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Database: UniProt/TrEMBL
Entry: R4S123_PHYAS
LinkDB: R4S123_PHYAS
Original site: R4S123_PHYAS 
ID   R4S123_PHYAS            Unreviewed;       713 AA.
AC   R4S123;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=pcrA {ECO:0000313|EMBL:AGL90438.1};
GN   ORFNames=SLY_0519 {ECO:0000313|EMBL:AGL90438.1};
OS   Strawberry lethal yellows phytoplasma (CPA) str. NZSb11.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Phytoplasma; 16SrXII (Stolbur group).
OX   NCBI_TaxID=980422 {ECO:0000313|EMBL:AGL90438.1, ECO:0000313|Proteomes:UP000013941};
RN   [1] {ECO:0000313|EMBL:AGL90438.1, ECO:0000313|Proteomes:UP000013941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZSb11 {ECO:0000313|EMBL:AGL90438.1,
RC   ECO:0000313|Proteomes:UP000013941};
RX   PubMed=23915186; DOI=10.1186/1471-2164-14-529;
RA   Andersen M.T., Liefting L.W., Havukkala I., Beever R.E.;
RT   "Comparison of the complete genome sequence of two closely related isolates
RT   of 'Candidatus Phytoplasma australiense' reveals genome plasticity.";
RL   BMC Genomics 14:529-529(2013).
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}.
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DR   EMBL; CP002548; AGL90438.1; -; Genomic_DNA.
DR   RefSeq; WP_015637985.1; NC_021236.1.
DR   AlphaFoldDB; R4S123; -.
DR   KEGG; nzs:SLY_0519; -.
DR   PATRIC; fig|980422.3.peg.476; -.
DR   HOGENOM; CLU_004585_5_2_14; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000013941; 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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_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:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
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          10..291
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          292..583
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   713 AA;  83682 MW;  354E51BEAF98FB4E CRC64;
     MSSKIDSWLK KLNKNQVEAA TSKSLATYLL AGAGTGKTTT LTTKIAYLIE KQNFLSKNIL
     TLTFTNKAAD QMKNKILEMI GEKSKGVNIL TFHALGNRIL RQFINILPFN YNRNFIILND
     KECNQILKIV AKEVNFDIQK VENIDNLRKE VFRLKKKTNE FLQHQQTSTQ NNNPLIVKIK
     NQYQKYLQKN NLVDFNDLIL YTYQLLKEYP EIKQFWQKKF QYILVDEFQD TDFYQYQILT
     FLTEKNPCIF VVGDPDQNIY SFRGACFGNS QLFLNKFNPQ IYVLKQNYRS SENILEKANL
     LISYNKDHPF KKKLNSVKGK GTKVNAHFFV DSRIEAQYIV QKIKHLVQIY HYNYRDFAIL
     YRVNSLGHFL EKYLISAGIP YMFLGNLSFY QKKVVKDFLA YLHLAVNPLQ DFYLRRVINV
     PKRQIGKITI TCLEKIVQEK ERSFFEILKD YKDIPVSDKT QKQLYQFYCL IEELNNKIIN
     NEFEKLSDII TYVDQKTQYS YQISLETQKN PQKSNEEQSS LVAIEELKSI LNQIDESFQG
     SNLQKINNFL EEVSLNNETK INNSSGNKAN NRVKLATIHK VKGLEFKVVF LAGLEKEFFD
     DLDDIQESRR LTYVAVTRAQ EKLFLTGVSQ RMLFGKNFSH EPSVFFKEMG FGSRKNYFLS
     QTQKPFQKGD QVRHNLFGLG IVLELERNNI IVEFVNPKKT KMFENSFKYL QKI
//
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