RAD25_HALMA
ID RAD25_HALMA Reviewed; 621 AA.
AC Q5V5F7;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative DNA helicase Rad25 {ECO:0000255|HAMAP-Rule:MF_01489};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01489};
GN Name=rad25 {ECO:0000255|HAMAP-Rule:MF_01489}; OrderedLocusNames=rrnAC0181;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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:0000255|HAMAP-Rule:MF_01489};
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01489}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV45245.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV45245.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004963031.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V5F7; -.
DR SMR; Q5V5F7; -.
DR STRING; 272569.rrnAC0181; -.
DR EnsemblBacteria; AAV45245; AAV45245; rrnAC0181.
DR GeneID; 40154481; -.
DR GeneID; 64823064; -.
DR KEGG; hma:rrnAC0181; -.
DR PATRIC; fig|272569.17.peg.977; -.
DR eggNOG; arCOG00874; Archaea.
DR HOGENOM; CLU_008213_4_0_2; -.
DR Proteomes; UP000001169; Chromosome I.
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:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..621
FT /note="Putative DNA helicase Rad25"
FT /id="PRO_0000429043"
FT DOMAIN 268..417
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01489"
FT DOMAIN 469..621
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01489"
FT REGION 441..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 371..374
FT /note="DEAH box"
FT COMPBIAS 446..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01489"
SQ SEQUENCE 621 AA; 69875 MW; B2F4A5192289CDA3 CRC64;
MTDEEPADRD DDSDSTPELE LDAVYDAIDA VGRPHLTATE FSRKTDLTPD EARAALERLA
DDGDIERQDV SEVESVWYPT DIAEVTDRER VVLFPDRREV VVEHPDQFTR AQLSQFARLQ
DTNRSGGYVY ELREEDIWAA PHESLDDLLT TMRDVLGERS PHLEEWVTSQ WERARKFRLK
THEDGYVVLE AESDDLMGNV ARPKLDDDHL RAPISDSESW VNEDATAEIK RTLYEAGYPV
RDDRDLETGD AIEMDLRLRL RDYQQDWVER FTEQGSGVFV GPPGSGKTVA AMGAMAAIGG
ETLILVPSRE LATQWRDELV RHTSLTDDDI GEYHGGEKEI RAVTIATYRT AGMDRHRKLF
DQRKWGLIVF DEVHHVPSPI HRRSADLQTK HRLGLTATPT RESDDEEEIF TLIGPPIGTD
WGKLFDEGYV AEPEVEIRLV PWGDETEQSE YSSTSGHDRR QAAASNTGKI DEIRYALAEN
PAAKALVFIE YLDQGEAISE AIDAPFISGE TPHARREKLF DEFRRGELTT LVVSRVGDEG
IDLPDAELAL VASGLGGSRR QGAQRAGRTM RPAGDARMVI LATRGTTEED FVRRQMRHLA
SKGIRVTETE AEAVEPPAKT E