ID F4QIP5_9CAUL Unreviewed; 1174 AA.
AC F4QIP5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN Name=addA {ECO:0000313|EMBL:EGF91804.1};
GN ORFNames=ABI_02360 {ECO:0000313|EMBL:EGF91804.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF91804.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) 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};
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DR EMBL; GL883077; EGF91804.1; -; Genomic_DNA.
DR RefSeq; WP_006270970.1; NZ_GL883077.1.
DR AlphaFoldDB; F4QIP5; -.
DR STRING; 715226.ABI_02360; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_0_0_5; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000006512; 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; IPR014151; DNA_helicase_AddA.
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 NCBIfam; TIGR02784; addA_alphas; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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 Pfam; PF13361; UvrD_C; 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}.
FT DOMAIN 10..488
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 505..804
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1174 AA; 130307 MW; DAB83C4080DB9933 CRC64;
MNAVNPQNPN PQNPNPQNIA ADPKASCFLT ANAGSGKTST LVNRVARLLL SRADPAHILC
VTYTKAAAAE MQERLFQQLG GWAVADDEQL IGDLERIGEP THDLPRARAL FAKALETPGG
LKIQTIHAFC EKLLRRFPLE AQLSPAFKVL DDLLADDLAD KASTAVLTLD APGLEAVAET
RDRLIRKLKV MGFEKLLGQF IHQHDALQER FRHLENQSED WQSALFHSLG LDGVCTSQEC
LDAYANTLEW HLLEDLGQTL LSGTTATNQK AGQAFLDLYE SKISGRPFEF EEIRGIFLTQ
AGTLRKSIYT KGTAPADARY LDRMAEEAVA LADRLKAVEI ASNTLDALRL FEIFSFVYLS
EKRGEGALDF TDLITYTKKL LDDPTHALWV LHKLDGGLDH ILVDEAQDTS EEQWIIVDAL
SSDFFSGEGV TRTIRTLFAV GDEKQSIYGF QGADPREFLK ARGQISQRAH DGGANLVEPQ
LIDSWRSLPE ILGFVDAVFK ADDVQHALNF SSDPIQHIAR RSDASGVVEL WPVVRPMAAV
ETTADDDDEQ AALDDPGRNP PSKRLAKQIA ATIRSEITAG RTIYDKALKR RRTVHAGDVL
ILVRKRDHLF EHIIRELKIA GVAVSGADRL KLGDHIAFQD LRALLRVCLQ PMDALSLACV
LRSPLCDLSE QDLFDLAHDR QMPLWSALLH HPATEGPVHD ARIFLLWAQK AAWQLTAFDF
LARVLNRRDF AGRSVRQRFL TRLGDECEDV LDETLALALK GEGSGAVALS ACLDLFEFQA
SQIKREQEEG GHAVRVMTVH GSKGLEAPWV IVPIGPQYGA RKEDLILTGE DGQMYLCAGG
KKADTAVTAD IRDGRALREE QESLRLFYVA LTRSRDRLTV CAYTGTKPAT TGNFPSWYDL
ASDAFDRLET TSEVMPLVNP FDDGEYYNEA LVRVHGQHSE ALTAQARLRE PEVPLPDFAL
AMVTHDDIET ERWAAISQMG DEDRTETEIA PSPLQTLGSL GRYRRGNLIH KLFEILPDIA
PDNRMAIAQR YLTRQADLTD AQREEMTDAV MTVLTDARFA EAFGPQSRPE VALAGQVGVN
PRGEAIMLSG RIDRLVVTDD RVVIIDYKSN RPAPDRAEDA AVAYQRQMAG YVALLRQVYP
DRAVEAALLW TDGPRLTPMP ETLVQLRLEE ILSR
//
