ID A0A093VHC2_TALMA Unreviewed; 586 AA.
AC A0A093VHC2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative mitochondrial chaperone BCS1-B {ECO:0000313|EMBL:KFX51555.1};
GN ORFNames=GQ26_0040040 {ECO:0000313|EMBL:KFX51555.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX51555.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX51555.1}.
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DR EMBL; JPOX01000004; KFX51555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VHC2; -.
DR HOGENOM; CLU_465528_0_0_1; -.
DR Proteomes; UP000029285; 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; 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}.
FT DOMAIN 185..358
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 391..523
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 67239 MW; 504B69096489EFA7 CRC64;
MAVNPIIIDV SLALGSKEMM TAYLSQDRKL ISLIKKYRSY NKEYYIQHRG WLRVSPTPYP
PQSEINIKTQ QLIGDSEVVQ EACGLSPVEV LHFDFLLFGI SRMFREFMRK YQNEREKFQR
IEELMLQRGN PFSSLITCAL KCGFQKPEVD LGFITEPIRK RVTKNCITLV QILQRADSFE
KLQPSTVARK LFGRDFPSSI EVQWTDNAFE ALEDWLGQEW VCKKSTRRLA TTGSRLPWNK
NESGGHEEHI LESTPPRTCS LPRLTLTPAN GKHWFMYGRH LILLIREERE DTWGRSRSLH
LKCFGWDGFI LRKILHAARL RHAELDENKT AVYHARYTQK SIGWTRLSGQ GIRPLSTVIM
DPSLQNRLIK DIDGYLRPET KMWHNRRGIP YRQGYLFEGP PGTGKTSLCI ALAGRFKLKI
YILNLSGIAD VALNDLMSSL PERCILLLED IDSQKITNPR TAEPDNSATG QRLTLSGLLN
AMDGVIASEG RILIMTTNHK NKLDPALIRP GRVDMTVSFE YPDSDGIKRL FFLMYAEHPV
EEQEEKREQQ LQHASPQCQI CPKLLPFPPA NIPRNDIPGC TSNSRK
//
