ID A0A177D5C7_ALTAL Unreviewed; 661 AA.
AC A0A177D5C7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Mitochondrial chaperone bcs1 {ECO:0000313|EMBL:OAG14708.1};
GN ORFNames=CC77DRAFT_555241 {ECO:0000313|EMBL:OAG14708.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14708.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG14708.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14708.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441498; OAG14708.1; -; Genomic_DNA.
DR RefSeq; XP_018380129.1; XM_018532156.1.
DR AlphaFoldDB; A0A177D5C7; -.
DR STRING; 5599.A0A177D5C7; -.
DR GeneID; 29117750; -.
DR KEGG; aalt:CC77DRAFT_555241; -.
DR VEuPathDB; FungiDB:CC77DRAFT_555241; -.
DR OMA; IFIRMYS; -.
DR OrthoDB; 819832at2759; -.
DR Proteomes; UP000077248; 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|SAM:Phobius};
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:UP000077248};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..241
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 274..533
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 344..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 73087 MW; D7A8246C90C2C1EB CRC64;
MENLKDSLPP GMADAAINIP GVGAILQLLL NKLGFDVGST MSLYLLLFGL FQGALFMYTQ
GRGFILGHGT SAIRIDDDDD LYPQFISWIS EHRMTEVSRD LKATSKKPRA RGDEIDNDDA
SEADFEDVLD DSGIFNYEKY KGTSPTYYEP NMGDDSFTHN GHYFQFSKDC QENKYQERIE
YFLIIRCMGR STKPVKDLID HVKEWSAHKP NKTTEIMRAE IKHGGYWHVQ SNRPSRPIST
VTLDEAQKNK VVADINEYLH PATARWYAAR GIPHRRGYLF HGPPGTGKTS LSFAVAGIFG
LSVYCASLSE RDMSESDLAS LFGQLPNRCI VLLEDIDSAG IRRDKSSVIP EQEHDSAVNE
SDKSSAPAPT EKVTEEKEDN NDNKSENKSE EKQHDSVEME KKKSIRRRIT HSLHPRKSSS
KPNSETTTLA TTASSPASAP PSVLTPAPSI KEVATSTKPT STPTPPPPPP PPPIDEEGSK
SKISLAGLLN IIDGAASSEG RVLIMTTNYP EKLDSALIRP GRVDLQIKFT LATRTQVEEI
FRRMYSDEAD GKKCDGSDGG EKKYAPEKKG SSSNDKRKEE ARWGATGNKS PNFATLPPDQ
LTEMARQFAD ALPEAVFSPA EIQGYLLQKK SDPQGALDGV GEWRDAVLEA KKKGKKVIEL
K
//
