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Database: UniProt
Entry: F8P9T7_SERL9
LinkDB: F8P9T7_SERL9
Original site: F8P9T7_SERL9 
ID   F8P9T7_SERL9            Unreviewed;       847 AA.
AC   F8P9T7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Actin-like ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SERLADRAFT_358241 {ECO:0000313|EMBL:EGO20416.1};
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1] {ECO:0000313|EMBL:EGO20416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S7.9 {ECO:0000313|EMBL:EGO20416.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA   Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA   Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA   Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA   Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA   Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "Evolution of plant cell wall degrading machinery underlies the functional
RT   diversity of forest fungi.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL945441; EGO20416.1; -; Genomic_DNA.
DR   RefSeq; XP_007323161.1; XM_007323099.1.
DR   AlphaFoldDB; F8P9T7; -.
DR   GeneID; 18809607; -.
DR   KEGG; sla:SERLADRAFT_358241; -.
DR   HOGENOM; CLU_005965_5_0_1; -.
DR   OrthoDB; 5491443at2759; -.
DR   Proteomes; UP000008064; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..847
FT                   /note="Actin-like ATPase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003376401"
FT   REGION          558..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  93625 MW;  5315A08E63273443 CRC64;
     MLSFGFHRFI SLCLIFLAVF ESSLASVLAI DYGSDWIKAS LMKPGIPFDV LLNKDSKRKI
     QSTVAWKKDD RLFGTDASNI ASRFPSDSFS SLKYLQGVTY GADLMSYFTS ISTADIFKTS
     RSTIGLRQSD GTEWSVEELI AMQLAYVKHL AETVAEEQVQ DVIITVPSYY SQCERDAVAD
     AVEIAGLRTL ALINDGTAVA VNYAMTRTFP APEYHVIYDA GASSIRATVV SFTPTGDTKS
     KSTGTQISAL GVGYDRRTGG TELDRRLREI LIDNFVSKHK RDIRTDKRGM VKLWKEAGRV
     KAILSANTDA TSTVESLAFD IDFKAKITRA QFEKACSDLQ GRFALPIRDA LADAGLTLNN
     ITSVILTGGS SRTPMIQTAV KEAVGEDKIA LNVNADEAVV LGAALHGASL SMQFKTKDIR
     VSDISTHDVQ ASYFATSPSS SARPRTISTL LFPSGSKYGT KKTLTFKRQE DFSIWLDYKK
     SILPGLPRDI LEAQISGVSE AIADLTERGA ADPVIKAVIS LSDSGFISVK EAFAYGELKD
     DSITGKLKSL FGGGTSTSEV GSSSIMSPPA ETPTPASTSA PDSKKEKQPS LKDLSTITLN
     VTVNLSSMPP MTVLEKKAAR DRLRNMDYQE MGKLRREEAR NSLEGYLYRV RDLLDDEIPD
     TPFKKCSKQS ERKAISEKLS ETITWLHSEG DDAETSQLRE KHNALETLEK PIIHRYQEIE
     AFPRALNNSQ MWNWSTRLFL TEARDNLTAE AKAGIQSKWT LEELDALETA LKEHETWLHQ
     WVEKQKSVKM YDDPVISTSE MKSRARILEQ HLQRLVKRKP AKVKKTASTK AEESGEKPQP
     TPGHDEL
//
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