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Database: UniProt
Entry: B2W372_PYRTR
LinkDB: B2W372_PYRTR
Original site: B2W372_PYRTR 
ID   B2W372_PYRTR            Unreviewed;       646 AA.
AC   B2W372;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Mitochondrial chaperone bcs1 {ECO:0000313|EMBL:EDU46708.1};
GN   ORFNames=PTRG_03870 {ECO:0000313|EMBL:EDU46708.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU46708.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231617; EDU46708.1; -; Genomic_DNA.
DR   RefSeq; XP_001934203.1; XM_001934168.1.
DR   AlphaFoldDB; B2W372; -.
DR   STRING; 426418.B2W372; -.
DR   EnsemblFungi; EDU46708; EDU46708; PTRG_03870.
DR   GeneID; 6342106; -.
DR   eggNOG; KOG0743; Eukaryota.
DR   HOGENOM; CLU_010189_4_2_1; -.
DR   InParanoid; B2W372; -.
DR   OMA; IFIRMYS; -.
DR   OrthoDB; 819832at2759; -.
DR   Proteomes; UP000001471; 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; 2.
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:UP000001471}.
FT   DOMAIN          61..244
FT                   /note="BCS1 N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01024"
FT   DOMAIN          277..519
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          110..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  71706 MW;  178A9B2C4D2AD14B CRC64;
     MAIKEDLEGM LPPGLADAAL NIPGLGAVLQ LFLNKLGFDV GSTMSLYLLL FGLWQGAQYM
     YGLGHSYLLD HGTAAIRIND DDDLYAHFIS WISAQRMTAI SRDLVASSRK PKARSDDSDD
     GDSDEEDDDE ALGESGIFNY DKWTGTNPVY YEPNLGDDSF THDGHYFQFK KDSQENKYAE
     RIDYFIVIRC MGRSTQPIKN LIAHVKEWSA NRTKTVTNIH RADARHGGYW ECQAQRPSRP
     ISTVTLDISQ KERIIADINE YLHPATARWY AARGIPHRRG YLFHGPPGTG KTSLSFALAG
     VFGLRVYCAS LSERNMGESD LASLFSMLPS RCIVLLEDID SAGIQRDKGV TAAEPESETE
     SVSDAVAETE PPLSEQHPQQ EDKSDKKADD MIKIEKNKSF RRKLTQSLRT RKTPKTDSET
     TTLVSTKDEI PASPTTQQQQ PQQTPSIQTK TSTPSPPPEP PSEDTKSKIS LAGLLNIIDG
     AASNEGRVLI MTTNYPEKLD SALIRPGRVD LQIKFTLATR EQMQEIFRRM YSNDADVVMK
     PKNTNKTPTA AGVKKKKQQH ASKAGVAGGI TVPLRPSFVT LDPKRLNAMA KQFAESLPED
     TFSPAEIQGY LLMRKTDPEG ALSGVQEWKE ALMEAKKKGK KVVEIK
//
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