ID I1BR13_RHIO9 Unreviewed; 1039 AA.
AC I1BR13;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Elongation factor 3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=RO3G_03347 {ECO:0000313|EMBL:EIE78643.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE78643.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE78643.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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}.
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DR EMBL; CH476733; EIE78643.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BR13; -.
DR STRING; 246409.I1BR13; -.
DR VEuPathDB; FungiDB:RO3G_03347; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR InParanoid; I1BR13; -.
DR OMA; EDHRKFG; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000009138; 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 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR034085; TOG.
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 SMART; SM01349; TOG; 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; PS50013; CHROMO_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT DOMAIN 444..657
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 684..999
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 812..873
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 997..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 115899 MW; ADC414D6D08AF07B CRC64;
MMVSAANEQA VLVNDLLSKI NTAPTSEEVE QAAQDLAKTV QEKGFIMIKQ YKILDQLLAS
VKNKKSGLER EGGLIGFNAM EEVLRHEIEP LMIQHLATFL DLYADKGGVV QEAAQTASRT
LVDMIPPEAT KVLLPALLEG MGHNSSSSKK WQTKIGALKL LERFTERAPD QIGECLPEII
PAVSDCLSDT KKEVAAAAEK AMMKVCSVGG NPDIHRHLKD LVLCMGNPTR VPQTIEKLAQ
TTFVAEVNGP TLAIMVPLLT RALNERSTTL LRQTVVITDN LCKLVRDPRT AAQFLPQLYP
GIERQADTAA FPEIRVLANK AKDTLIAAGG HNEKTDNIST FVTVEEATTA VKTAATKVQG
FLDSFFAPYL SYVGTIAADF ARQEMFIKEN WLKIFTPYLK AFLMKSDIPT VVDSVYDQVH
KLFKERNKDA DDSAIDEQEG EEICHVDDFS LAYGTRLLLN HTRLKLHRGQ RYGLCGENGA
GKSTLMKAIH NGKVEGFPSQ DEVRTALVDY NSQAADTSLK VVDYVAADEL LKNIPRETIE
KSLRDVGFDD ARLDISVSGL SGGWKMKLEL ARAILSKADI LLLDEPTNHL DVDNIKWLED
YLNAQSQVTC LIVSHDSGFL DNVCTKILHY NNKKLRLYHG NLSAFVDVYP AARTYYTLDA
STVEFTFPKP SVLQGVRSNT KAILKMTDCT FTYPGNKQPS LYNASASLSL SSRVAVVGPN
GAGKSTMIKL LTGETIPQTG TVWRHPALRI GYVAQHAFHH LNQHLEKTPT DYLQWRYSTG
EDKEVAEKET RAWSQDEIAQ MEKPITVDGE QRLIEALLGR TKFKKTFQYE IKWKNKLHKF
NTWISREKLL ELGFQKLVQQ FDDKEASREG LLYRELSMPT IRQHFADIGL DPDIAQYTKM
SALSGGQKVK VVIAAAMWNN CHMLVLDEPT NFLDREALGG LATAIKKWEG AVVMISHSNE
FVSALCPESW KLIGGKLYKE GQSAVDDESK IDEAKVKAKL SKKKKKTRNE LKAQEERRRA
RHLKWIIEGG VKEPDTESD
//
