ID A0A0F4GRC2_9PEZI Unreviewed; 530 AA.
AC A0A0F4GRC2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Mitochondrial chaperone bcs1 like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TI39_contig352g00011 {ECO:0000313|EMBL:KJX99793.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX99793.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX99793.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX99793.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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:KJX99793.1}.
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DR EMBL; LAFY01000344; KJX99793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GRC2; -.
DR STRING; 1047168.A0A0F4GRC2; -.
DR OrthoDB; 819832at2759; -.
DR Proteomes; UP000033647; 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:SF232; 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:UP000033647}.
FT DOMAIN 61..255
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 286..443
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 353..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58005 MW; CCC16DCC12F6D005 CRC64;
MSANRALARL PLAGLSHMVN HAAAGLRGDT SDVLLLSVDS VCRQTFAMLR TASPLLEQSL
KTILPFALLA YGLSRYIKKL LKARDSAHQA FGSFLSHITV SGSSPLNKQV RQYMVKENIG
QNTRSLTISD NDPKDISSGL KFLPSLDATA WFKFQGVWLK FSRSRSEDET PEKTMRNKNG
HVQVVSGGPA EHDLKISCFS LMGCVKPIKA FLEHVKADAE ADKALMTKIV RYVSDGHGDI
YGVPLFRTAR KLDSVAMEAT KKAELVADIT MYLGAKAWYN DRGIPYRRGY LLFGPPGTGK
TSLSSAIAGH FGLQLIIISL TSHGMDDSKL QEIFDRLPQQ CVVLLEDIDS AGVSRENMTD
NEDEAEDEPA PERRPRPSRH SRPKAPAKKT KGVTLSGLLN AIDGPCSQEG RVLIATTNCP
DNLDPALCRN GRVDMKILLG YATAEVSETL FLHIFEDSTG TLSEHDLPTL AKKFATLVPE
DQISPAEVQG YLMLHRWDPA HAVEGAPGWA EKLLEIRRQG GNVASFAGQI
//
