ID   A0A2Z2NY84_9GAMM        Unreviewed;      1183 AA.
AC   A0A2Z2NY84;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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:ASJ76412.1};
GN   ORFNames=IMCC3135_31825 {ECO:0000313|EMBL:ASJ76412.1};
OS   Granulosicoccus antarcticus IMCC3135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Granulosicoccaceae; Granulosicoccus.
OX   NCBI_TaxID=1192854 {ECO:0000313|EMBL:ASJ76412.1, ECO:0000313|Proteomes:UP000250079};
RN   [1] {ECO:0000313|EMBL:ASJ76412.1, ECO:0000313|Proteomes:UP000250079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3135 {ECO:0000313|EMBL:ASJ76412.1,
RC   ECO:0000313|Proteomes:UP000250079};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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; CP018632; ASJ76412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z2NY84; -.
DR   KEGG; gai:IMCC3135_31825; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000250079; Chromosome.
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:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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: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; 2.
DR   Pfam; PF13361; UvrD_C; 2.
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:UP000250079}.
FT   DOMAIN          3..501
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          513..778
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          896..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         24..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1183 AA;  132243 MW;  8D884DD4E2EBAC3B CRC64;
     MSAPLDAAVR ARALDPQTSF IVQAPAGSGK TELLTRRILT LLQSVEEPEE ILAITFTRKA
     ASEMRQRVVE TLERANSGEP ASNVYEEEGL ALARDVLKRD AERQWQLIRN PQRLNLRTID
     ALATQLAHRL PVTSALGAPT GIVEDASALY RDVASRFIES NIDSMGLVLL QVGNRLEQAR
     QLLANLLASR DQWKRHVYGF GDNHDELRAI LESMLGELVE SRLDNLYALV PDVLIEGLPE
     RLHMACGFLL EDAEGDLSEL PEEMQGWLDL EELPGTSLED LSGWDGIGAA LLTKSGGLRK
     RLTKAEGFPA KGDAKKRGVE PALLVSHKEH MLELLERVAE SPEFIEALAE VCSLPYPRYR
     DEQWALLSQL LGVLPKLLLE LHMVFAERRV VDFTELAERA QRALGTEQEP TDLALSMDLS
     LKHILVDEFQ DTSQTQFRLF AQLVGGWEPG DGRTFFVVGD PMQSIYRFRD GDVALFAQAG
     DDGIGPVKLE SLTLSVNFRA APDVIKWVNQ IFASIFPKRA DADSGAVTYS PSDAHLTTDG
     GVQVHTLVNK ERFDEAELVA CLAAEALAID PQHTVAILVR TRSQAGDIFD ALRARSLAYE
     SIDMDQVGER AVVRDLVSLC LALRYPHDRL HWLSLLRAPF VGMTLNDLHA LMSESGREAT
     VIELLRDPAR LALLSADGQA RAARLLPILE PALKRASRGR LLPWVESVWL QLGGPVVCRD
     AVDRDAAERA LARLSSLEAD GRLWEKSVLT EVMKSLYAAN AEEGECRIQV MTLHKAKGLE
     FGTVILPALD RQPRGDSTQL LNWFESTLDG RPQLLLAPLE QSGLPPGRRD RINRLVRKAR
     ERCDEQEKLR LLYVACTRAR HHLHLIGRIR RNTEDQYQTP INSSLLKPLW PLLEPDLPTE
     DTHKSPEPIS PAPEEVSDTH KSLAEISDTH EPPGLPIESD PVSATVSSFE RLPVDVEMPS
     FVSFEWEKVA KKQEVDSESV KFSWAGRTAR DIGTVVHQQL QMLAQSADSL ANVDFDALGI
     IAERQLRNMG VQKEMLPQAT ETVLLAVRST LADERGRWAL SPHAEARSEW ALSVVQEAEE
     GDGDPEKFMG VWNREVRQMV IDRTFVDEQG VRWIVDFKTG DHQGGQVELF LDSEQMRYAD
     QLNRYADIIR RMDEGPVRVG LYFPLLKGWR EWEPPNREQG SKH
//