ID K2RGZ8_MACPH Unreviewed; 252 AA.
AC K2RGZ8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 40.
DE SubName: Full=Heat shock protein DnaJ {ECO:0000313|EMBL:EKG21816.1};
GN ORFNames=MPH_00735 {ECO:0000313|EMBL:EKG21816.1};
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:EKG21816.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG21816.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG21816.1,
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 HscB family.
CC {ECO:0000256|ARBA:ARBA00010476}.
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:EKG21816.1}.
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DR EMBL; AHHD01000035; EKG21816.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RGZ8; -.
DR STRING; 1126212.K2RGZ8; -.
DR VEuPathDB; FungiDB:MPH_00735; -.
DR eggNOG; KOG3192; Eukaryota.
DR HOGENOM; CLU_068529_1_0_1; -.
DR InParanoid; K2RGZ8; -.
DR OrthoDB; 1479333at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Stress response {ECO:0000313|EMBL:EKG21816.1}.
FT DOMAIN 168..240
FT /note="Co-chaperone HscB C-terminal oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF07743"
FT REGION 42..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 174..205
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 42..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 252 AA; 28652 MW; 3092E0988348ABC2 CRC64;
MRAATPQALS WLRTVIRREL QPTILRSTSL RPSSHLRIHT SAALSTHSSP ARAFGTTNSR
HQSSHTSSAP SPTPQHTHYT FFPKTLPHGP PPAGPFAIDL RALRNEFLQL QAGAHPDRHS
GADKRRAEAL SARINEAYRA LQNPLLRAQH LLQLRGIDVA EDERLKVEDP ELLMEVLEAR
ERIEEAESEE ALQDMKEENE RRIEQSVEVL DRAFKEDDMD KAKEEAVRLR YWVNIKDSLD
AWEPGKPVVL QH
//