ID K2RC67_MACPH Unreviewed; 389 AA.
AC K2RC67;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=ATPase AAA+ type core {ECO:0000313|EMBL:EKG20111.1};
GN ORFNames=MPH_02556 {ECO:0000313|EMBL:EKG20111.1};
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:EKG20111.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG20111.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG20111.1,
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 -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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:EKG20111.1}.
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DR EMBL; AHHD01000095; EKG20111.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RC67; -.
DR STRING; 1126212.K2RC67; -.
DR VEuPathDB; FungiDB:MPH_02556; -.
DR eggNOG; KOG0728; Eukaryota.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; K2RC67; -.
DR OrthoDB; 1465143at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19502; RecA-like_PAN_like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF12; 26S PROTEASOME REGULATORY SUBUNIT 8; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 165..304
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 11..45
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 389 AA; 43519 MW; 93BFF90055183E8D CRC64;
MALDTFFHNK IESMKLEIIQ GQAKLRRLEA QRNDYNSRVR LLREELGLLQ QPGSYVGEVV
KVMGTKKVLV KVHPEGKYVV DVSDQVDISK LTAGKRVTLL SDSYKLEKML PSSVDPLVSL
MMVEKVPDST YDMIGGLDQQ IKEIKEVIEL GLKHPELFES LGIAQPKGVL LYGPPGTGKT
LLARAVAHHT DCKFIRVSGS ELVQKYIGEG SRMVRELFVM AREHAPSIIF MDEIDSIGSS
RVEGSSGGDS EVQRTMLELL NQLDGFEPTK NIKIIMATNR LDILDPALLR PGRIDRKIEF
PPPTVEARAD ILRIHSRSMN LTRGINLTKI AEKMNGCSGA ELKGVCTEAG MYALRERRVH
VTQEDFDLAT AKILNKHDDK QMSLSKLWK
//
