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Database: UniProt
Entry: A0A0F7KKM6_9PROT
LinkDB: A0A0F7KKM6_9PROT
Original site: A0A0F7KKM6_9PROT 
ID   A0A0F7KKM6_9PROT        Unreviewed;       730 AA.
AC   A0A0F7KKM6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   Name=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   ORFNames=AAW31_12530 {ECO:0000313|EMBL:AKH39628.1};
OS   Nitrosomonas communis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH39628.1, ECO:0000313|Proteomes:UP000034156};
RN   [1] {ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Draft genome of Nitrosomonas communis strain Nm2.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKH39628.1, ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|EMBL:AKH39628.1,
RC   ECO:0000313|Proteomes:UP000034156};
RX   PubMed=26769932;
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic Ammonia-
RT   Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC       Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC       least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01488}.
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=3.6.4.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01488};
CC   -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR   EMBL; CP011451; AKH39628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7KKM6; -.
DR   KEGG; nco:AAW31_12530; -.
DR   PATRIC; fig|44574.3.peg.3040; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000034156; Chromosome.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd17933; DEXSc_RecD-like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 1.10.10.2220; -; 1.
DR   Gene3D; 2.30.30.940; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01488; RecD_like; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR006345; DNA_helicase_RecD-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029493; RecD-like_HHH.
DR   InterPro; IPR041451; RecD-like_SH13.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01448; recD_rel; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR   Pfam; PF13245; AAA_19; 1.
DR   Pfam; PF14490; HHH_4; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   Pfam; PF18335; SH3_13; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000034156}.
FT   DOMAIN          348..489
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         359..363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   730 AA;  80663 MW;  7B4F6E8B5A1AC477 CRC64;
     MKASSYLPHD TDHPQEKLQG SVERVTFHSE SSGFCVLRVK VKGQRELVTV IGSAASVTPG
     EYIDCLGFWV NDRQHGQQFK SVSIKIVPPT TLEGIEKYLG SGMIKGIGPH FARKLVKAFG
     VDVFDVIECT PDRLMTLPGI GRKRLERVTG AWAEQKVIRE IMVFLQSHGV GTSRSVRIYK
     TYGEQAIEKV REDPYRLALD IHGIGFKIAD TLAQKLGIAP NSLMRSQAGV RHVLQEWSNE
     GHCAAARDTL RDMAVKLLDI PAPVIEEGIT AELVAGNLTA ETINQQESIF LTPLYRAEVG
     CANHLLRLNQ GQPPWGTIDA HKAIPWVEEK TGLILSASQR AAIELMLRHK VAVITGGPGV
     GKTTLVNSIL KILKAKQIQI ALCAPTGRAA KRLSESTGLE AKTVHRLLEF DPAIFAFKHN
     EEFPLELDCL VIDESSMMDV TLMNQLLKAM PSKAALLIVG DVDQLPSVGP GAVLADIIDS
     GKIATVRLTE IFRQASTSKI ITNSHRINQG LLPITTHAQG LSDFYCVYAE TPEEIFSKLI
     QVVLERIPQR FNLHPVHDIQ VLAPMNRGGL GARSLNIELQ QRLNGSSEPK VMRYGSIYAP
     GDKVIQQINN YDKEVFNGDI GIVLSVDIEE SLLQIQFDER IVDYDFNELD EISLAYAISI
     HKAQGSEYPA VVIPLAMQHY MLLERNLLYT GVTRGKQLVV MIAQPKALAM AVKNQRSQRR
     VTNLISRLNS
//
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