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Database: UniProt
Entry: E9T5I8_RHOHA
LinkDB: E9T5I8_RHOHA
Original site: E9T5I8_RHOHA 
ID   E9T5I8_RHOHA            Unreviewed;       824 AA.
AC   E9T5I8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
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:EGD22598.1};
GN   ORFNames=HMPREF0724_13816 {ECO:0000313|EMBL:EGD22598.1};
OS   Prescottella equi ATCC 33707.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Prescottella.
OX   NCBI_TaxID=525370 {ECO:0000313|EMBL:EGD22598.1, ECO:0000313|Proteomes:UP000004245};
RN   [1] {ECO:0000313|EMBL:EGD22598.1, ECO:0000313|Proteomes:UP000004245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33707 {ECO:0000313|EMBL:EGD22598.1,
RC   ECO:0000313|Proteomes:UP000004245};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-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,
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:EGD22598.1}.
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DR   EMBL; ADNW02000018; EGD22598.1; -; Genomic_DNA.
DR   RefSeq; WP_005514855.1; NZ_CM001149.1.
DR   AlphaFoldDB; E9T5I8; -.
DR   STRING; 43767.A6I91_12215; -.
DR   HOGENOM; CLU_004585_5_2_11; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000004245; Chromosome.
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; 2.
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; 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}; 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:UP000004245}.
FT   DOMAIN          32..324
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          325..634
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   824 AA;  89280 MW;  2E42B367FA09E7B8 CRC64;
     MNTISGSTLG IPGHSQGGSQ GGSRGPADAL LEGLNPQQRE AVLHAGSPLL IVAGAGSGKT
     AVLTRRIAYL LAERGVMPGQ ILAITFTNKA AAEMRERVAQ LVGPRANSMW VSTFHSSCVR
     ILRAQAGLLH GLNSNFSIYD ADDSRRLLTM ISKDLEIDTK RYSARLLATK ISNLKNELID
     PEEAAADADR DSNDLDKLVA RVYAHYQQRL RAANALDFDD LIGETVGLLQ ANPQVAEYYR
     RRFRHVLVDE YQDTNHAQYV LVRELVGEES DDPYAVPPGE LCVVGDADQS IYAFRGATIR
     NIEEFERDYP DARTILLEQN YRSTQNILSA ANSVISRNTG RREKRLWTDS GEGELITGYV
     ADNEHDEAQF VASEIDRLVD AGETKFGEVA VFYRTNNSSR ALEEIFIRLG IPYKVVGGTR
     FYERKEVRDI VAYLRVLANE DDTVSLRRIL NTPRRGIGDR AEACVSVYAE QKGVGFAEAL
     RAAGEGSVPL LNTRSQKAIA SFLELLDGLR ALMVSTDADG NDLTDIGEVV EGVLDRTGYR
     RELEVSSDPQ DGARLDNLNE LVSVAREFSS DARNAAAFAE ENAAEGDVVE DEGQPDPGSL
     AAFLERVSLV ADSDQVPDEG EGVVTLMTLH TAKGLEFPVV FVTGWEDGQF PHMRALGDPA
     ELSEERRLAY VGITRARHRL YLTRAIVRSA WGQPVTNPES RFLQEIPADL VNWRREDPGV
     LGTGGAIGGG RPRGQGYGGG FGGGGAGFGS TGRSGASSPS FGAPRGRNNN LVLAVGDRVS
     HDKYGLGKVL ETKGAGPTAT VTIDFGSAGK VRLMLIGGVP MVKL
//
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