ID A0A0P7B927_9HYPO Unreviewed; 631 AA.
AC A0A0P7B927;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mitochondrial chaperone BCS1-B {ECO:0008006|Google:ProtNLM};
GN ORFNames=AK830_g9688 {ECO:0000313|EMBL:KPM36862.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM36862.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM36862.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM36862.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) 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}.
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:KPM36862.1}.
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DR EMBL; LKCW01000186; KPM36862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7B927; -.
DR STRING; 78410.A0A0P7B927; -.
DR OrthoDB; 819832at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR014851; BCS1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR PANTHER; PTHR23070:SF11; MITOCHONDRIAL CHAPERONE BCS1; 1.
DR Pfam; PF00004; AAA; 2.
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.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424}.
FT DOMAIN 67..278
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 311..520
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 378..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 70182 MW; 18D4C48A60530B5F CRC64;
MTKLGLPPFF QSQGGNFTAN ASSPFPPGMV DSFLATAGQA SPLLQLFFFV YRQIGVQFGL
DPSLLLTLLG VLWGLSKILN QVYAMLQSFS SRYLMCALYV GENDHIYSHL MNFLAQQQNI
AKDRYLMAQT VWKSAWEEEE EMANLLTLVE VGDGDDENEP KYLNFASQAA RSSPRYVPAM
GTTGFWHNGT YFRVNRKKES FMNTSGWSAM KDLEEIKISC FGRSITPIKL LLADAKTMYY
LDTRQKTTIY RPRAKESRRD SNMWQQVARR PVRPMRTVVL DSKEKHDVLR DVNEYLHPGT
PRWYASRGIP LRRGYLFHGP PGTGKTSFSF ALAGVFGIDI YVISLQDVSV TEEDLAALFT
RLPRRCIVLL EDIDTAGLRR DPDADADGDA EDSTKSDAAE KKDGEKDTKA SKEKAKKKAK
KQKEEEESDS DSDSDSSEDE SSRKKKNKKK SKRSRRGGRG LGGVLSVETI SLSGLLNAID
GVASHEGRIL IMTTNKPESL DEALIRPGRV DVQVGFKNAS SAQAGELFHR MYEASRAKQL
ANGSAASAAK GDKAGAAPKQ DEVLDVTMAE LRGISDKFGA LIPEGMFSPA EIQGFLLKRK
KTPRKALEEA EEWIEAAIKQ KESRSKVVTV Q
//
