ID E3SAP8_PYRTT Unreviewed; 282 AA.
AC E3SAP8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Prohibitin {ECO:0000256|RuleBase:RU366048};
GN ORFNames=PTT_20268 {ECO:0000313|EMBL:EFQ84959.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ84959.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ84959.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU366048}.
CC -!- SIMILARITY: Belongs to the prohibitin family.
CC {ECO:0000256|ARBA:ARBA00009658, ECO:0000256|RuleBase:RU366048}.
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DR EMBL; GL538163; EFQ84959.1; -; Genomic_DNA.
DR RefSeq; XP_003306953.1; XM_003306905.1.
DR AlphaFoldDB; E3SAP8; -.
DR STRING; 861557.E3SAP8; -.
DR EnsemblFungi; EFQ84959; EFQ84959; PTT_20268.
DR KEGG; pte:PTT_20268; -.
DR eggNOG; KOG3083; Eukaryota.
DR HOGENOM; CLU_047969_0_2_1; -.
DR OrthoDB; 1330394at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0035632; C:mitochondrial prohibitin complex; IEA:EnsemblFungi.
DR GO; GO:0005777; C:peroxisome; IEA:EnsemblFungi.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IEA:EnsemblFungi.
DR GO; GO:0000001; P:mitochondrion inheritance; IEA:EnsemblFungi.
DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:EnsemblFungi.
DR GO; GO:0006457; P:protein folding; IEA:EnsemblFungi.
DR CDD; cd03401; SPFH_prohibitin; 1.
DR Gene3D; 3.30.479.30; Band 7 domain; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR000163; Prohibitin.
DR PANTHER; PTHR23222; PROHIBITIN; 1.
DR PANTHER; PTHR23222:SF0; PROHIBITIN 1; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00679; PROHIBITIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU366048};
KW Mitochondrion {ECO:0000256|RuleBase:RU366048};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU366048};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..282
FT /note="Prohibitin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003181959"
FT DOMAIN 25..186
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 258..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 30842 MW; 58356A8B2D002C2C CRC64;
MAALPASLFR FAVPLAIGAS IVQSSLYDVK GGTRAVIFDR LSGVKEQVVN EGTHFLVPWL
QRAIVFDVRT RPRNISTTTG SKDLQMVTLT LRVLHRPEVK QLPKIYQNLG LDYDERVLPS
IGNEVLKAIV AQFDAAELIT QREAVSNRIR TDLLKRANEF NIALEDVSIT HMTFGKEFTK
AVEEKQIAQQ EAERARFIVE KAEQERQANV IRAEGEAEAA DTISKAVAKS GDGLVLIRRI
ETQKDIAQML ARNPNISYLP GGGSGGNGGG SSGGSFLLGL RS
//
