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Database: UniProt
Entry: K2RR25_MACPH
LinkDB: K2RR25_MACPH
Original site: K2RR25_MACPH 
ID   K2RR25_MACPH            Unreviewed;       996 AA.
AC   K2RR25;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Heat shock protein Hsp70 {ECO:0000313|EMBL:EKG12634.1};
GN   ORFNames=MPH_10300 {ECO:0000313|EMBL:EKG12634.1};
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:EKG12634.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG12634.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG12634.1,
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   -!- 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:EKG12634.1}.
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DR   EMBL; AHHD01000446; EKG12634.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2RR25; -.
DR   STRING; 1126212.K2RR25; -.
DR   VEuPathDB; FungiDB:MPH_10300; -.
DR   eggNOG; KOG0104; Eukaryota.
DR   HOGENOM; CLU_005965_5_0_1; -.
DR   InParanoid; K2RR25; -.
DR   OrthoDB; 5491443at2759; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10230; HYOU1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Stress response {ECO:0000313|EMBL:EKG12634.1}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..996
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003864200"
FT   REGION          598..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..784
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..926
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..996
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  107372 MW;  61E0AF14268D1E4F CRC64;
     MAPPGRRRYG ALTTVLALFC LFASTASAAS AVLGIDLGTS YLKGALVKPG IPLEIVLSKD
     SKRKEAAAVA FKTPRTPLSA AGPAFPERAY GGDALALSAR FPADVYPNLK PLLGQRIAEA
     GHAQEYQKLH PAIEVVGVDG RGTVGFRSPS FEADAPPFSV EELLAMELQN LRENAETMAG
     KGTRITDAVI TVPPFYTAAE KRAVELAAEL AGLKVLALLS DGVAVGLNYA TSRTFPSVSE
     GGKPENHLVF DMGAGSTTAT VLRFQGRTVK DVGRFNKTVQ EVQVLGAGWD KSLGGDALNE
     LIIDDIITQF TENAEAKKVG VQAEDVRKHG RTMAKLWKDV EKVRQVLSAN QESGSSWEGL
     YQDVDFKYKI SRSHFEELAA GHAARVEGPV KRALEAAGLS FADLDSVILH GGAVRTPFVQ
     KTLEGLAGDA SKLRSNVNAD EAAVFGAAFK GAGLSPSFRV KEIRDSDTAN YPVNMKYTWN
     LKERNQKLFS ATSRQGTVKE MPFKMLGDFE FSLFQQTDEA TEQPILSVRT GNLTAVVTNL
     IDKEGCERED INTKFSIRLD PTTGLPEIVK AEASCEVDET EKKGGVVDGV KDFFGFGSKD
     GKQEPLSDTE AAADESTESV EPETSPSASA SGSSTSEDAK ATESAEAKVP KKKTVTSNIR
     FSTTREGFKK VPKEEMKRMK DRLSAFDASD RARFAREAAL NELEAYTYRS RDLLEDEGFI
     SASTEAQRTE IETKLHEVSE WLYGDGSDAE EKVLKAKHSD LKALIDPIIT RRDESRKRPE
     SIQKVKDALG QTENIIKIIK ESIEKAAEAS SSSAASASSA SAAPSSSTPT PEASAEADPL
     ADLEEDEPAA SSSSSAEEAQ TTEQPSYLSP YTQDDLEELT KALEDATKWL DEKLAEQEKR
     KDTEDPAVSS KDLEKKAKDL NDVTLELLQR KIKMPAGGNK KSGGGKKSGG KKASGKKGGK
     KDKKAEEKKA KEAEAEVEGD KKGEEEGKQT PEHSEL
//
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