ID A0A2T6DLV6_9BACT Unreviewed; 1197 AA.
AC A0A2T6DLV6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=DB346_06070 {ECO:0000313|EMBL:PTY03447.1};
OS Verrucomicrobia bacterium LW23.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=2161867 {ECO:0000313|EMBL:PTY03447.1, ECO:0000313|Proteomes:UP000244158};
RN [1] {ECO:0000313|EMBL:PTY03447.1, ECO:0000313|Proteomes:UP000244158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW23 {ECO:0000313|EMBL:PTY03447.1,
RC ECO:0000313|Proteomes:UP000244158};
RA Buenger W., Mueller J., Hurek T., Reinhold-Hurek B.;
RT "Genomic and phenotypic characterization of four novel plant-associated
RT Verrucomicrobia indicate a new subdivision with one cultivated member.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:PTY03447.1}.
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DR EMBL; QAZA01000011; PTY03447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6DLV6; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000244158; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000244158}.
FT DOMAIN 16..459
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 504..782
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 518..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1197 AA; 131614 MW; 0E6D5F76D43DC74C CRC64;
MTESNLTPEP PRPGQPVDQP ERERFIYGLD RNFSVIAPAG VGKTRSIVER IAAIAAQPDA
VQVLPHLVVV TYTDRAAREM KRRARQRILQ LQSVAGQSHA EAADSSATPA PAISPAAVAA
FNQTFFGTIH SLCVKLLQTH GHFLGVPAKF EVADDDRLDE LWDEFISNDI PWQHSLSEAE
RTAMLRHIGL LDVFRLSREV RLPLPEPLEP PGPVPAVPLD ALIAELQASN SKHDTVADTL
SNAQRFQRQM DRAAKDVKRS VTAPASPAFD AINHNLDQPL PGEVFCPLPE RKTKAKALAT
MWDDTFRPLR DWLSRAATVA AVEIAEAFVQ FRIRQGVLTF DDQVSLALEL LSTPEIAARI
LKKPWRIILD EAQDTDPIQF QVLLRLARVL GAELKEGTSD VPGTSHVPAD AWRWAMVGDF
QQSIYGQRAD IPTYRQHHLE ITTAPNGAQA TFQVTFRCSQ SVVGFVNTVF PHVFAPKEDT
KQPGASGAAA ATLDDQARFV QLMAAATTAQ GQVLRLPVAA LPEPEHRETP DGRPSKRRRK
DAEVASHVAE HVAHSIQTLG LEGLQASRWS EVAVLCPRIA WLAPIRKALA ARGIDSQSLS
THDIAGDHPA RAWLTALVWV MAEPLSGYEI VGVLRDIFGL PDHVLASFSG GDGARFQIAS
APQTIALTRD TAALPVRDAL VFLAGLREKI ATMPVRTAVE LILSETQLLE RLELLPDVRD
WPGGSMRDEL EALLVLAAHA EAAGTTFRGY AHNLRNSFGT ARSETRIKPD AVQLITSYKA
KGLEWDAVVI PFMFREIQMR TKHYPRFTQL SPGQNPRVIF SRDDTREPER AAADRIRDME
YERLLYVMCT RPRRTLVLTD DSACWAEPKY NKAAETMQRT FARCMRLDKV PEVQQLWDAL
PLAPALSADE IPAPAPSESS ASAGRAALSA PVSAPGAGRP AHFETAQTLP LFQHARDQWE
RRRELASRTA GGFRRRVTPH SLAKSLEVLG PLPGSQQGHS MSPGQDVSLP VSVAPGDPES
SSEPEDARPL NAERPGGTEY GTWWHALMER LPWSGPESGA AARLAAFEAA LPLCQLPERA
RREFDLLQQS ELPARLAAPG LVLHAELPFL LAETATPEAC LEGIIDMAWF DPASDRWTVL
DWKTNFIRAE QSEELRQLYM PQLQAYARAL TRLTGKGASA VIYSTTLGVL LSADVAE
//
