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Database: UniProt
Entry: A0A139P996_9STRE
LinkDB: A0A139P996_9STRE
Original site: A0A139P996_9STRE 
ID   A0A139P996_9STRE        Unreviewed;      1037 AA.
AC   A0A139P996;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=SWF/SNF family helicase {ECO:0000313|EMBL:KXT84732.1};
GN   ORFNames=STRDD11_00797 {ECO:0000313|EMBL:KXT84732.1};
OS   Streptococcus sp. DD11.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1777879 {ECO:0000313|EMBL:KXT84732.1, ECO:0000313|Proteomes:UP000070514};
RN   [1] {ECO:0000313|EMBL:KXT84732.1, ECO:0000313|Proteomes:UP000070514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD11 {ECO:0000313|EMBL:KXT84732.1,
RC   ECO:0000313|Proteomes:UP000070514};
RA   Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA   Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT   "Highly variable Streptococcus oralis are common among viridans
RT   streptococci isolated from primates.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT84732.1}.
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DR   EMBL; LQRF01000081; KXT84732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139P996; -.
DR   STRING; 1777879.STRDD11_00797; -.
DR   PATRIC; fig|1777879.3.peg.878; -.
DR   OrthoDB; 9760715at2; -.
DR   Proteomes; UP000070514; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR013663; Helicase_SWF/SNF/SWI_bac.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PANTHER; PTHR10799:SF1020; BTAF (TBP-ASSOCIATED FACTOR) HOMOLOG; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF08455; SNF2_assoc; 1.
DR   Pfam; PF04434; SWIM; 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.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:KXT84732.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          39..74
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          598..755
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          867..1025
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1037 AA;  119256 MW;  4EE77DEB79467516 CRC64;
     MAKLIPGKIR TEGIALFESK KVVILEVRDS LLYARVDDFN LRYSLDDDVI FCSCDFFKKK
     KYCAHLAALE YFLKNDPSGK DVLDSMEKKE STSQETQKLV SIGSLFLDKI LPEKREQEVR
     YELSATGQED SYTGQFLWSL RISRLPDERS YVVRDILSFL RTLDKGGHYQ IGKSYYEPIH
     MENFDEASQD LIEFLQGLTE DYQGQDASLV FPNAGRNLYF PASLFEEGVT RLMNLASFRL
     DYSLYDYAEV FFQDLHEEAD IYHFQVEADE EYFELAIAEK HYKLLYDGRY IFYGDTFYQL
     NQQQIKLVKA LRELPLEQDR MKRLQFDLTE QSKLASSLGD FRTVGRVEAP ERLIIHDFQA
     SFAFGLGQDQ RLILDVAFDY GDRTVTNRRS LERLPFASNF EQEQRIFREM LSAGFIADFY
     SQRPPLRPEE IYHFFSAVIP RFEALGQVSL SEELQALSHV EQPAISINMT GGLLEIGFDF
     AGIDQSEIDA VLDSLFGEQD FFISKNGQVL IFDEETKRIS RTLQNLRSQS SKNGVIQAHS
     LAAYHLSEFF KGKDRVQFSQ DFQQLAYDLT HPETFALPAV KVKAELRDYQ ETGIKWLSML
     DKYGFGGILA DDMGLGKTLQ TISFLSSRLD QSKRVLILAP SSLIYNWSDE LAKFAPDLDV
     AVVYGLKNVR DELIAQNRQI TITSYASFRQ DVEEYRGLRF DYLILDEAQV MKNDQTKIAQ
     YLRDFEVAHT YALSGTPIEN HLGELWSIFQ IVLPGLLPSK REFLKLPPET VARYIKPFVM
     RRKKEDVLQE LPDLIEVTYR NELADSQKTI YLALLKQMQD RIMQATEDEL NRSKVEILSG
     LMRLRQICDT PQLFMEDYQG ESGKLESLRE LLEQIQDGNR RVLIFSQFRG MLDIIESELN
     TLGMDSFKIT GSTPAKERQD MTTAFNQGQR SAFLISLKAG GVGLNLTGAD TVILVDLWWN
     PAVEAQAIGR AHRIGQERNV EVYRMITRGT IEEKIQELQE NKRNLVSTIL DGSETRSSLS
     LEEIREILGI SAESLEK
//
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