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
//