ID A0A0A2L3P7_PENIT Unreviewed; 413 AA.
AC A0A0A2L3P7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Translation initiation factor IF2/IF5, zinc-binding {ECO:0000313|EMBL:KGO73776.1};
GN ORFNames=PITC_034920 {ECO:0000313|EMBL:KGO73776.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73776.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO73776.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73776.1,
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 -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC {ECO:0000256|ARBA:ARBA00010397}.
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:KGO73776.1}.
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DR EMBL; JQGA01000771; KGO73776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L3P7; -.
DR STRING; 40296.A0A0A2L3P7; -.
DR HOGENOM; CLU_026663_1_0_1; -.
DR OMA; YRYKMEK; -.
DR OrthoDB; 5475947at2759; -.
DR PhylomeDB; A0A0A2L3P7; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd11561; W2_eIF5; 1.
DR Gene3D; 1.25.40.180; -; 1.
DR Gene3D; 2.20.25.350; -; 1.
DR Gene3D; 3.30.30.170; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; EUKARYOTIC TRANSLATION INITIATION FACTOR; 1.
DR PANTHER; PTHR23001:SF7; EUKARYOTIC TRANSLATION INITIATION FACTOR 5; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF100966; Translation initiation factor 2 beta, aIF2beta, N-terminal domain; 1.
DR SUPFAM; SSF75689; Zinc-binding domain of translation initiation factor 2 beta; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:KGO73776.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 247..409
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 141..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 45790 MW; CCBCBA905B3BC58F CRC64;
MATVNIRRDI TDPFYRYKME KLQAKVEGKG NGIKTVVVNL NSVAQSLSRP PAYLIKYFGF
ELGAQANAKP SDDRWIINGS HDAPKLQDYL DGFISKFVLC KKCKNPETDV SIKDEKITLD
CKACGQRSDV DPRLKLSTFI VRNNPKGGKK EKKKSRRERE KEKAANGEDA SPGDSNNSEN
GEDGDYALEA NSDDEVTRQA QAIEAEAEIK DDEWAVDVSE EAVKARAKDL PSDLKRALVI
EDGDDEGADG ASSYEQLGSW IVDTAAEKGG VTKVTDVEIY MKAKEFGIES KHKTCAVLAQ
SIFDEKIAKQ IEGRAGLLKK LITSDRHEKA FLGGTERFVG QDHPELVAQV PAILLGYYQN
DLVSEETLKA WGAKTSKKYV DISTSKKIHK AAKPFIEWLE NAESDEESEE DSE
//
