ID A0A3P8NHS6_ASTCA Unreviewed; 420 AA.
AC A0A3P8NHS6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Mitochondrial chaperone BCS1 {ECO:0000256|ARBA:ARBA00016942};
DE AltName: Full=BCS1-like protein {ECO:0000256|ARBA:ARBA00032816};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000004356.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000004356.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000004356.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8NHS6; -.
DR STRING; 8154.ENSACLP00000004356; -.
DR Ensembl; ENSACLT00000004445.1; ENSACLP00000004356.1; ENSACLG00000002897.1.
DR GeneTree; ENSGT00390000005415; -.
DR OMA; WMTLYQR; -.
DR OrthoDB; 664379at2759; -.
DR Proteomes; UP000265100; Chromosome 16.
DR Bgee; ENSACLG00000002897; Expressed in ovary and 6 other cell types or tissues.
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 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; 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: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.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..191
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 222..358
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 420 AA; 47467 MW; 414BA26DB6194B54 CRC64;
MPLTDFLDGL KDNPYFGAGF GLVGVGTALA LARKGAQVGM IFFRRHYMIT LEVPSRDKSY
NWLLSWITKH AKHTQHLSVE TSYLAHESGR VHTQFDFHPS PGNHIIWYGR KWIRVERTRE
KQMVDLHTGT PWESVTFTAL GRDRQIFFNI LQEARELALK QEEGRTVMYT AMGAEWRPFG
FPRRRRPLSS VVLDVGVAER IVDDVKDFIG NPKWYTDRGI PYRRGYLLYG PPGCGKSSFI
TALAGELGYS ICLMSLSDRT LSDDRLNHLL SVAPQQSIIL LEDVDAAFVS RDLLPTENPL
AYQGMGRLTF SGLLNSLDGV ASSEARIVFM TTNFIDRLDA ALIRPGRVDL KQYIGHCTHW
QLTQMFRRFY PDEPASEAEH FAKHALATHS EISAAQVQGH FLLHKMDPAG SIDNVAQIKG
//