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Database: UniProt
Entry: F8N3H6_NEUT8
LinkDB: F8N3H6_NEUT8
Original site: F8N3H6_NEUT8 
ID   F8N3H6_NEUT8            Unreviewed;       473 AA.
AC   F8N3H6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Mitochondrial chaperone BCS1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NEUTE1DRAFT_72346 {ECO:0000313|EMBL:EGO52581.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO52581.1};
RN   [1] {ECO:0000313|EMBL:EGO52581.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO52581.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007448}.
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DR   EMBL; GL891382; EGO52581.1; -; Genomic_DNA.
DR   RefSeq; XP_009856223.1; XM_009857921.1.
DR   AlphaFoldDB; F8N3H6; -.
DR   GeneID; 20829592; -.
DR   KEGG; nte:NEUTE1DRAFT72346; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_72346; -.
DR   HOGENOM; CLU_010189_6_2_1; -.
DR   OrthoDB; 664379at2759; -.
DR   Proteomes; UP000008065; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd19510; RecA-like_BCS1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR014851; BCS1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR   PANTHER; PTHR23070:SF232; MITOCHONDRIAL CHAPERONE BCS1; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08740; BCS1_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01024; BCS1_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}.
FT   DOMAIN          33..215
FT                   /note="BCS1 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01024"
FT   DOMAIN          246..378
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   473 AA;  52105 MW;  80356B9A12E91FBA CRC64;
     MSTDPQTPLT AGSILNLDVL FNNPVFAGGM GLAGLGAAAA FGRRAAIRGA GLLKRQMLVN
     VEISKRDPSY NWVLAWLALP RDNTGFIAQR LTRLRNLSVS TTTKSITPGK DEGSSHADFR
     VQPGFGRHII RHKPGVYIAV NREKASTTQT ATGEPHETLT LTLLWPHRHV LGEIFTEAHQ
     MAHRFHEGKT VVYTAKRMEW MPLGKPRLKR PLGSVILDKG VKESIVDDVK EFLAAQQWYT
     DRGVPYRRGY LLYGPPGTGK TSFIQALAGE LDYSVAMINL SEVGITDDLL AHLLTQQPEK
     SILVLEDVDA ALVNRRPRDS DGYSGGTVTF SGLLNALDGL AAGENRIAFL TTNHIDRLDP
     ALIRPGRVDM MMRIGEATRH QAAEMWDRYY GDIDADHSGR ERFLNRLDEL GLFGENNQDP
     DAPKRHTSTA AIQGLFQFNK NDMEGAIKMA EGLIPRTFVA ENPSSDGSMK SPA
//
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