ID Q1QS38_NITHX Unreviewed; 1162 AA.
AC Q1QS38;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 118.
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=Nham_0058 {ECO:0000313|EMBL:ABE60959.1};
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE60959.1, ECO:0000313|Proteomes:UP000001953};
RN [1] {ECO:0000313|EMBL:ABE60959.1, ECO:0000313|Proteomes:UP000001953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14
RC {ECO:0000313|Proteomes:UP000001953};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) 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; CP000319; ABE60959.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1QS38; -.
DR STRING; 323097.Nham_0058; -.
DR KEGG; nha:Nham_0058; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_0_0_5; -.
DR Proteomes; UP000001953; 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; 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:UP000001953}.
FT DOMAIN 8..490
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 520..795
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1162 AA; 128208 MW; 1F2068031551CD95 CRC64;
MKAPRPVHPD ASARQQRASD PATSVFVSAN AGSGKTHVLV QRVIRLLLNG VDPARILCIT
FTKAAAANMS ERVFSTLGHW VTLDDEALNA ALRDTGIAQP DAWSRQRARK LFAAALETPG
GLKVQTIHAL CTRLLQQFPF EARVPARFSV LDERDQTGMM ERASISVMLD ASQNPDSPAG
RALQYAMGAA ADTTLRDVVN QACLSRDHFM AWTEDRGIEQ AISDVADALD VDPAERVEDV
EREIVDGPNL PISEWEALAA ILETGNKSDI EQARRLREAH AMIGEAAQAD RYLDVFLTGD
SVLRKSFVTK KISDVRPDIA AMLDRESQRV IALLERRRAL TIRDRTQSLL VIATAVAANY
RREKQERGLL DYDDLIDKTL AMLDQTSPGW VHYKLDRGVD HVLIDEAQDT SPKQWDIVER
IIADFTTGEG AREGVRRTVF AVGDEKQSIF SFQGAAPREF DERRSKLERK FRDAELPFRK
EDFIYSFRSG KTILESVDYV FRDAAIYTSI HAVGAHPVHE SLADAAPGVV DLWSLEERDA
RQQIEGWRAP FDAVSATSSE VKLARRIRNE VKTLIAQGTM TGHLGDRRPL RYGDILVLVR
RRGNAFDAII QALKQSGIPV AGADRLKLTE HIAIIDLMNL ADALLLPRDD LALAVALKSP
LFGLDDDDLF AIAHNRKGSL RDALADHATA NDKFRDAFER LKMCETRAAH ESPFAFYAWL
LGGDGGRRRI LRRLGHEAND ALDEFLELAL TYERKAPASQ QGFMAWLRAA DTDVKRDMEI
SRDEVRVMTV HGAKGLEASV VFLADTVTSP ADTERLNLIR MSRGNAPAHA AGVTVWAGRK
AEDPPDVVNA RAAMIAETEH EYRRLLYVAM TRAADRLIVG GCKPGNRKDV REHAWYDLID
KGLGKSGLAM REIETAAGTV KRFTRPGETE PDAAGPATPV AAAPIALPPW LHSMAAPEAP
AGPSLRPSDA DDNAHHRIWP GESPDQRRRA LLRGTLVHRL LQSLPDVPVD RRGDTALAYL
GRNARDWSEA ERDALAAQVL ALIGDSQFAP VFTDGSRAEV AIAGRLTTRR GDPVLVSGQI
DRLVVTREAV LIVDFKTNHA PPRNPADAPP AYVRQLALYR AVLARLYPEL PVKAALLWTE
TPEMMEISAL ALDAGLEAII SM
//
