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Database: UniProt
Entry: A0A166TVT0_9EURY
LinkDB: A0A166TVT0_9EURY
Original site: A0A166TVT0_9EURY 
ID   A0A166TVT0_9EURY        Unreviewed;       583 AA.
AC   A0A166TVT0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Putative DNA helicase Rad25 {ECO:0000256|HAMAP-Rule:MF_01489};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01489};
GN   Name=rad25 {ECO:0000256|HAMAP-Rule:MF_01489};
GN   ORFNames=A4G99_23210 {ECO:0000313|EMBL:KZN26086.1};
OS   Haladaptatus sp. R4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haladaptataceae; Haladaptatus.
OX   NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN26086.1, ECO:0000313|Proteomes:UP000076599};
RN   [1] {ECO:0000313|EMBL:KZN26086.1, ECO:0000313|Proteomes:UP000076599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R4 {ECO:0000313|EMBL:KZN26086.1,
RC   ECO:0000313|Proteomes:UP000076599};
RA   Mukhopadhyay S.K.;
RT   "Genome sequence of halophilic archaea.";
RL   Submitted (APR-2016) 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=3.6.4.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01489};
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006637, ECO:0000256|HAMAP-Rule:MF_01489}.
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:KZN26086.1}.
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DR   EMBL; LWHG01000006; KZN26086.1; -; Genomic_DNA.
DR   RefSeq; WP_066139246.1; NZ_LWHG01000006.1.
DR   AlphaFoldDB; A0A166TVT0; -.
DR   STRING; 1679489.A4G99_23210; -.
DR   OrthoDB; 8379at2157; -.
DR   Proteomes; UP000076599; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01489; Helicase_Rad25_arch; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032438; ERCC3_RAD25_C.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR030882; Helicase_Rad25_arc.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR   PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR   Pfam; PF16203; ERCC3_RAD25_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   PRINTS; PR00851; XRODRMPGMNTB.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01489};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01489, ECO:0000313|EMBL:KZN26086.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01489};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01489}.
FT   DOMAIN          234..383
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          435..583
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          8..35
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   583 AA;  66519 MW;  A69A045EFA5F458E CRC64;
     MLTADEVARV LDRSHEDANR ALERLRDERD VARLDVENDP VVWFPTEWER LADRERIVVF
     PKRREIVADQ PEQFTRAQLS QFAHLTDTTR AGSYSYQVRQ EDIWSAPYDS LDNLMRTVRQ
     VLPEPSPDLE AFIEGQWKRA KQFRLYTHED GYVVLQAASD DLMGNVARQK LNDNHLRAPI
     ADDESWVAED KVAEVKRILY EAGYPVQDER ELETGDELPV ECALSLRDYQ REWVEEFIDL
     KSGVLVGPPG SGKTVAAMGV LEAVSGETLI LVPGRELAGQ WRDELLTHTD LTREQVGEYH
     GGEKNVRPVT IATYQTAGMD RHRQLFDQRR WGLIVYDECQ HIPSRVFRRS ANLQSKHRLG
     LSATPVREDD KEKDIFTLIG PPIGTDWDAL FEAGFVAEPE VEIRYVGWDE ETYQGEYANA
     DGRGKRQIAA TNPAKLDEIR FLLAEHPTSK ALVFVEYLEQ GDRIAEALDV PFLSGQMRHP
     ERERHLQAFR DGREDTLVIS RVGDEGIDLP DAEIAIVASG LGGSRRQGAQ RAGRTMRPAG
     RARMYVLATR GTREEEFARQ QLRHLASKGI RIQETVLDER DEE
//
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