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Database: UniProt
Entry: A7F897_SCLS1
LinkDB: A7F897_SCLS1
Original site: A7F897_SCLS1 
ID   A7F897_SCLS1            Unreviewed;       973 AA.
AC   A7F897;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=SS1G_13828 {ECO:0000313|EMBL:EDN98968.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN98968.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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DR   EMBL; CH476647; EDN98968.1; -; Genomic_DNA.
DR   RefSeq; XP_001585259.1; XM_001585209.1.
DR   AlphaFoldDB; A7F897; -.
DR   STRING; 665079.A7F897; -.
DR   EnsemblFungi; EDN98968; EDN98968; SS1G_13828.
DR   GeneID; 5481344; -.
DR   KEGG; ssl:SS1G_13828; -.
DR   eggNOG; KOG0742; Eukaryota.
DR   HOGENOM; CLU_004471_0_0_1; -.
DR   InParanoid; A7F897; -.
DR   OMA; FDWENKY; -.
DR   OrthoDB; 1379677at2759; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd19481; RecA-like_protease; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR46411:SF1; AAA DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR46411; FAMILY ATPASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT   DOMAIN          751..876
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..129
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..172
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..217
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..590
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   973 AA;  110096 MW;  9452C9AF72DFED6C CRC64;
     MDTPSSSKGS EQVNEREEPA TVVTGEGSST AQIEVKPRQA TEKQCKAKKS KKEKADKSYK
     SKSKKTKEVI ETESESEIDE SSDLDSTSSS SSDSDESETE TEKEKRKRKA KLKAKQKLKE
     KRKAKSKKKA KKDDTSDSDL TSDSESNSDN EDEEDGDDSG DAEADDDADE VVDVTNAQLQ
     AQLMQIQAQL QRSSLSHPPQ LPPVWNLPPP PAAPNSLPPG TRQHQALRRK LLLDERNQGK
     KIKNDKGKRK RGSKLEYKRV DQLWDSTIHN YKLTDTAEDE ESSEYDQYLF NVRRTFDWEG
     KYKATVVDIK SKLLKEALNE AMDGVKGVSL VEETPCIDPN LLFLYLEDLR KSCKQLKNKK
     ITEKKGKKKL KKRNETKRKH LKVLLKYLDK DYASTKKTLY PMLETGIITF DLLWALYKPN
     TLAYTTTYGT IDEPRAFKIE LAEKNISFMK GTWYNIEGKY LEYDGKTWGM GTMDCDVPAF
     KGARKITSLN CYPLKYHKNE AKLRTELIER GKKFVALQGV HYKSHKGMAY YKKRKSIVKV
     NIDGRVMVDP AIHRRILPNY NVSTVKPNDP DLIDDSDSED YECGCCGDDD SDDGQGDRGD
     RGLEKREDND EPKMKLKVVL DEKEKPHLVS VPVDEDGNEV VVEKLDEVPS KITNKDNKDE
     TTQAEDDKKS LPIFTDEEYL IASPVVLGFA FAEKLWLEFT VSGIKDIVWN EGAYDSLVLE
     DNTKAIVKAL VESHKYHPAE SIDDVIQGKG KGLVAVLHGP PGTGKTLTAE GISELLKCPL
     YMVSAGELGT DPRTLEAELQ KILDIAHAWG AVLLLDEADV FLERRTIQDI HRNALVSIFL
     RLLEYFQGIL FLTTNRVETF DDAFQSRIHI ALRYGDLSPK AKKSVFKMFI ERVRVLEGID
     TMPFTEEDYN ALARNNLNGR QIKNTIRTAQ ALAVNNKEPL SMEHIKRVLD VSNAFDRDLK
     GGTGFEDAMR GYF
//
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