ID R1ESV7_BOTPV Unreviewed; 1118 AA.
AC R1ESV7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Putative elongation factor 3 protein {ECO:0000313|EMBL:EOD50883.1};
GN ORFNames=UCRNP2_2334 {ECO:0000313|EMBL:EOD50883.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD50883.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB915925; EOD50883.1; -; Genomic_DNA.
DR RefSeq; XP_007581639.1; XM_007581577.1.
DR AlphaFoldDB; R1ESV7; -.
DR STRING; 1287680.R1ESV7; -.
DR KEGG; npa:UCRNP2_2334; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_002848_0_1_1; -.
DR OMA; EDHRKFG; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000013521; 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 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; 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; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Elongation factor {ECO:0000313|EMBL:EOD50883.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EOD50883.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT REPEAT 121..158
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 485..703
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 729..1046
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1061..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 122613 MW; BC373902950176B3 CRC64;
MPHHESPPMA AAVVAKTADP ENAVPPTADE VSQVLSACLA AKTSQASLDS AYALTGLLES
SVGFRGLKGY GILDEVKKAA ANKKDAVKKE GSMFILGALF ERLSASQPLS EVVFLLQEEN
LVPLCLDALA DKNTTIKESA QYALDALFKN LRSEALVDGL LPVLAKYLSK STGKWQGTVG
AFSLLTQMAD KAKMGMGSLE EEREKDVLRE AMGKKLASLI PIVEGGMHDL KADVAKQAVK
AMTSLSTLLQ NDDVTPKIPL LIESMKNPSA ASTQKAIHAL SMTTFVAVVT APVLAMLTPL
LERSLNNPST NQEVLRQTVV VVENLTKLVH DPVEARNFLP KLKPGVQGVK DRASLPEVRE
LATRAIEVIK HAMGEDADGT SPIERTTPEQ VGTVLDKEIA TNGGLLNYPG DADVWKIARS
YIAEMVAEDT NQRALERVVK SIEPYIRPLV NQGSSTTIAE NVHSYFVEED ERKYGKPIVE
DDGETEIVNA TFSLGYGGML LLSHTNLRLL KGHRYGLCGR NGAGKSTLMR SIAEGKLEGF
PPQDEVKTCF VEHNQGEDAD LSILEYISND PRFKDESKER ISEVLEEVGF TAGPNGRQSE
NVGSLSGGWK MKLALARAML MRADVFLLDE PTNHLDVANI AWLQDYLKNH TEITSLIVSH
DSGFLDEVCT DIYHYEQKKL VCYKGNLAEF VKQKPEAKSY YTLSNTQMQF KFPPPGILTG
VKSNTRAILR MTGCSYTYPG SSKASLNDVT CSLTLSSRVA IIGANGAGKS TLIKVLTGEV
IPQTGKVEKH PNLRIGYIKQ HALEHVEMHM EKTPNQYLQW RYANGDDREV LMKQTRILTD
EDKAQMDQEI DIGDGKGPKK IEALIGRQKY KKSFQYEVKW VGWLPKYNTM VSRETLLERG
YQKLIQEFDD HESSREGLGY RQLEPKVISK HFDDLGLDPE IANHNEIGGL SGGQKVKVVI
AGAMWNNPHL LVLDEPTNFL DRDSMGGLAA AIRDYKGGVV MISHNEEFVG ALCPEQWHVA
DGRVIQKGSL AVNAGAFEDS KPGSIASSAV PSTAASSAAP SAVNSEAEGG DMKFKAKKKK
KMTRAQLKER EVRRRLRHIE WLNSPKGTPH PPDTDDEA
//