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Database: UniProt
Entry: A8N682_COPC7
LinkDB: A8N682_COPC7
Original site: A8N682_COPC7 
ID   A8N682_COPC7            Unreviewed;      1089 AA.
AC   A8N682;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 2.
DT   24-JAN-2024, entry version 98.
DE   SubName: Full=mRNA export factor elf1 {ECO:0000313|EMBL:EAU91504.2};
GN   ORFNames=CC1G_01993 {ECO:0000313|EMBL:EAU91504.2};
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU91504.2, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU91504.2, ECO:0000313|Proteomes:UP000001861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC   {ECO:0000313|Proteomes:UP000001861};
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:EAU91504.2}.
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DR   EMBL; AACS02000003; EAU91504.2; -; Genomic_DNA.
DR   RefSeq; XP_001830357.2; XM_001830305.2.
DR   AlphaFoldDB; A8N682; -.
DR   STRING; 240176.A8N682; -.
DR   GeneID; 6006797; -.
DR   KEGG; cci:CC1G_01993; -.
DR   VEuPathDB; FungiDB:CC1G_01993; -.
DR   eggNOG; KOG0062; Eukaryota.
DR   eggNOG; KOG1242; Eukaryota.
DR   HOGENOM; CLU_002848_0_1_1; -.
DR   InParanoid; A8N682; -.
DR   OMA; EDHRKFG; -.
DR   OrthoDB; 49929at2759; -.
DR   Proteomes; UP000001861; 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; IPR023779; Chromodomain_CS.
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   InterPro; IPR034085; TOG.
DR   PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 1; 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; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   PROSITE; PS00598; CHROMO_1; 1.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   REPEAT          88..123
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   DOMAIN          443..675
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          701..1017
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          830..891
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          1008..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1037
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1089
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  119400 MW;  030337D014B48419 CRC64;
     MADNDFPALF EALKTAPTAP DARAAADRLA RQILKEGPQS MADANVISTL HSFATNKKSG
     YERESAAMAF HSLATVIGAP GVPLLLPSLP VLYDLLMDKG DVVRSAASAA IKSILKLCPP
     ESVPVVFRQL ETILDTAKWR SKVGVLDGLK SFVASSRDVV ASELGKVLPH VEKAMHDTKS
     EVSSAATKCA TALCTTLANP DLTAHIPALV KCMAEPGSVP ACIKSLSNTT FVAEVKAPAL
     AVLVPLLQRA LNDRSMEVQR RTVIVIDNLV KLVRDPRVAA TYLSPLLDGV EKIAHGASFP
     EVRAFGQSAL ETLLKSGASA SGPPPEHRDI ETEIKDVLVA LRTLLPEELR SPSPNSPNAP
     SEVKYSLLES SLKFAASLAA DLVHDRRFTD QNAWNRCIGV YMSLWIEKPQ AEAFAEAARA
     HFHAIDQEKH KVVTGASSEE GELLCDTLFS LAYGALLLLS HTTLRLFRGR RYGILGANGS
     GKSTLMRQLR DGKVENFPPP SQVKCVMVEH SLQGEDTSLN VIDFIASGVS RLVVSAVKLA
     NGSADPQLTG VSRSEIQKQL SDVGFDEERQ REIVGGLSGG WKMKLELARA MLYKADLLLL
     DEPTNHLDRA SVKWLEDWLL AQKQVTCLIV SHDSGFLDNV TSDIIHYEQK KLVYYPGNLS
     AFVAKRPEAK SYYTLEASSV KFSFPPPGSL MGVRSNTRAI LKLQNCTFTY PGRDKPSLYD
     VSCALSLSSR VGVVGPNGAG KSTMIKLITG ETTPQTGTVY KHPALRVGYV SQHATHHIER
     HLEKTPIQYI QWRFQDGHDR ELLEKSTRVL TDEDKKLLDQ EWVGKDGSKR KLELIMGRQK
     LKKSLQYEIK WRGLDHRFNT WVPREELLKK GFSKIVQQFD DLESSREGAG ARETSTHLVR
     KHLEDIGLDG DIAQYNEISG LSGGQKIKLV IAACLWNNPQ ICVLDEPSNF LDREALGGLA
     VAIKNWTGAV VIISHNHEFV SSLCPEIWNV ENGRMVQQGK TAVVEDFNEK AGRSGTNTPA
     RSRLQTPAAS TAGTPAGSGA ENAAEARPVV KKKKKLTRNQ IKERDERRRL RLLRWLNEGG
     PKPEDTDSD
//
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