ID A0A1L8MLT5_9STRE Unreviewed; 830 AA.
AC A0A1L8MLT5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN Name=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN ORFNames=A9Q68_06565 {ECO:0000313|EMBL:OJF71645.1};
OS Streptococcus bovimastitidis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1856638 {ECO:0000313|EMBL:OJF71645.1, ECO:0000313|Proteomes:UP000182015};
RN [1] {ECO:0000313|EMBL:OJF71645.1, ECO:0000313|Proteomes:UP000182015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ1587 {ECO:0000313|EMBL:OJF71645.1,
RC ECO:0000313|Proteomes:UP000182015};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC Rule:MF_01488}.
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=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01488};
CC -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01488}.
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:OJF71645.1}.
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DR EMBL; LZDD01000002; OJF71645.1; -; Genomic_DNA.
DR RefSeq; WP_071793900.1; NZ_LZDD01000002.1.
DR AlphaFoldDB; A0A1L8MLT5; -.
DR STRING; 1856638.A9Q68_06565; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000182015; Unassembled WGS sequence.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 1.10.10.2220; -; 1.
DR Gene3D; 2.30.30.940; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01488; RecD_like; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR006345; DNA_helicase_RecD-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029493; RecD-like_HHH.
DR InterPro; IPR041451; RecD-like_SH13.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01448; recD_rel; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF14490; HHH_4; 1.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 344..532
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 748..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 830 AA; 93157 MW; 23950D21C289B500 CRC64;
MEYFFSGTID RIIFENASNF FKILLLEVED TDSDFDDFEI IVTGTMADVM EGEDYTFWGQ
LTQHPKYGQQ LKLSRYQKAK PTKSGLVKYF ASDHFKGIGK KTAEKIVSLY GDNTIDKILD
DPSQLETITG LSKSNREAFV NTLKLNYGTE LIIAGLVELG ISNHFAFQIY DAYKEEALER
VKSNPYQLVE DIQGIGFKLA DNLAAEIGIE SDAPERYRAA LLHSLLQESI SQGDTYIEAR
DLLEAAITLL EEARQIECDP ADVARELTQL IDDQKVYNVD TKIFDSSLYQ AEGGIQKNLD
RILDMPLEES IEESQISQSI EQIEEDLNIQ YDQVQKEAIR KALQSKVFIL TGGPGTGKTT
VIKGILQAYA SLHDIDLYKK DLPIILAAPT GRAARRMNEL TGLPSATIHR HLGLNGDNDY
QAIEDYLDCD LIIIDEFSMV DTWLANQLLS SISSRTQVII VGDSDQLPSV GPGQVLADLL
KVPQVPQIAL RKIFRQSQDS TIVDLANQMR QGYLPADFKE KKADRSYFDA LPQHIPTMVT
KIVAAAIKSG IDQDEIQILA PMYKGQAGIN NLNQLMQELL NPLDGKTEFF FNDTHFRIGD
KILHLVNDAQ LNVFNGDIGY ITDLIPAKYT ESKQDEIVMS FEGSEVSYPR NEWLKITLAY
AMSIHKSQGS EFQVVILPIT RQSGRLLQRN LIYTAVTRSK SKLIMLGEYS AFDYAIKNEG
DKRQTYLVQR FGLTSESEVD TLSAEKSVDS SAILPEKEKE TKRSVKPSEQ APSKRADASE
KEGLPQGENE KVDIEQVPEA GFRLTSENLL TIDPMIGLTE EDILIFFQKN
//
