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Database: UniProt
Entry: D2RS11_HALTV
LinkDB: D2RS11_HALTV
Original site: D2RS11_HALTV 
ID   D2RS11_HALTV            Unreviewed;       806 AA.
AC   D2RS11;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Helicase c2 {ECO:0000313|EMBL:ADB62628.1};
GN   OrderedLocusNames=Htur_3766 {ECO:0000313|EMBL:ADB62628.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB62628.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB62628.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
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DR   EMBL; CP001860; ADB62628.1; -; Genomic_DNA.
DR   RefSeq; WP_012944872.1; NC_013743.1.
DR   AlphaFoldDB; D2RS11; -.
DR   STRING; 543526.Htur_3766; -.
DR   GeneID; 8744393; -.
DR   KEGG; htu:Htur_3766; -.
DR   eggNOG; arCOG00770; Archaea.
DR   HOGENOM; CLU_313456_0_0_2; -.
DR   OrthoDB; 27512at2157; -.
DR   Proteomes; UP000001903; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11472:SF65; DNA HELICASE REPD; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:ADB62628.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          3..357
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          136..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  89071 MW;  77F7C4683F2B6BF0 CRC64;
     MTDWRSIFGH ERPYDEQVDG IETAIDTARD GGYSVVEGAC GTGKTMIALT AGIDLVRDPD
     TDYERVFVLT SVKQQLHQFE EDLETINENL PDDWNPVSGL TLVGKADVCP YNRAGAGGID
     DGNVYDRCET LRDRTRDLTG EGGDTTAGSL TAQARSQQMG LADSGRQGGG PRLLQTAGET
     APYSPDLPEY SDGGPVDVST EYCPFYAQYL EDLPEEGSDG DAVEAVPYDF TEAGMITPED
     LVARSVSHGT CPHSVMGAVL GHVEVVIGNY YHAFDPRTTG SFTGALLDDS TFAVCDEAHM
     LEPRVRDLVS DGVADRTLRD AETELSRVIQ PIKFEREGRR AEGGSKTADA DLVRAELNDS
     DVSYDELEQT LEFVRDLRSE LDRRVTAHLD RKHRGWQSNL TDLADDEIPL RDPAEPAEDE
     LTAWAREAGY GDADWVRAEA VGAVVERILN EAEDEDRTRA APAVGRVLGE WYRRDHTDYF
     REIELERTWD DTEPADSWRR AYNARLALHN CVPSDAIGER LGMFGGGILM SATLEPMDAF
     TEVTGLDYLE REEERPVVER RYGLHFPEEN RESFAVAAPK YTYDNRGRPG EESEAQRASS
     GAGDSPRNPT RRQYVDAVTK VGRLPGNVLV GMPSYAEADW LAGVLEERLE KPVLLDAASD
     DETTQALKRE FFDGDGKVLV TSLRGTLTEG VDYSGDRLAA AVVCGVPIVN TSSPRTKAVR
     RAYDDEFGDG FTYALTIPAV RKARQAIGRV IRSPEDVGVR VLLDERYARD SWDSVRPYLP
     DDGEFQPVSP DMLDVGLERF RGRLEQ
//
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