ID A0A439CR90_9PEZI Unreviewed; 595 AA.
AC A0A439CR90;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EKO27_g10482 {ECO:0000313|EMBL:RWA04622.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA04622.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA04622.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA04622.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-2018) 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:RWA04622.1}.
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DR EMBL; RYZI01000540; RWA04622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A439CR90; -.
DR STRING; 363999.A0A439CR90; -.
DR Proteomes; UP000286045; 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; 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:UP000286045}.
FT DOMAIN 68..272
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 305..470
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 482..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 67350 MW; 766890E7C6AD457B CRC64;
MDISSLLRGF IPETVDNATA AANNVSVPHS MPANVVETIL PLIGMKGFAP MYRFIGSWLG
WDPTSLLTIV GVIWATNKVI RQIYSFLYGL VTEYMMSKVH ISSTDDIYIH LMVWLSRQPR
MVNSRALMAE TVSKTAWEDE DESTVARDRS GLYLNFSNQE ARARPQYIPA IGVHSFWWKG
QYFRLHRKKE SIFDDGGNGG FAAFKDKEDL VISCLWRSPK PIKQLLAHAK EQYYSDHQAR
TTVKRPCPAY VRRARNNWLQ VANRPVRDMK TVVLDQQQKL QVLADMNEYL HPDTPRWYAN
RGIPLRRGYL FHGPPGTGKT SLSFALAGVF GLDIHVISLL EPTLTEEDLS GLFSTLPRRC
VVLLEDIDTA GLRRPLEELR ASKRSAKQED KEESHKTVNN DIKELAKVLK KDSEDQKKGI
SLSGLLNAID GVASHEGRVL IMTTNVPEEL DEALIRPGRV DLQVEFTYAT REQAKELFIR
MYEGDQGRPR HMDSRSAAKD ELPRSSPSST KGHALSPETS SAVRSGELDI SIDELPEIAR
QFSEKIPDGE FSPAEIQGYL LKRKKHPRRA VEEAEKWVAA VIEQKINRTK ISQVQ
//
