HEX1_EMENI
ID HEX1_EMENI Reviewed; 221 AA.
AC Q9P8K9; C8VAY2; Q5B435;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Woronin body major protein {ECO:0000303|PubMed:10783241};
GN Name=hex1 {ECO:0000303|PubMed:10783241}; ORFNames=AN4695;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10783241; DOI=10.1038/35008652;
RA Jedd G., Chua N.-H.;
RT "A new self-assembled peroxisomal vesicle required for efficient resealing
RT of the plasma membrane.";
RL Nat. Cell Biol. 2:226-231(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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:10783241). Hex1 binds directly or indirectly to
CC the Woronin body tether that in turn is anchored at the rim of the
CC septal pore (PubMed:10783241). {ECO:0000269|PubMed:10783241}.
CC -!- SUBUNIT: Forms oligomers (By similarity). Self-assembles into hexagonal
CC rods (By similarity). {ECO:0000250|UniProtKB:P87252}.
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000250|UniProtKB:P87252}.
CC Note=Localizes at Woronin bodies, fungal-specific organelles that plug
CC the septal pore in case of physical damage.
CC {ECO:0000250|UniProtKB:P87252}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. Hex1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF76981.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF239659; AAF67173.1; -; mRNA.
DR EMBL; AACD01000080; EAA60737.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF76981.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_662299.1; XM_657207.1.
DR AlphaFoldDB; Q9P8K9; -.
DR SMR; Q9P8K9; -.
DR STRING; 162425.CADANIAP00005736; -.
DR PRIDE; Q9P8K9; -.
DR EnsemblFungi; EAA60737; EAA60737; AN4695.2.
DR GeneID; 2872493; -.
DR KEGG; ani:AN4695.2; -.
DR eggNOG; KOG3271; Eukaryota.
DR HOGENOM; CLU_021655_0_0_1; -.
DR InParanoid; Q9P8K9; -.
DR OrthoDB; 769149at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0140266; C:Woronin body; ISS: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 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 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..221
FT /note="Woronin body major protein"
FT /id="PRO_0000142508"
FT MOTIF 219..221
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 221 AA; 25091 MW; 567634BFA7A62C93 CRC64;
MGYYDDDGNY HSFRRGVERA VDRITHPFHH HHHDHHDHHR EEVIVTDERG PVRYRDGVKE
NVRIVEPRGA AATTSETVPI PTHFIRVGDI LVLQGRPCQV IRISSSPMTD QRRYTGVDLF
TRELHEESSF VSNPKPSVVV QTMLGPVYKT YRILDIQEGT IVALTESGDV KSGIPVIPQG
NLYQRIKDAF LEGRGSVRAL VINDGGRELV VDYKIIHSSR L
