ID A0A3A9Z839_9ACTN Unreviewed; 804 AA.
AC A0A3A9Z839;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN Name=pcrA {ECO:0000313|EMBL:RKN44455.1};
GN ORFNames=D7223_19605 {ECO:0000313|EMBL:RKN44455.1};
OS Micromonospora endolithica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=230091 {ECO:0000313|EMBL:RKN44455.1, ECO:0000313|Proteomes:UP000281726};
RN [1] {ECO:0000313|EMBL:RKN44455.1, ECO:0000313|Proteomes:UP000281726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12677 {ECO:0000313|EMBL:RKN44455.1,
RC ECO:0000313|Proteomes:UP000281726};
RX PubMed=15046305; DOI=10.1078/072320204322881781;
RA Hirsch P., Mevs U., Kroppenstedt R.M., Schumann P., Stackebrandt E.;
RT "Cryptoendolithic actinomycetes from antarctic sandstone rock samples:
RT Micromonospora endolithica sp. nov. and two isolates related to
RT Micromonospora coerulea Jensen 1932.";
RL Syst. Appl. Microbiol. 27:166-174(2004).
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 ECO:0000256|RuleBase:RU364053};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|RuleBase:RU364053}.
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:RKN44455.1}.
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DR EMBL; RBAK01000007; RKN44455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9Z839; -.
DR OrthoDB; 4812256at2; -.
DR Proteomes; UP000281726; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
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 NCBIfam; TIGR01073; pcrA; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
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}; DNA-binding {ECO:0000256|RuleBase:RU364053};
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}; Reference proteome {ECO:0000313|Proteomes:UP000281726}.
FT DOMAIN 41..325
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 326..612
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 804 AA; 88599 MW; C54DF411651B6DA6 CRC64;
MHPLFDIPVS PPAPESAPEP ARTPPRRPGP SAHLDPRQLV DGLNGPQRDA VTHSGSPLLI
VAGAGSGKTR VLTHRIAYLL AARDVHPGEI IAITFTNKAA GEMKERVAHL VGPRARLMWV
STFHSACVRI LRAEHEHAGL KSTFSIYDAD DSRRLMQMVT RELDLDPKRY PARGLAAQVS
NLKNELVDPE EFAGRAKGPN ERALAEAYTL YQRRLREAHA LDFDDLIMTT VHLLQSRPHV
AESYRRRFRH VLVDEYQDTN HAQYVLIKEL VAGTEGLEPA ELCVVGDADQ SIYAFRGATI
RNILEFERDF GDARTILLEQ NYRSTQTILN AANAVIDRNT SRKPKRLWSE AGAGEPIVGY
VADTEHAEAD WVGREVDRLV DEGDTRPADV AVFYRTNAQS RVFEEVFIRV GLPYKVVGGV
RFYERKEVRD ALAYLRAVVN DDDTVSLRRI LNTPRRGIGD RAEACVEALS SRDRISFGAA
LRRAKEAPGI STRAANGIGE FVALLDGARE LADTGTPEEV LEALLTRSGY LTELEESLDP
QDAGRVDNLQ ELVSVAREYT ERVEATGADG ERATLAGFLE QVALVADADQ IPAEDPDHQG
VVTLMTLHTA KGLEFPVVFL TGLEDGVFPH LRSLGDTREL EEERRLAYVG ITRARQRLYL
SRAVTRSAWG QPAYNPPSRF LEELPTELVR WERTEGSYTS WAGGGGGVGG RADRVSGGRG
GFTGGTPRAE QLARRIGVDA SRLTTASELP QGPKVAVGDR VNHQRYGLGR VLAVEGHGPG
ARAQIDFGDQ TMWLVLRHAP IDKL
//
