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Database: UniProt
Entry: A0A507BJK0_9PEZI
LinkDB: A0A507BJK0_9PEZI
Original site: A0A507BJK0_9PEZI 
ID   A0A507BJK0_9PEZI        Unreviewed;       509 AA.
AC   A0A507BJK0;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   18-JUN-2025, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:TPX19014.1};
GN   ORFNames=E0L32_011331 {ECO:0000313|EMBL:TPX19014.1};
OS   Thyridium curvatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Thyridiales; Thyridiaceae; Thyridium.
OX   NCBI_TaxID=1093900 {ECO:0000313|EMBL:TPX19014.1, ECO:0000313|Proteomes:UP000319257};
RN   [1] {ECO:0000313|EMBL:TPX19014.1, ECO:0000313|Proteomes:UP000319257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D216 {ECO:0000313|EMBL:TPX19014.1,
RC   ECO:0000313|Proteomes:UP000319257};
RA   Varaljay V.A., Lyon W.J., Crouch A.L., Drake C.E., Hollomon J.M.,
RA   Nadeau L.J., Nunn H.S., Stevenson B.S., Bojanowski C.L.,
RA   Crookes-Goodson W.J.;
RT   "Draft genome sequence of the filamentous fungus Phialemoniopsis curvata
RT   isolated from diesel fuel.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000256|ARBA:ARBA00004431}.
CC   -!- SIMILARITY: Belongs to the eIF-5A family. Hex1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00061629}.
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:TPX19014.1}.
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DR   EMBL; SKBQ01000103; TPX19014.1; -; Genomic_DNA.
DR   RefSeq; XP_031000725.1; XM_031134048.1.
DR   AlphaFoldDB; A0A507BJK0; -.
DR   STRING; 1093900.A0A507BJK0; -.
DR   GeneID; 41978778; -.
DR   InParanoid; A0A507BJK0; -.
DR   OrthoDB; 9975114at2759; -.
DR   Proteomes; UP000319257; Unassembled WGS sequence.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0045901; P:positive regulation of translational elongation; IEA:InterPro.
DR   GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR   CDD; cd04469; S1_Hex1; 1.
DR   FunFam; 2.40.50.140:FF:000229; Woronin body major protein; 1.
DR   FunFam; 2.30.30.30:FF:000033; Woronin body major protein HEX1; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR037318; Hex1_S1.
DR   InterPro; IPR001884; IF5A-like.
DR   InterPro; IPR048670; IF5A-like_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR020189; Transl_elong_IF5A_C.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11673; TRANSLATION INITIATION FACTOR 5A FAMILY MEMBER; 1.
DR   Pfam; PF01287; eIF-5a; 1.
DR   Pfam; PF21485; IF5A-like_N; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000319257}.
FT   DOMAIN          364..415
FT                   /note="Translation initiation factor 5A-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21485"
FT   DOMAIN          437..502
FT                   /note="Translation elongation factor IF5A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01287"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  58034 MW;  571CD0D9BBC6C3B3 CRC64;
     MIPALASRAS SSQQRQTSPQ PTALQQLSYF IPISSRLSRS STLSPLLSST QIQTQLHRQN
     SPLLPLPSGI KAEEELGFFF PFLPVDFFLG KEARGFFFVF LSNTSEARVP VPFSIFPSAY
     RESETEQTTT QSTHEELEIK LPHKAGREGQ YSSFSATADL PPRKEQSRYS EEEVRITREE
     DRYRRPGVRQ EYYREERRPS HASSSYSETH IETDRHSHHR DYSTPIDVAE REYRSRFQPN
     YREEVHVTGS TVDGPRYPSY HQESASRVDD TTVDPPTQRP VYHKDVKITE ETVEVPRYSN
     TPRQKSKMGY YDEDGHYHSF RHGIHKMADR MLHPEGHEKV EITEIRESRG PSRRASSEGG
     YVPNTVTIPC HHIRLGDIVI LQGRPCQVIR ISTSNATGQH RYLGVDLFTK QLHEESSFIT
     NPGPSVVVQT MLGPVFKQYR VLDMQDGTVV AMTESGDVKQ SLPVIDQSNL WSRLSKAFES
     GRGSVRVLVV SDHGREMAVD MKVVHGSRL
//
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