ID K2RHX5_MACPH Unreviewed; 510 AA.
AC K2RHX5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=ATPase AAA+ type core {ECO:0000313|EMBL:EKG14218.1};
GN ORFNames=MPH_08593 {ECO:0000313|EMBL:EKG14218.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG14218.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG14218.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG14218.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG14218.1}.
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DR EMBL; AHHD01000364; EKG14218.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RHX5; -.
DR STRING; 1126212.K2RHX5; -.
DR VEuPathDB; FungiDB:MPH_08593; -.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_4_2_1; -.
DR InParanoid; K2RHX5; -.
DR OrthoDB; 819832at2759; -.
DR Proteomes; UP000007129; 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:SF87; ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14760)-RELATED; 1.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 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:UP000007129}.
FT DOMAIN 39..209
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 242..381
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 469..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 55656 MW; B4AC9477765DD274 CRC64;
MESDTTSTPS KGGKVDRVVK AFEDGCASPL CHSIAGLVWG LLAGYMLLKS YWAALETLIL
AHYACTLTIH SGERIGDDVV EWMSKNLELD SNVFEIHYSR APEEERANIQ LKPGLGTHTF
RYGGTWLRIS RSRIKVGERE GGKIGLAKEV LKISSFGRGN SVLQAFLEEC RDFASNQVGK
LTHIYRTSPQ ARGRWDSPTS RVSRPMSTID IDEAVKKNLL EDARRYFHVS ARNFYANRGI
PHRRGYLFYG PPGCGKSSIS QAMAGHFRIP IFTVSLASSD MTDDVLEQLF DGVADRCDPP
KCIVLLEDID SAGISREKMR AARARRRQRG VTLSGLLNII DGVAALEGRL LIMTSNTPDT
LDAALVRPGR IDKQVYFGPV THAVAASIFA RMFTVGPDEQ FDYEQSARQQ QQQQPDCGLP
ALASAFGAVV PEKLVTPAET QCYLLEHRDD PVAAVERAAD WVARLVEAKT KGTSVSEPTP
VGAGAQAAGG AGEGGEGKGD DDDDDDNDHP
//
