLDSEQR IIAARVIKRF IMHSKKTAFI VEHDFIMATY LADRVIVFDG
     KPSVDARANT PESLLTGCNK FLKNLDVTFR RDPNSYRPRI NKYQSQMDQE QKLAGNYFFL
     EDES
//
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