ID Q5NNI8_ZYMMO Unreviewed; 1162 AA.
AC Q5NNI8;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 133.
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 OrderedLocusNames=ZMO1098 {ECO:0000313|EMBL:AAV89722.1};
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV89722.1, ECO:0000313|Proteomes:UP000001173};
RN [1] {ECO:0000313|EMBL:AAV89722.1, ECO:0000313|Proteomes:UP000001173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173};
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., Jin S.J.,
RA Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; AE008692; AAV89722.1; -; Genomic_DNA.
DR RefSeq; WP_011240933.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NNI8; -.
DR STRING; 264203.ZMO1098; -.
DR KEGG; zmo:ZMO1098; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_0_0_5; -.
DR Proteomes; UP000001173; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001173}.
FT DOMAIN 7..486
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 520..794
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 953..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1162 AA; 130215 MW; 9AF4CD5FA6759F5D CRC64;
MAHPQRLMPL EAEQLQASDP KGNIWLSASA GTGKTHVLTA RVLRLLLNRA APESILCLTF
TKAGAAEMSE RINQRLAKWV IQLNDDELRE ELQALGARYD RDTLALARTL FARVLDAPGG
LRIQTIHSFC QSLLTAFPVE AGLIPGFQLI EGREEATEAK KTLTRILDHQ TLPYHIKDDD
IALLAEKLGE QGAEDYIYQC RFHAFAFNNL GVAIESRVKR ALDLPFSDIN QALEEACDDD
HFDFALLRQI AEANEKWDTA TAHKNLAIIQ DFVAASPADR LASLGDFQSL VLTQKGELKK
APTGITKKIA PEYEEWMIAL SKAIHQIISL KKRHEFSQFA IAALRTGQAY SQAWQQTKKE
SGLVDFNDMI ETSVALLRTP GIGEWVRYKL DRTTDHILVD EAQDTNIFQW AIISALAEDF
FSGESAKSVE ASRSIFAVGD FKQAIYGFQG TDPQAFVDAR DYFNDKSQGS GREILDLSLN
RSFRSTPPIL AIVDQMLADI ESSCGGIGIS QQALQPHQSA RSDLGGSVVL WQPISDYQEE
GENTSEETDA DDEEQLENGE LELAIRLARQ IETWLNPKTP LYLPALGRNA APRDILILVR
NRGRLASLIV GCLHAQKIPV AGLDRLTLTA PLAVSDLLSA IRFVLQPDDD LTLACLLVSP
LIGWDQERLY RLAAKRAKKE SLFDRLRKSE AEKETWDIIR EWLSKADFIT PYRFLEMLLS
GKGEGRRKLL ERLGEEARDP INELLNAALL LESETTPSFQ RFLDWFDSGD VEIKRDPSVR
QNTVRIMTVH GAKGLQAPVV ILADATRDPH QSNGFRKEII TWPLDEANAP IPMPSNDDIA
YLPSDFGDII NEKKAKDLQE HWRLLYVAAT RAEEYLVITG HLGSRAKNIP PKDSWYACAT
RAITAMGIAW QEDAMWQQKA VYHWEGRKKV TDIPKKQPTF PKEAMPSWIK NEIPEEPKPA
YPLRPSDLVK DNTSNPPPDG GSITAAKRGT LLHALFERLP MLPVEEREKA GLRWLETSAG
VKDAALRNSL IKDACDAMSN PVYRDIFSEK ALAEAPIAAK VGEHVISGTV DRLWIDRNKK
RVHIVDFKTG RRVPATKEQV SEAYQRQLAA YVVALEKIFP DYAIEASLLY TTAPKLVSFE
QPFLHDYFVQ MDKGDIQSEN QI
//
