ID   HEXA_ASPFU              Reviewed;         537 AA.
AC   Q4WUL0;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Woronin body major protein hexA {ECO:0000303|PubMed:23332467};
GN   Name=hexA {ECO:0000303|PubMed:23332467}; ORFNames=AFUA_5G08830;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23332467; DOI=10.1016/j.ijmm.2012.11.005;
RA   Beck J., Ebel F.;
RT   "Characterization of the major Woronin body protein HexA of the human
RT   pathogenic mold Aspergillus fumigatus.";
RL   Int. J. Med. Microbiol. 303:90-97(2013).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23869404; DOI=10.1111/mmi.12316;
RA   Beck J., Echtenacher B., Ebel F.;
RT   "Woronin bodies, their impact on stress resistance and virulence of the
RT   pathogenic mould Aspergillus fumigatus and their anchoring at the septal
RT   pore of filamentous Ascomycota.";
RL   Mol. Microbiol. 89:857-871(2013).
CC   -!- FUNCTION: Major component of Woronin bodies, fungal-specific organelles
CC       that occlude septal pores in order to separate intact from damaged
CC       compartments (PubMed:23332467, PubMed:23869404). HexA binds directly or
CC       indirectly to the Woronin body tether that in turn is anchored at the
CC       rim of the septal pore (PubMed:23869404). Woronin bodies are important
CC       for stress resistance and virulence (PubMed:23869404).
CC       {ECO:0000269|PubMed:23332467, ECO:0000269|PubMed:23869404}.
CC   -!- SUBUNIT: Forms oligomers (By similarity). Self-assembles into hexagonal
CC       rods (By similarity). Binds directly or indirectly to the Woronin body
CC       tether lah (Probable). {ECO:0000250|UniProtKB:P87252,
CC       ECO:0000305|PubMed:23869404}.
CC   -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:23332467}.
CC       Cytoplasm {ECO:0000269|PubMed:23332467}. Note=Localizes at Woronin
CC       bodies, fungal-specific organelles that plug the septal pore in case of
CC       physical damage (PubMed:23332467). Binds to the septal pore in a lah-
CC       dependent manner (PubMed:23869404). {ECO:0000269|PubMed:23332467,
CC       ECO:0000269|PubMed:23869404}.
CC   -!- DISRUPTION PHENOTYPE: Leads to an increased sensitivity to stressors
CC       that affect the integrity of the cell wall and membrane, such as SDS,
CC       the antifungal agent fludioxonil, the acyclic sesquiterpene alcohol
CC       farnesol and the cell wall perturbing agents Calcofluor White and Congo
CC       Red (PubMed:23869404). Does not affect the resistance to hypo-osmotic
CC       stress but leads to a higher sensitivity to physical damage
CC       (PubMed:23869404). Results in the lack of Woronin bodies
CC       (PubMed:23869404). Attenuates virulence in a murine model of infection
CC       (PubMed:23869404). {ECO:0000269|PubMed:23869404}.
CC   -!- SIMILARITY: Belongs to the eIF-5A family. Hex1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAHF01000003; EAL91716.2; -; Genomic_DNA.
DR   RefSeq; XP_753754.2; XM_748661.2.
DR   STRING; 746128.CADAFUBP00005518; -.
DR   EnsemblFungi; EAL91716; EAL91716; AFUA_5G08830.
DR   GeneID; 3510955; -.
DR   KEGG; afm:AFUA_5G08830; -.
DR   VEuPathDB; FungiDB:Afu5g08830; -.
DR   eggNOG; KOG3271; Eukaryota.
DR   HOGENOM; CLU_021655_1_0_1; -.
DR   InParanoid; Q4WUL0; -.
DR   OMA; PPARKMG; -.
DR   OrthoDB; 769149at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0000934; C:porous cell septum; IDA:AspGD.
DR   GO; GO:0140266; C:Woronin body; IDA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0045901; P:positive regulation of translational elongation; IBA:GO_Central.
DR   GO; GO:0009611; P:response to wounding; IMP:AspGD.
DR   CDD; cd04469; S1_Hex1; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR037318; Hex1_S1.
DR   InterPro; IPR001884; IF5A-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11673; PTHR11673; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..537
FT                   /note="Woronin body major protein hexA"
FT                   /id="PRO_0000455965"
SQ   SEQUENCE   537 AA;  61406 MW;  C56E0FB5B92A0BAF CRC64;
     MYSVESKFER DSRRDAQRTA NLDFDARVPI PFSVFPSSYR SDAVPETTLT RVEGEVNLDR
     TSHVEREDTR TSAPLPDPRV YGREEVDIHI SKDRLHAPSR KGDDFQVIYE DRAHKDSRVP
     EVELSRERWK RSENNAKQNK NKNNTSTRRS GDVLKAVSAK KVAPQAQTRA DEKASYQLTQ
     KARYRESTSR YEPLPPKPVY DQALESQLDI TEREYRRRTD PTYDVNLSYG RHQAPVDSYQ
     AYQPQQTSDV SLHRSKTEID VSYDKAYTPK PLETRKGDSF SRSELTVESV PSRPSSASSI
     SQVKVLKPYT AIDQPPARKM GYYDDDGNYH SFRRGVERAV DRITHPFHHH HHHHDREEVV
     IADERGPVRY RDGVREDVRI VEPRASKTTA ESVPIPCHFI RIGDILILQG RPCQVIRISV
     SPQTGQHRYL GVDLFTRQLQ EESSFVSNPS PSVVVQTMLG PVYKTYRILD LHEDGTITAM
     TETGDVKQAL PVVTQGQLFR KIRDAFSEGR GSVRALVIND GGRELVVDYK VIHGSRL