ID A0A0D1YWL4_9EURO Unreviewed; 998 AA.
AC A0A0D1YWL4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Actin-like ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_02513 {ECO:0000313|EMBL:KIV86937.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV86937.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV86937.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV86937.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846951; KIV86937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YWL4; -.
DR STRING; 1016849.A0A0D1YWL4; -.
DR HOGENOM; CLU_005965_5_0_1; -.
DR OrthoDB; 5491443at2759; -.
DR Proteomes; UP000053599; 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; 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:UP000053599};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..998
FT /note="Actin-like ATPase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002237265"
FT REGION 604..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 106336 MW; B551D21813B4C63D CRC64;
MAPPGRRKLS LLSALPLLVL LILSLASNVH AASAVLGIDL GTEYFKAAVA KPGSPIDIVL
SKDSKRREAA TLAFKPARLQ ANNAEVFPER LYGGDAVALS ARFPTDVYPN LKSLLGVESS
ANAVKTYSAR YPGLDVQTVS RLDGAGTVGL KSHSFGKRDE VFMVEELLAM QLKNIRGNAE
AMVPKGTFIT DVVITYPAFY TAQEKRAIEL AADLAGMRVL GLISDGLAVG LNYATHRTFD
SISEGGKPEH HLVYDMGAGS TTATVLKFQG RTIKGYAKRN QTIQEVVVLG TGFDTTLGGD
SLNDVIVADI ISQFLESPKV QKFGLDSAQV RASGKTMARI WKEAERMRQL LSANAVSSAT
FEGLYDEEIT FKYSLTREKY EELAADHAAR VGSPLSTALE SAGLKLDDID SIILHGGAVR
TPFVHKQLEK VAGGTSKLKS NVNADEAAVM GAGFKAASLS PSFRVKDIRD MDISGSTYTL
KWTQDSKEKS QKLFTPMSQV GTEKQVPIKV LEDVKLGFVQ GVNEKDLPIL DIEATNLTKS
TAQLKDKHGC TATNISTVFN IRLSPVDGLP EVLSGTVSCE ANSTKVGSVM DNVKGLFGFG
SNKDDSQKVL DDEDASEDSS ATLTPLPASD PTSSGSTVSE ASATPADSSA SSSASKSAKS
GKATPSTVTI PLALKSTVMG LNTPPAETLP KVRQRLTQFD TSDQNYVLRA EALNTLEGFT
YRARDYLEDQ SFITASTETV RKELEKQLSS VSEWLYGEGL DASLQDFKDK LRSLQSLVDP
VLKRKDEATK RPDAVIALRE QIENLTGMIQ MVEGSIKKAA EGAASSVSSA ASSVASSVTG
SASSSVADAD DLDDDPYSGT STAEAATETE EPAPKLYEYT KEDLSVLTTN YEKAKAWLEE
KMALQDKLGP NDEPAFSVSE LETRGKELQK VVQDMILKTI KFQDVPKKAK SGSRKVKGKA
KKSKATSATG DGAGSSGGST GTPAASGTAT KSSVKDEL
//