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Database: UniProt
Entry: M3C541_SPHMS
LinkDB: M3C541_SPHMS
Original site: M3C541_SPHMS 
ID   M3C541_SPHMS            Unreviewed;       991 AA.
AC   M3C541;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Actin-like ATPase domain-containing protein {ECO:0000313|EMBL:EMF15391.1};
GN   ORFNames=SEPMUDRAFT_147294 {ECO:0000313|EMBL:EMF15391.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF15391.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF15391.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF15391.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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DR   EMBL; KB456261; EMF15391.1; -; Genomic_DNA.
DR   RefSeq; XP_016763512.1; XM_016904204.1.
DR   AlphaFoldDB; M3C541; -.
DR   STRING; 692275.M3C541; -.
DR   GeneID; 27901341; -.
DR   eggNOG; KOG0104; Eukaryota.
DR   HOGENOM; CLU_005965_5_0_1; -.
DR   OMA; SRTPMIQ; -.
DR   OrthoDB; 5491443at2759; -.
DR   Proteomes; UP000016931; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..991
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004032305"
FT   REGION          598..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          783..810
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        623..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..930
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   991 AA;  107439 MW;  E0196651231D79FE CRC64;
     MIASQRAGAL SPLTICLAVL LLLASTASAA VLGIDFGTLN IKAALVKPGI PLDIVLTKDS
     KRKETAALAF KPTRDEKNNI VAKEGSFPER AYGGDALALQ GRMPGEVFPN LKQLLGLSTQ
     QAAERVATYK QRYPAVQVEH VESLGSSVFK SAAFPSEHPP YSVEELIGME LANIKRNAEL
     MAGKGTPVND AVITIPTFYT ADEKRAIVHA AYYAGFNVLG LISDGLAVGL DYAKTRTFPD
     ITKGESPEYH LVYDMGAGST TASVLRFQSK SVKDYGKHNK TVQEVTVQGV GYDRTLGGDA
     LNHVILDDFV AQLLAKSDVQ SRGITEADIR SNGRAMARFW KEAERVRQVL SANSETSAGF
     EEILPDIDLR VKLNRSDFEK MTAEYAARVA TPLERALEMA KLTSKDLKSV ILHGGAIRTP
     FVQSRLEAVV DDKAKLRSNV NPDESAVFGA AFKAASLSPS FKVKEIRDSE AAVYPASLVY
     QDNGKERKQG LFTPTSQAGS GATVKQVTFK DREDFSFGFI QNVEGLDRPI LSVKVDNLTA
     SVDELKTKYG CEKDDMVTRF SVKLNANFAL PDVLTGSVGC EVDDSVKSGS VGDSVKGWLG
     LGKKKDQEPL TDDEDDSPVE EVHATVSSAS GSTQASSSTS ASAETTSSPP KKRIEVVMLK
     FSTLPLGNVQ PEAAQIQRLV ERLKEFDASD RARTARDEAQ NVLESYTYSV RDFLENADFG
     AVSTASQREA ISTLLQTTKD WMESGEPGKA TTEILKEKYQ ALKDLVDPIK LRRTEHTQRV
     TLVPALQKSL EKAKKSIAKY QDKIDKAKAA LTASSSSTSS ETPSASSDLD DLEEADTSSK
     AAPKATDEPS PLINLDLTSV QSKYDEISSW LAEKLAAQEK LKPFDDPVLL VKDIERRSTE
     LGDAVADLVR RASVKPVVKK PPKPKASPKP KASKKTGSDE STPQEPQPAD TPEAEGEKPV
     KGGESMEDME DWLNKAKEKT KDSEVPPRDE L
//
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