ID A0A0G2G060_9PEZI Unreviewed; 648 AA.
AC A0A0G2G060;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative mitochondrial chaperone bcs1 {ECO:0000313|EMBL:KKY39489.1};
GN ORFNames=UCDDA912_g00507 {ECO:0000313|EMBL:KKY39489.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY39489.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY39489.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY39489.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY39489.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY39489.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-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:KKY39489.1}.
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DR EMBL; LCUC01000018; KKY39489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2G060; -.
DR STRING; 1214573.A0A0G2G060; -.
DR OrthoDB; 819832at2759; -.
DR Proteomes; UP000034680; 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:UP000034680}.
FT DOMAIN 69..279
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 312..502
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 381..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 71749 MW; 670B178089CD3BCC CRC64;
MDFKSVFGKQ LHHGAFNSNL TATNMSGSMP GLEGIITLLG SRNPLVQLFM LLHQMVGSRI
GIDPTMILTL AGFAWAANKI WRQFFMVIYR FIAEYLMASI HVSSGDEIYL HMIKWLASQP
NLVNSRSLTA ETLSKTAWEE EDEADVLATR ISPDGEGVYL NFSNQEAKMP PRFVPALGVH
GFWFDRNYFR LHRKQESFFE DSASGGQTFK DKENLVISCL GRSPEPIKKL LKHAKESYYN
DHYAKTIVKR PSPMNMRRYG GRHAWAQVAN RPVRPMKTVV LDGKQKVQLL ADVNEYLHPA
TPRWYANRGI PLRRGYLFHG PPGTGKTSLS FALAGVFGLD IYVISLLEPS LTEEDLLSLF
NSLPRRCVIL LEDIDTAGLA RPKEEQDQDV DVDVDGEGNE GSKREGGRGR KGGRPNGIGG
GDGGDGGMND WKVSDLAREL KKQGGPDEKK GISLSGLLNA IDGVASHEGR VLIMTTNKPE
ALDDALIRPG RVDLQVAFTN ATQEQARELF ERMYEADSKR KPTAAPQQKQ PATNGKPVAN
GHTRKPEKAD AHAAGPDYRP NEAHVSGGGG TISSEALDDH RLDMTIEELR VVAADFAAKI
PDGFSPAELQ GFLLKRKKDP RRALAEVEHW VDAMMKQKAS KTKVLQVQ
//
