ID F0UVC4_AJEC8 Unreviewed; 1113 AA.
AC F0UVC4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Elongation factor 3 {ECO:0000313|EMBL:EGC49851.1};
GN ORFNames=HCEG_09066 {ECO:0000313|EMBL:EGC49851.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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DR EMBL; DS990644; EGC49851.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UVC4; -.
DR STRING; 544711.F0UVC4; -.
DR VEuPathDB; FungiDB:I7I53_06136; -.
DR HOGENOM; CLU_002848_0_1_1; -.
DR OMA; EDHRKFG; -.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Elongation factor {ECO:0000313|EMBL:EGC49851.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EGC49851.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 477..694
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 721..1038
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1056..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 122368 MW; 15DD43A0EA55A968 CRC64;
MSSAPLVIPK TPSSVPPSEE EVASLMNTIL NADKSQESLD ASYALTNLLI QSVGFRGLHG
YGLLRGIQKA AVDKKSGAKR ESAMLILGAL FERFPREQPL SEVIFLIEDG GLLSLALDAL
GDKGAVVREA AKYAVDALFA CLKVESLVTA FAPALSAYLS KPTAKWQGAV EAYRLLEKVA
EKTQAGSDTK EESLQKDLLR DSVGKCLKDL IPIVESGMHD MKNEVSKQAV KTMTALTTVL
YNDDVAPRIP LLIKAMENPD AQILQKAIHA LSQTTFVAIV TSPVLALLTP LLERSLNTPT
TPQEVLRQTV VVVENLTKLV HDPNEARTFL PKLKPGVQGV KDRASLPEVR ELATRALNVI
QKAMGDDSSN LANGAVAQVT TDEVLKVLEQ QVKAHGGLVR KEDEPFWAIT KTYISEMVRD
DVNSRLLQRI PLCIGPYLSQ LVKEGQEGVI ASAVHAHFIE EDKRKYGAPV QEDTDEVEIV
NADFSLAYGG MLLLSHTNLR LLKGHRYGLC GRNGAGKSTL MRSIAEGKLE GFPPKDVLKT
CFVEHNQGED ADLSILEFVA KDPELAASGK KRISEVLSEV GFTAGPGGRQ QQKVGSLSGG
WKMKLALARA MLMGADVLLL DEPTNHLDVA NVKWLQEYLK KHTEITSLIV SHDSGFLDEV
CTDIYHYEGK KLVWYKGNLA AFVKVKPEAK SYYTLSSSNV QFKFPPPGIL TGVKSQTRAI
LRMTNVTYTY PGNSKPSLID ASCSLTLSSR TAIIGGNGAG KSTFIKLLTG ELIPQSGKVE
KHPNLRIGYI KQHALEHVEM HMEKTPNQYL QWRYQNGDDR EVLMKQTRIL TEEDRIQMEK
TIDIGDGRGP RRIEALIGRQ KLKKTFQYEV KWVGMLPKHN SFISRETLLK EGFQKLVQEY
DDHEASREGL GYRVLEPKVI SKHFEDVGLD PEIANHNQIS GLSGGQKVKV VLAGAMWNNP
HLLVLDEPTN FLDRDSLGGL AVAIRDYKGG VVMISHNEEF VGALCPEQWH VENGRMTHKG
HVSLSLDRFE DSSRGPSTVA SSVVSSTVAS AAASAANSGA EDAGGELKFK AKKKKKLTRA
QMKEREVRRR LRHIEWLNSP KGTPHPPDTD DEA
//
