ID A8N1J6_COPC7 Unreviewed; 444 AA.
AC A8N1J6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 09-JAN-2013, entry version 33.
DE RecName: Full=Elongation factor Tu;
GN ORFNames=CC1G_06762;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC
OS 9003) (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC Agaricomycetes; Agaricomycetidae; Agaricales; Psathyrellaceae;
OC Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W.,
RA Borodovsky M., Burns C., Canbaeck B., Casselton L.A., Cheng C.K.,
RA Deng J., Dietrich F.S., Fargo D.C., Farman M.L., Gathman A.C.,
RA Goldberg J., Guigo R., Hoegger P.J., Hooker J.B., Huggins A.,
RA James T.Y., Kamada T., Kilaru S., Kodira C., Kuees U., Kupfer D.,
RA Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J., Mackey A.J.,
RA Manning G., Martin F., Muraguchi H., Natvig D.O., Palmerini H.,
RA 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 -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC aminoacyl-tRNA to the A-site of ribosomes during protein
CC biosynthesis (By similarity).
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-Tu/EF-1A subfamily.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data.
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DR EMBL; AACS02000001; EAU93042.2; -; Genomic_DNA.
DR RefSeq; XP_001828776.2; XM_001828724.2.
DR ProteinModelPortal; A8N1J6; -.
DR GeneID; 6005202; -.
DR KEGG; cci:CC1G_06762; -.
DR KO; K02358; -.
DR OrthoDB; EOG42RHGS; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR HAMAP; MF_00118_B; EF_Tu_B; 1; -.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR PANTHER; PTHR23115:SF31; PTHR23115:SF31; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; Elong_init_C; 1.
DR SUPFAM; SSF50447; Translat_factor; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 3: Inferred from homology;
KW Complete proteome; Elongation factor; GTP-binding; Nucleotide-binding;
KW Reference proteome.
SQ SEQUENCE 444 AA; 48866 MW; CB418BB9017561F9 CRC64;
MLSLANCKAA SQAFACARLS LRSACQRNRV LPTYPSSGFA LRRGYAEVFQ RNKPHMNIGT
IGHVDHGKTT LTAAITKVLS SQGGAKFTDY NQIDKAPEEK ARGITINSSH VEYESDSRHY
GHIDCPGHAD YIKNMITGAA QMDGAIIVVS ATDGQMPQTR EHLLLARQVG IKRLVVWINK
VDQISDPEML ELVDMEMRDL LSTYNFDGEN TPIIMGSALA ALEGRDDKIG ESKIRELVKA
CDEWLELPVR DLEKPFLMPV EDVFSISGRG TVATGRVERG VATKGTDVEI IGFGANLKTT
LTGIEMFHKE LDRAEAGDNM GALLRGIKRE QIRRGQVLAA PGSVKSAKKF LAQIYVLTKE
EGGRYTPFMQ NYRPQCFVRT ADITVSLSFP EGTPDAAEKM VMPGDNVEMV CDLVFDVALE
EGTRFTLREA NKTIGTGIVT KIFE
//
