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Database: UniProt
Entry: S3C3J6_OPHP1
LinkDB: S3C3J6_OPHP1
Original site: S3C3J6_OPHP1 
ID   S3C3J6_OPHP1            Unreviewed;      1125 AA.
AC   S3C3J6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Elongation factor 3 {ECO:0000313|EMBL:EPE08094.1};
GN   ORFNames=F503_00877 {ECO:0000313|EMBL:EPE08094.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE08094.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE08094.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE08094.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA   Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT   a comparison with the bark beetle-associated pine pathogen Grosmannia
RT   clavigera.";
RL   BMC Genomics 14:373-373(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}.
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DR   EMBL; KE148149; EPE08094.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3C3J6; -.
DR   STRING; 1262450.S3C3J6; -.
DR   VEuPathDB; FungiDB:F503_00877; -.
DR   eggNOG; KOG0062; Eukaryota.
DR   eggNOG; KOG1242; Eukaryota.
DR   HOGENOM; CLU_002848_0_1_1; -.
DR   OMA; EDHRKFG; -.
DR   OrthoDB; 49929at2759; -.
DR   Proteomes; UP000016923; 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; 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; 3.
DR   Pfam; PF00385; Chromo; 1.
DR   SMART; SM00382; AAA; 2.
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; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Elongation factor {ECO:0000313|EMBL:EPE08094.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:EPE08094.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   REPEAT          209..247
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   DOMAIN          475..692
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          720..1037
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1022..1125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1046
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1071
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1091..1106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1125 AA;  122749 MW;  5216863ABCB9ED6F CRC64;
     MDGTAIAHRP AKDGKAEVAA VLSAVFSAST SNASVEAAYQ LCDLLLNNPA AGFRGLAEYG
     VLAEIKKAAA DKKSGLRRES AQNLLGALFE RFPPKQAASE VAFLLQDGGM VAVALDALAD
     KGTVVRNAAQ YGLDALLGHL RAESLVVGLL PALVTYLNKR TGKWQGTVGA LKLLQRMADK
     AKMEIGSTKE EAIEKEVLRD LMGSKLASLI PIVEAMMSDL KTEVEKQAVI TMTSITSLLS
     NDDVAPRVPL LIDTMQHPSV QSLQKAIHAL AHTTFVAIVT SPVLALLTPF LERSLNTPTT
     AQEVLRQTVV ITENLTKLVH DPIEARTFLP KLQPGVKAVR DRAALPEVRD MAARALSVMD
     IAMATDKEGK NVAVERVSAD DVAVQLYSEV QKAGGLLPAD ADNFKTISPY ISSMVAEDAN
     ARYINRIHTS VAPYLGPLLK NSAAAETIAA AVQQYYLEED QRKFGVPEKE DDGEVEIVNA
     DFSLGYGGML LLSHTNMRLL KGHRYGLVGR NGAGKSTLMR SIAGGKLEGF PPQDVLRTCY
     VEHNQGEDAE ISILDFVAKD PTIAQEGRER ISAVLLEFGF TDGPDGRQAQ KVGSLSGGWK
     MKLALARAML QKADVLLLDE PTNHLDVANI AWLQTYLKTN TEITSLIVSH DSGFLDEVTT
     DIYHYEPGKK LAHYKGNLAT FVSNHPEAKS YYTLSDSMVQ FKFPPPGILS GIKSQTRAIV
     RMSNVTFAYP GAAAPSLSDA SCQLTLSSRV AVIGPNGAGK STLIKLLTGE VIPTIGKVEK
     HPNLRIGYIK QHALEHVEMH LEKTPNQYLQ WRYQFGDDRE VHMKQTRQMS EADRAQMDKI
     VELGEGMGQR QIEALVGRQK YKKTFQYEVK WKLMLPKENT MVTRETLLAL GFDKLIQEFD
     DHESSREGLS FRELQPAIIS KHFEDLGLDP EIANHNEIGG LSGGQKVKVV IAGAMWNNPH
     LLVLDEPTNF LDRDSLGGLA VAIRDFKGGV VMISHNEEFV GALSNEQWHV VAGRMTHRGH
     AAVSNDRFED SSRPGSGINT PGVSTPGIMS PGGATPAMSS MQSSAVNSGV EDNATGDLKF
     KAKKKRKKTK KDLKEQENRR RQREIVWLNS PKGTPKPLDT DDEEE
//
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