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Database: UniProt
Entry: A0A0N0NS12_9EURO
LinkDB: A0A0N0NS12_9EURO
Original site: A0A0N0NS12_9EURO 
ID   A0A0N0NS12_9EURO        Unreviewed;       893 AA.
AC   A0A0N0NS12;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Putative mitochondrial chaperone BCS1-A {ECO:0000313|EMBL:KPI45721.1};
GN   ORFNames=AB675_909 {ECO:0000313|EMBL:KPI45721.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI45721.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI45721.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI45721.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-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:KPI45721.1}.
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DR   EMBL; LFJN01000001; KPI45721.1; -; Genomic_DNA.
DR   RefSeq; XP_018005684.1; XM_018149606.1.
DR   AlphaFoldDB; A0A0N0NS12; -.
DR   STRING; 1664694.A0A0N0NS12; -.
DR   GeneID; 28741475; -.
DR   Proteomes; UP000038010; 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   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; 2.
DR   Pfam; PF08740; BCS1_N; 1.
DR   SMART; SM00382; AAA; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT   DOMAIN          541..759
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          146..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..701
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  100440 MW;  1C4C72D5845503E9 CRC64;
     MPAPQRSVCD LRWLKPASSA IFRDVSLDTL TRIDPRSEEF NDACISLVAS SSTLGCFIAI
     SITQRAFNMA GFLSQLAGKI DWDAAAHGTA DYISDVANHI DTTAAKEKML ASETNKEYKD
     ISNQSIQAIT REVTERVLLD LDSRYMSTTS SPRSSFLDRR TPFYPNGDSP TKESLRLVGS
     DSKALAENDL SCVLYSRPGE DPRSACPPDA STPTTNTPSI SGSSSTSALS LITHQSTSAG
     RMAPPLNPRF MNPSEGSSSL KRFFMLFLRR YACKSGYAMV QDTFGSEVAA LARLWSTFSN
     VINVIALIRD IFRFVGSMNS SLSQIPGKIL ESVKTNHMVR MRTYLGTELA TNALEWIKAA
     KKKKGSDLSR IDRAKLFLMR KALARPCRFF TASTHEGDEH DASEQDADKD NGKKDDEKRG
     KLRIDEREYV TDFFIYRGKL ILFEESESEN ENNVLDFFCL DKSTKVLEDW LEEVNKSAQQ
     KGKVRIFTYS GGTSWTLLKS KIQRAVENVW MEDDLRADIL SEITAYYEED EAVARSLGIP
     WRKGYLFHGK PGTGKTTLAY ALAGHFGMRV HVLSLTHPNL DDEMLLKLGE ALGEKDLLLL
     EDIDCVGLSR QRTAPIVNSR SKHDIRSVQL SMRSQYPEKS SNTQRRQHAH QRRIAQLSHK
     PGDKGAYRRW QRDQLLDENA ESESGYDEGS WHEEEEEQEE EPSQSPNRVT LAGLLNMLDS
     GRAPEGHIVV MTTNHKDVLD DALIRHGRVS RQIEFKYITK SIAKQMFTKM YDVKSRKAVN
     YSGAQIPFLA EDFARNCPEG VLSPAAIQDF IFARKQNPKR AVDEIKQWAA ARRERRLRRE
     AMPCMMKPLS RLSMDLEKCE AGAKIKLPRL QSNSHSEMTH VSFPGKQGFS AVT
//
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