ID A0A146G7N8_TERSA Unreviewed; 672 AA.
AC A0A146G7N8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=TSACC_22143 {ECO:0000313|EMBL:GAT33725.1};
OS Terrimicrobium sacchariphilum.
OC Bacteria; Verrucomicrobiota; Terrimicrobiia; Terrimicrobiales;
OC Terrimicrobiaceae; Terrimicrobium.
OX NCBI_TaxID=690879 {ECO:0000313|EMBL:GAT33725.1, ECO:0000313|Proteomes:UP000076023};
RN [1] {ECO:0000313|Proteomes:UP000076023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT "Draft genome sequence of Terrimicrobium sacchariphilum strain NM-5.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT "Draft genome sequence of Terrimicrobium sacchariphilum NM-5(T), a
RT facultative anaerobic soil bacterium of the class Spartobacteria.";
RL Genome Announc. 0:0-0(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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:GAT33725.1}.
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DR EMBL; BDCO01000002; GAT33725.1; -; Genomic_DNA.
DR RefSeq; WP_075079425.1; NZ_BDCO01000002.1.
DR AlphaFoldDB; A0A146G7N8; -.
DR STRING; 690879.TSACC_22143; -.
DR InParanoid; A0A146G7N8; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000076023; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF3; ATP-DEPENDENT HELICASE_DEOXYRIBONUCLEASE SUBUNIT B; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 20..304
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 305..574
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 672 AA; 75586 MW; 803F29464D7C6162 CRC64;
MARHYQLDPT SAGPATDFAA ELNEQQLAAV TAAPGPSLVI AGAGSGKTRT LTYRVAWLLE
QGTAPRNILL LTFTNKAARE MLERVGALSQ SAAEGIWGGT FHSIGNRILR RNAERIGFRQ
GFTIMDREDQ EEMIESIVAR EGLRTNDRRF PKGEVLADIF SYSINTGAPI SQVVATKYRY
FMPLIAQIER VQVAYEGRKR EANSLDFDDL LSKTLELLQM CEDVAAQYQQ QFQHILVDEY
QDTNRIQAEL VDWLGRKHGN IMVVGDDAQS IYSWRGANFA NILDFPKRYP TAQVFKIETN
YRSVPEVLNV ANASILGNER QFPKNLAPVR TSYPMRPALV PLSTNNQQAT FLAQRILELH
EEGVRLNEIA VLYRAHFHSM EVQLEFTRRG IPFSITSGLR FFEQAHVKDV SAFLKFATNP
RDEVAFKRMV KLLPGVGAKS AESIWSQTSD VLDGGTEFGR LHGLKVPSKS AKNWEQLVHT
LAELAPDGSI LAPSTMIDSV LFAVYDDYMK SKFANYEARR EDLNTLAGFA RQFESTEEFL
SQLALLGAVE TTDALAVESE SEKVTLSTIH QAKGLEWKVV FLIWLTEGMF PSSRSAETDE
GIEEERRLFY VGVTRCCDEL YLTYPDLRLN AGYGEALQRP SRFLTEIPEE LVEGWEVSAS
RQKEPTSDDE PF
//
