ID K2SFN6_MACPH Unreviewed; 392 AA.
AC K2SFN6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Prohibitin {ECO:0000313|EMBL:EKG15625.1};
GN ORFNames=MPH_07060 {ECO:0000313|EMBL:EKG15625.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG15625.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG15625.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG15625.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000256|ARBA:ARBA00005495}.
CC -!- SIMILARITY: Belongs to the prohibitin family.
CC {ECO:0000256|ARBA:ARBA00009658}.
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:EKG15625.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHHD01000293; EKG15625.1; -; Genomic_DNA.
DR AlphaFoldDB; K2SFN6; -.
DR STRING; 1126212.K2SFN6; -.
DR VEuPathDB; FungiDB:MPH_07060; -.
DR eggNOG; KOG3083; Eukaryota.
DR HOGENOM; CLU_047969_0_0_1; -.
DR InParanoid; K2SFN6; -.
DR OrthoDB; 1330394at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR CDD; cd03401; SPFH_prohibitin; 1.
DR Gene3D; 3.30.479.30; Band 7 domain; 1.
DR Gene3D; 3.90.1590.10; glutathione-dependent formaldehyde- activating enzyme (gfa); 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR006913; CENP-V/GFA.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR000163; Prohibitin.
DR PANTHER; PTHR23222; PROHIBITIN; 1.
DR PANTHER; PTHR23222:SF0; PROHIBITIN 1; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF04828; GFA; 1.
DR PRINTS; PR00679; PROHIBITIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 25..186
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 392 AA; 43589 MW; ED868E3C78D65CB7 CRC64;
MANALQAIYK WAVPLAVGAS VAQAAMYDVK GGTRAVIFDR LSGVRENVVN EGTHFLVPWL
QRAIIYDVRT KPRNISTTTG SKDLQMVSLT LRVLHRPEVK MLPRIYQNLG TDYDERVLPS
IGNEVLKAIV AQFDAAELIT QREAVSNRIR TDLLKRAQEF NIALEDVSIT HMTFGKEFTK
AVEEKQIAQQ EAERARFIVE KAEQERQANV IRAEGEAEAA DTISKAVAKS GDGLIQIRRI
ETQKEIAQML AANPQVTYLP SGSKGSGEGQ GGNFLLGLRS EWILLFYAKA FGTNYGLTAK
LPKDSFKYTQ GTPKEHVADN GSGTMLHREF CDNCGSFILE YGEPAKNDFR YICVGSLDDP
EALAPKGEFF CKSRSSWMPE VPGTFQKKEI KE
//
