ID   A0A150USI8_9PEZI        Unreviewed;       594 AA.
AC   A0A150USI8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-SEP-2023, entry version 27.
DE   RecName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M433DRAFT_76641 {ECO:0000313|EMBL:KYG41075.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG41075.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG41075.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG41075.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG41075.1}.
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DR   EMBL; JPDO01000827; KYG41075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150USI8; -.
DR   STRING; 766039.A0A150USI8; -.
DR   Proteomes; UP000075602; 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   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639:SF32; HEAT SHOCK PROTEIN PDR13; 1.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   REGION          491..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..524
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  62932 MW;  1DCA1B7FB2ADF483 CRC64;
     MSAEEVIDET RTAIGISFGN SYSSIAYTGA DDKAEVIANE EGDRQIPSIL SYVSGEEFQG
     TQAKAQIVRN PRNTIAFWRD YIGKDFKDID PSPCHASAHP VELNGGKEVG FTVQESIEEA
     EGDSVPAKST LSVSEVTTRH LRRLKQSASD YLGKDVTAAV ITVPSDFSEK QKTALSCAAK
     NAGIEVLQFI PDTVSALLAH DAKQQLSEGG ASSTPQDKVV IVADLGGTRS DIAVIASRGG
     IYTTLATAHD YELGGQSLDK VLVEYAAKEF LKRNKSASDP RATERSLAKL TLEAEAVKKA
     LSLGATASFS IESLIDGLDF SLSVNRTRFE LLANKVFAAF TRLITSVVQK ADLDLLDIDN
     ILLSGGTSHV PKIASNLQNS FPESTIIIAP STSASAVNPS ELTARGAAIQ ASLVSAFETT
     EIAASTEAVV TVTPHLQHAI GLVTAGSEGK DEQFALIIDS DTPVPVRRTA HISVPEGGDV
     LLRLAEGSRQ IHVRKENKPQ ANGVKGSADE DEDEDEEDGE SDDEPEEVRS KIYLPGKLLA
     EAAIRNVKKG GKVEVQVNVA ADMSVTFVCR EVGGKGGIRG TVEAGNPIMN GNAA
//