ID L0D6T0_SINAD Unreviewed; 1211 AA.
AC L0D6T0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=DNA/RNA helicase, superfamily II, SNF2 family {ECO:0000313|EMBL:AGA24575.1};
GN OrderedLocusNames=Sinac_0117 {ECO:0000313|EMBL:AGA24575.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA24575.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA24575.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003364; AGA24575.1; -; Genomic_DNA.
DR AlphaFoldDB; L0D6T0; -.
DR STRING; 886293.Sinac_0117; -.
DR KEGG; saci:Sinac_0117; -.
DR eggNOG; COG0553; Bacteria.
DR eggNOG; COG4715; Bacteria.
DR HOGENOM; CLU_000315_21_0_0; -.
DR Proteomes; UP000010798; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016787; F:hydrolase 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; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
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; 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; 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; PS51193; HELICASE_ATP_BIND_2; 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:AGA24575.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 48..86
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 766..926
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 865..1211
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 1050..1198
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 101..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 132810 MW; D3F5D033F9D43F9F CRC64;
MGIAQKVSRV FSDAVRSRGQ SYFAKGRVAL TSSTPGEVIA RVRGTAKYRV RLRIRGIKLH
IACSCPYFGP FGEPCKHIWA TILMTDARGL LPAAPVRPLK LVSDMPRRPT SPEGGGPPPG
HRAVPGPGYG PGPGSSYGPN PGSGYGPNSG ANRSPGPGVG PSPNRGPGPG ASSRSPGAGR
GPGSGPPGRG PGAGPPGRGP GPGYGPGAGR GTGPGRAPGL NHGPGPGGPG PGPEGQQRPG
GRYRKERPVR GGVPQPWSAG KEAGSTARAK PVNRNSKRLL VYVLDVSSTL NQNQVVIDLA
RRQRRPAGDW GPLKPWWHAP GSPHAKYEPE DRDLLALLEE TQAAAVANGA TMGDPMMGTR
RYVLRSNQAL IVEKLAKSGR LRLRRTEGED DPPTMRWDDG PAWRFSLDIR PELGGKRWSW
RGSLRRGDGR TDRMDLAEPL VLVPGLVIQG VGRASRFDDV GVMPWIVRLR HEKEIVFAEP
QQDIMIGRIL AEARVSPAEL VETIQFEEID TPPRPCLTLR TPRQNWGPGS DRLLAELEFD
YNGALIPAGR TTPLAVSTEL GLIIRRNPQV EAQADILLFE LGFRESKDPR VEPGTMELPP
KRMGQVTRDL VQVGWRVEAE GKLIRPAGEF KLAVTTGIDW FELGGQVDYG DQSLSLPELL
AAVRRGDSMV TLGDGSMGML PEEWLKKYGM LVDLGTSEDG HLRFGNAQAG LLDALLAAQP
EIRVDSAFEK VRKSLHKFEG VQPVDAPAGF HGELRPYQRE GLGWLDYLQK FDFGGILADD
MGLGKTIQVL ALLQKRRARR LAKGPSLAVV PRSLVFNWIQ EATKFTPRLK VLDYTGPARH
ALRESFSSHD LVITTYGTLR TDIAELSQLD FDYVILDEAQ AIKNADSQAA KAARLLRGRH
RLAMSGTPIE NHLGELWSIV EFLNPGMLGA SSVFKKHTGS GGNLDDSDRS LLAKSLRPFI
LRRTKAEVVK DLPEKTEQTL HCDMEPAQRK LYEELKAHYR LALLRKETSE LNRSKIEVLE
ALLRLRQASC HPGLIDPTRT AEPSAKLDML LPQLSEVVEE GHKTLVFSQF TSFLAIVKDR
LDKEGLRYEY LDGRTRNRAD RVERFQNDPD CPIFLISLKA GGLGLNLTAA EYVYLLDPWW
NPAVEAQAID RSHRIGQTQR VFAYRLVCRD TVEEKILELQ QKKRDLADAI LNADKSLIQT
LSREDLEFLL T
//
