ID A0A0A2L6N7_PENIT Unreviewed; 1113 AA.
AC A0A0A2L6N7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Translation elongation/initiation factor/Ribosomal, beta-barrel {ECO:0000313|EMBL:KGO75747.1};
GN ORFNames=PITC_029940 {ECO:0000313|EMBL:KGO75747.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO75747.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO75747.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO75747.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO75747.1}.
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DR EMBL; JQGA01000442; KGO75747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L6N7; -.
DR STRING; 40296.A0A0A2L6N7; -.
DR HOGENOM; CLU_002794_3_1_1; -.
DR OMA; FARCDIQ; -.
DR OrthoDB; 166721at2759; -.
DR PhylomeDB; A0A0A2L6N7; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000313|EMBL:KGO75747.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:KGO75747.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 10..293
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 206..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 206..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 123329 MW; 8D93055F4F48F32E CRC64;
MPVVNVDQLI RLQRQPEDIR NDHGKTSLTD SLIATNGIIS PKLAGKIRYL DSRPDEQLRG
ITMESSAISL FFSMLRRPSP DAEPVPKEYL INLIDSPGHI DFSSEVSTAS RLCDGAVVLV
DAVEGVCSQT VTVLRQTWVE QLKPILVINK MDRLVTELKM SPAEAFSHLS RLLEQVNAVI
GSFYQGERME EDLQWRERME DRLNAAAARD QDNKKSSADD ESAQSIAEVT EFEERDDEDL
YFAPEKNNVI FCSAVDGWAF TIRQFAAIYE RKLGIKRTVL EKVLWGDYYL DPKTKRVLGV
KHLKGRALKP MFVQLVLDSI WAAYQATTGG DKGKGDPVLL EKITKSLNIN IPVHVLRGRD
PRNIMNTLFS QWLPLSTALL VSVIEYLPSP PAAQAARLPE MIKTSPGAAF IADDIKTAMV
DFKTGPEQPV VAYVSKMVAI PESEILSNKK RSEGAMTAAE AMELARRKRE EIAKMQAEAR
SKGQEDDFER MTSIFETTSL ITETTEEPEE PVEKDDPDHL IGFARLYSGT LSVGDEIYVL
PPKFSPAHPH ASPEPKKVIV TDLYLMMGRA LEPLKSVPAG VVFGIGGLAG HVLKTGTLCS
RLDGSINLAG VSLSMPPIVR VALEPVNPAD LSKLVTGLRL LEQSDPCAQY EVLPSGEHVI
LTAGELHLER CVTDLRERFA RCEIQTGEAI VPYRETIVHG PEMAAPKNPD LGRGAVLTVS
ASKQMTLRLR VVPMPEAVTE FLTKQVGTIK QLQLEKRSET EGKTETENAA EAAVDGTGEA
PEGHILSKQE FREGLDKLFN EEVKEDKELW KNVVNRITAF GPRRVGPNIL VDATAVNTCE
KFLVDDTKQQ IDGDNHQALL VRDFNDKIAY AFQLATGQGP LCQEPMQGVA VFLEDLSVQS
SAGDELDMGR LTGESIRLVR EGISAGFLDW SPRIMLAMYS CEIQATSKHS VLFLSLCIHI
TQSTFASSYK PCAKTNSQLT HHLHPPKAEV LGRVYAVITR RRGRILSEIM KEGTPFFTIL
ALLPVAESFG FAEEIRKRTS GAAQPQLIFA GFEALDEDPF WVPATEEELE DLGELADKQN
VAKRYMDAVR NRKGLVVQGR KLIDAEKQKT LKK
//
