ID A0A179HGN2_PURLI Unreviewed; 1105 AA.
AC A0A179HGN2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Elongation factor 3 {ECO:0000313|EMBL:OAQ89576.1};
GN ORFNames=VFPFJ_05990 {ECO:0000313|EMBL:OAQ89576.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ89576.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ89576.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ89576.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-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:OAQ89576.1}.
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DR EMBL; LSBI01000005; OAQ89576.1; -; Genomic_DNA.
DR RefSeq; XP_018178295.1; XM_018323065.1.
DR AlphaFoldDB; A0A179HGN2; -.
DR STRING; 33203.A0A179HGN2; -.
DR GeneID; 28888114; -.
DR KEGG; plj:VFPFJ_05990; -.
DR OMA; EDHRKFG; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000078340; 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; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Elongation factor {ECO:0000313|EMBL:OAQ89576.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:OAQ89576.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078340};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT REPEAT 114..151
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REPEAT 213..251
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 474..691
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 719..1036
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 121897 MW; 5B6A21D61E364585 CRC64;
MPHPVSPPTM VSKDDPPPPS QEDVSAFVNT VFTAKTSGAS VDASYGLCDL LLNSVGVSGL
QQYGVLAEIK KAAADKKDGF RRESSQNLLG AIFERFPARQ HVSEVVFLVQ EDGLVPCALD
ALADKGAVVR EAAQYGLDAL LGNLSAEALV TGLLPVLVQY LSRKTGKWQG TVGAYKLLQK
MADKSQMAIG TTKEEAVEKD ILREAMGAKL AGLIPIVESG MHDLKAEVEK QAVQTMNSLT
TLLSNDDVAP RIPLLVETMQ HPSAQTLQKA IHALSMTTFV AIVTSPVLAL LTPFLERSLN
SPNTAQEVLR QTVVIVENLT KLVHDPIEAR TFLPKLTPGV KGVCDRASLP EVRELANRAL
ATMEKAMGND KDIVARTTAD DVGKVLDEQI KKHGGLAGHP DLYKVARPYI SDMVATDVNY
RFVKRISGRV APYLETLMRD SEAHQKVGDA IEQFYIEEDN RRYGVPEKED DGEVEIVNAD
FSLAYGGMLL LSHTNLRLLK GHRYGLCGRN GAGKSTLMRS IANGKLEGFP PQDVLRTCFV
EHNQGEDADI SILEFVSKDP TIADQGTERI SEVLSEFGFT AGPEGRQAQK VGSLSGGWKM
KLALARAMLQ KADVLLLDEP TNHLDVTNIA WLENYLKTHT EITSMIVSHD SGFLDNVTTD
IYHYEPNKKL ACYKGNLANF VTLRPEAKSY YTLSASNVQF KFPPPGILSG VKSQTRAIIR
MSNVSYTYPN APKPSLMEVS CQLSLSSRVA IIGPNGAGKS TLIKLLTGET IPTTGKVEKH
PNLRIGYIKQ HALEHVEMHL EKTPNQYLQW RYANGDDREV HMKQTRILSD KDREQMDKWV
DLKDGKAARQ IETLVGRQKY KKTFQYEVKW RNLLPKHNTM ISRETLSELG FDKLVQEFDD
HEASREGLGY RELLPKVISK HFEDLGLDPE IANHNEIGSL SGGQKVKVVI AGAMWNNPHL
LVLDEPTNFL DRDSLGGLAV AIREFKGGVI LISHNEEFVG ALCSEQWHVA DGRVALRGNT
AVSLDRFEDS RPGSGVTSTA ASSVVSSAVN SGVEDNADMK FKAKKKKKMT KKELKEREVR
RRLRHIEWLN SPKGTPHPPD TDDED
//
