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Database: UniProt
Entry: F1A199_DICPU
LinkDB: F1A199_DICPU
Original site: F1A199_DICPU 
ID   F1A199_DICPU            Unreviewed;      1044 AA.
AC   F1A199;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=SNF2-related domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DICPUDRAFT_158303 {ECO:0000313|EMBL:EGC30034.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC30034.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
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DR   EMBL; GL871365; EGC30034.1; -; Genomic_DNA.
DR   RefSeq; XP_003293445.1; XM_003293397.1.
DR   AlphaFoldDB; F1A199; -.
DR   STRING; 5786.F1A199; -.
DR   EnsemblProtists; EGC30034; EGC30034; DICPUDRAFT_158303.
DR   GeneID; 10511362; -.
DR   KEGG; dpp:DICPUDRAFT_158303; -.
DR   eggNOG; KOG0389; Eukaryota.
DR   InParanoid; F1A199; -.
DR   OMA; IGLNWMA; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10799:SF964; SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD/H BOX 1; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT   DOMAIN          461..631
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          873..1036
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..68
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..386
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1044 AA;  120232 MW;  CB7DAC55C45C3393 CRC64;
     MVVLENRRTR IQRTDISKSF IKNESEEEEE IESNDDSDYE DQAEESEESE SEHLDLDESE
     DDNSDEDYSD GESIKKNSKK PPSSRSKPTA KPTVVKKTTN GKKLAAKDSD DDSDDFCLPK
     SKKKTTVDKE KELMESKLVY EQTLKQASMD QWILKKPNNE KEKTEPSRFF SFAKKSSTTT
     TTSTAATTAA ATTTTTSPNK TNNGTPQILR LASIKNTHRP LGMGNSSEKN DFFSNFLYNK
     STGKSKEESI KIEDEGEKIE EEEKENKKEE EEDDSLFGKG FNSPKFNATS VKNHVQKMVK
     DSLSESDTED EELPLVNKKR KEGKDASQQK KTMVIEISDK EDDSDTEEES EPKSKNKKSV
     TTTIDSDNET VEIPDEEEEE EGSRNIDDEP TIEKLIYACE CFSKRMLEIL SNSDLEEKKL
     TTTTTTSINK KTTDKNKLIT QPKTINKTMR NYQLIGLNWM AVLYKENING ILADEMGLGK
     TVQTISVLAH IMETYNDCGP HLIIVPATVM SNWGRELETW CPTLKVIRYY GNIKEREELR
     YDIRKMKPKK DFHIILTTYN LLFSNLDRAF LKKFDYSYLI LDEAQNIKNS DSRRYKNIFK
     IQSKHRLLLT GTPLQNNLYE LWSLLNFLMP HIFGSTSKNN YLLNQLLEYK GDDSDSALSR
     MKKILSPFIL RRLKSTVSKE LKPKKEIIER CVMPEFQQNT YNTVIKRSKA QWANRDLIKQ
     KEDTKKRKKK STSLLDPDCD LLDLTIDDSV VENGNGEEKL TAKQKELAKQ IKQGNGSFVL
     NNILMQLRKA SNHPLLCKNI FYTEEQIDDI VKTLARNDKE WIEYRYDVPA LKELFQSFSD
     YEVFKNICEN PLLADKYWID DEQFYETSAK CIKLKEILQK EIHENKSKVL IFSQMTKVLD
     ILEDVLSIFG ESFTRLDGQT PVNERQDIID HFTNSKDIPV FLLSTNAGGL GINLTCANVV
     IFYDLSFNPQ VDRQAEDRAH RLGQEREVIV YKLLTENTVD IDIFNSANEK KKLNDNILEE
     GTYTEKETKL ESKKILKILD SIFT
//
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