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Database: UniProt
Entry: A0A1C2HY24_ACITH
LinkDB: A0A1C2HY24_ACITH
Original site: A0A1C2HY24_ACITH 
ID   A0A1C2HY24_ACITH        Unreviewed;       727 AA.
AC   A0A1C2HY24;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=A6M23_07695 {ECO:0000313|EMBL:OCX73721.1}, A6P07_17785
GN   {ECO:0000313|EMBL:OCX68658.1};
OS   Acidithiobacillus thiooxidans (Thiobacillus thiooxidans).
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=930 {ECO:0000313|EMBL:OCX68658.1, ECO:0000313|Proteomes:UP000094893};
RN   [1] {ECO:0000313|Proteomes:UP000094893, ECO:0000313|Proteomes:UP000095008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A02 {ECO:0000313|EMBL:OCX68658.1,
RC   ECO:0000313|Proteomes:UP000094893}, and DXS-W
RC   {ECO:0000313|EMBL:OCX73721.1, ECO:0000313|Proteomes:UP000095008};
RA   Zhang X., Feng X., Tao J., Ma L., Xiao Y., Liang Y., Liu X., Yin H.;
RT   "Comparative genomics of the extreme acidophile Acidithiobacillus
RT   thiooxidans reveals intraspecific divergence and niche adaptation.";
RL   Int. J. Mol. Sci. 0:0-0(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}.
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:OCX68658.1}.
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DR   EMBL; LWSA01000288; OCX68658.1; -; Genomic_DNA.
DR   EMBL; LWRY01000067; OCX73721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C2HY24; -.
DR   eggNOG; COG0507; Bacteria.
DR   OrthoDB; 1826980at2; -.
DR   Proteomes; UP000094893; Unassembled WGS sequence.
DR   Proteomes; UP000095008; Unassembled WGS sequence.
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}.
FT   DOMAIN          346..511
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         357..361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   727 AA;  79763 MW;  5F640DCF16AFFC67 CRC64;
     MAKSERPQQD VPTELLGGLI ERVTFHNDNN GFCVLRIKAR GHRDLVTLVG HAAAVTAGEW
     ITASGIWVTD RDHGLQFKAA FLKVSAPTSR EGIEKYLGSG MIRGIGPVYA KKLVKAFGEQ
     VFTVIEETPE RLAEVDGIGP IRRERMVAAW ADQKVIREIM LFLHTHGVGT ARAVRIFKTY
     GIDAVRIMTE NPYRLARDIH GIGFKTADAI AMKMGIAQNA PIRVQAGISY ALMEARDDGH
     CGLPHEALTP LAEQLLEVPI DAIEAAIAAE IQEGTLIADQ VQNTPGVFLA PLYRNEQGIA
     QILKKLCAGQ APWSGIAADT AMDWVQKRLD IVLADSQKAA IRMVLQEKVA LITGGPGVGK
     TTLVNAILHI LDAKKLRIVL AAPTGRAAKR MSETTGKEAK TIHRLLEINP LGGGFKRRED
     YPLECDLLVL DECSMIDVPL MHALLKALPP TAGLLMVGDP DQLPSVGPGQ VLADLIAAQT
     LPEVHLTEVF RQAAESRIIR AAHQIHAGHL PDLRPPEKLS DFYFIDVEDP AEAADKLVKV
     VTTHIPRRFY LNPLRDIQVL CPMNRSALGA RALNDALQTA LNGESTPVVE KFGRRFAPGD
     KVMQIQNDYE KDVFNGDIGF VQAVDTEENT LTVDFEDRMV SYGFGELDLL QPAYAITVHK
     SQGSEYPAVV IPLSTQHYPM LQRNLLYTAV TRGKTLVILL GQKKAVAMAT RNGSSKRRWT
     KLCDWMV
//
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