ID A0A194VC34_9PEZI Unreviewed; 496 AA.
AC A0A194VC34;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative mitochondrial chaperone BCS1-B {ECO:0000313|EMBL:KUI61448.1};
GN ORFNames=VP1G_08639 {ECO:0000313|EMBL:KUI61448.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI61448.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) 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 ---------------------------------------------------------------------------
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; KN714777; KUI61448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VC34; -.
DR STRING; 694573.A0A194VC34; -.
DR OrthoDB; 819832at2759; -.
DR Proteomes; UP000078576; 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:SF87; ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14760)-RELATED; 1.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 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.
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:UP000078576}.
FT DOMAIN 48..238
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 271..412
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 496 AA; 56244 MW; 3BA9F269995638AF CRC64;
MAQPFHAGGA VSTFRLHDSS IQGIYSVATA YFPSLAHLDI TRLGSLIAIA GVVPAVWRIL
RSAWHETYNW IRQFFIASVV IPGRDPLNKN VINWVLDKVI RPRRNTRFFT ARTEVRDRIG
RGDVLESASL KKTQRQVQYL PHFESVWFWH NGRLFLIHRS LESFNTSMCD PGYDGIGGEE
LQISCPGRSA EPIRSLIQTC RDYADQQTQY FVMIYSRDRY GISWQPRSRK PIRLLETVHF
DLDAKQELLS DIRKYLDPET QKRYQSRSMP YRRGYLFYGP PGTGKSSLST ALAGEFGLDL
YEVKIPSVAS DADLEQMFQE IPPQCIVLLE DIDAVWTADR ELSEQEDRTI ASNGSRSPRS
NCTLSGLLNV LDGVGSQEGR IVIMTTNKPE MLDPALVRPG RVDMKVHLGN ITRKLAAEMF
LRMFSDSNEN DIGQLANEFA EHIPENKFTP SQLQGFFQMH LDSAADAAES VAMWVAKELS
KSIMDDDIEI VGQIRA
//
