ID K2RWX6_MACPH Unreviewed; 794 AA.
AC K2RWX6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Chaperonin ClpA/B {ECO:0000313|EMBL:EKG19268.1};
GN ORFNames=MPH_03131 {ECO:0000313|EMBL:EKG19268.1};
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:EKG19268.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG19268.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG19268.1,
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 ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:EKG19268.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHHD01000163; EKG19268.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RWX6; -.
DR STRING; 1126212.K2RWX6; -.
DR VEuPathDB; FungiDB:MPH_03131; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_0_1; -.
DR InParanoid; K2RWX6; -.
DR OrthoDB; 35211at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 120..263
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 519..659
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 698..789
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 57..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..420
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 794 AA; 88337 MW; F7469B6EBF63DB31 CRC64;
MLSARARLAA RRLSTTIHDV SARPMLARPL SSLAQPITAQ SRITANTVRP VTAIRHYANG
RPHPPGGTHR MNMGGGEEEK PALEQYGIDL TAKAKDGKLD PVIGRDAEIH RTIQILARRT
KNNPVLIGSA GTGKTAILEG LAQRIVRGDV PESIKNKRVV SLDLGSLIAG AKFRGDFEER
LKKVLKEVEE AQGGVILFID ELHTLLGLGK AEGSIDASNL LKPALSRGEL QCCGATTLNE
YRQIEKDVAL ARRFQPILVG EPTVADTISI LRGIKERYEV HHGVRITDGA IVAAATYSNR
YITDRFLPDK AIDLVDEAAS ALRLQQESKP DTIQELDRQI MTIQIELESL RKEDDIASKE
RREKLEEQLK AKKEELGKLN EKWENERREI EEIKKVKEDL EKARLELEQC QREGNFAKAS
ELRYATIPAL EQRLPKDGTD RGKSPDSLLH DSVTADDIAN VVSRTTGIPV SKLMSGEMEK
LIHMEDILRQ SVKGQDEALT AVANAVRMQR AGLSGENRPL ASFMFLGPTG VGKTELCKKM
AEFLFSTETA VIRFDMSEFQ EKHTVSRLIG SPAGYVGYED AGQLTEAVRR KPYAVLLFDE
FEKAHRDISA LLLQVLDEGF LTDAQGHKID FRNTMIVLTS NLGAEVIVGD DMLHRHQVDA
ETGEISPQVK KAVMDIVAAN YPPEFLNRLD EFIIFRRLSK SALKEIVDIR LKELQQRLDD
RRISLRVPEE VKQWLCDRGY DPKFGARPLN RLISREIGNN LADKIIRGEL RNNTTAVVGI
NEGQTGLTVA AEAS
//
