ID A0A1E3I2G4_9TREE Unreviewed; 1095 AA.
AC A0A1E3I2G4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Elongation factor 3 {ECO:0000313|EMBL:ODN82545.1};
GN ORFNames=L203_05354 {ECO:0000313|EMBL:ODN82545.1};
OS Cryptococcus depauperatus CBS 7841.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN82545.1, ECO:0000313|Proteomes:UP000094043};
RN [1] {ECO:0000313|EMBL:ODN82545.1, ECO:0000313|Proteomes:UP000094043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN82545.1,
RC ECO:0000313|Proteomes:UP000094043};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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:ODN82545.1}.
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DR EMBL; AWGK01000025; ODN82545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3I2G4; -.
DR STRING; 1295531.A0A1E3I2G4; -.
DR VEuPathDB; FungiDB:L203_05354; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000094043; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd03221; ABCF_EF-3; 1.
DR CDD; cd18626; CD_eEF3; 1.
DR Gene3D; 2.40.50.990; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR015688; eEF3_ABC2_chromodomain-like.
DR InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 3; 1.
DR PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Elongation factor {ECO:0000313|EMBL:ODN82545.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:ODN82545.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094043};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT REPEAT 99..136
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 455..671
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 697..1013
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 826..887
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1007..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 118810 MW; 8BBBF0C55AC4B9B8 CRC64;
MPAAIPTLSA LPASSHLEEF TKLASAPSNV EAKSIADSIA LSLKKAPRSL NAIQDAKIVD
VVLVWASSKS GYEKESAAVL VERICRSFGT GVEGVFLPLI PALLNLAMDK GQPVRSAVNS
AMTSLIKATA PEGARKVFEV LACVLDETKG WRTKIATLKA MEGLVKPGAE DYVANELGTV
IPIVEHAMHD TKSEVSTAAQ KAATTLCSIL PNADVIKHID LLVSAMASPA AVPSTIKGLS
STTFVAEVNG PTLAVMVPLL TRALKERSTD TQRMTCVVIG NLVKLVRDPT VAARYLGPLF
GGVQQIAEGA AFPEIRAFAQ TALDILIGAG ASAVATPLPP RNIASSVTET LTVMVPHLAI
PDFPAHPSLP LSASLPNSPI IAHALEYQGN VVADLVDMRR WDASIWEGKG LGAFMKLLRG
AQEGAKATAG IRKAFMDIDK ARYAPAEEDD GSEGQLLCDI QFSLAYGGLL LLNHTNLKLR
RGRRYGICAA NGAGKSTLMK AIRDGKVEGF PPQDELRTIM VEHALQGEDT SMAIIEFVVA
DSKLAHRKRQ EIVDMLLSVG FSEEKQKDPV ASLSGGWKMK LELARAMLIG ADILLLDEPT
NHLDVQTVAW LEQYVCNLPD ITCMIVSHDS GFLDNVCTDI IHYEQKKLVY YPGNLSKFVE
KVPSAKSYYT LAATSIKFTF PPPGNLVGVR SNTRAILKLN NCTFTYPGAS KPSLKNVSCS
LSLSSRVGVV GPNGAGKSTL IKLLTGETVP QEGSVHKHPA LRVGYVAQHA FHHINQHLDK
TAVQYIQWRY QDGHDREMME KATRILTDED KEMMEKPIEG RNGELRKIEY ILGRQKLKKS
FQYEVKFKGY DHKYNAWIPR DVLIEKGFQK LVTQFDDLES SREGAGMRDT GANAVREVLE
AVGLDGDIAQ YNEMSGLSGG QKVKVVIAAS MFNRPQCLFL DEPTNFLDRE ALGGLAVAIK
EWGGAVCIIS HSTEFVSALC PEIWHVDHGE LTHQGKVALV EDAFDNPSMS NSRTASKAGT
PRTVPGTPGT ATPADSAANS GVDDVVDGLA RLMEKKKKKK KMTRNELKAQ EERRRLRKLN
WLTYGGTREP DTDEE
//
