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Database: UniProt
Entry: D0LRT5_HALO1
LinkDB: D0LRT5_HALO1
Original site: D0LRT5_HALO1 
ID   D0LRT5_HALO1            Unreviewed;       729 AA.
AC   D0LRT5;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Helicase c2 {ECO:0000313|EMBL:ACY19077.1};
GN   OrderedLocusNames=Hoch_6611 {ECO:0000313|EMBL:ACY19077.1};
OS   Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC   Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX   NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY19077.1, ECO:0000313|Proteomes:UP000001880};
RN   [1] {ECO:0000313|EMBL:ACY19077.1, ECO:0000313|Proteomes:UP000001880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC   {ECO:0000313|Proteomes:UP000001880};
RX   PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA   Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA   Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA   Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL   Stand. Genomic Sci. 2:96-106(2010).
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC       {ECO:0000256|ARBA:ARBA00038058}.
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DR   EMBL; CP001804; ACY19077.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0LRT5; -.
DR   STRING; 502025.Hoch_6611; -.
DR   KEGG; hoh:Hoch_6611; -.
DR   eggNOG; COG1199; Bacteria.
DR   HOGENOM; CLU_012117_2_0_7; -.
DR   Proteomes; UP000001880; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00487; DEXDc; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ACY19077.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001880}.
FT   DOMAIN          22..297
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          265..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   729 AA;  79354 MW;  4BE82FCA45CD037A CRC64;
     MFSDIASHAG LSVERVLGPS GILRACTPHY EDRPEQRHMA HAVAEALAHQ GALLVEAGTG
     TGKTLAYLVP ALLSGKRVVI STGTRALQDQ ITRNDIPLLE EILPRQFTAV TLKGVSNYVC
     VRKLWDVSAR LAMAPEARRD YQTVAEWARD SPTGDRAELT AVADDAPIWA ALTNTPDTRI
     GPRCPFFEQC FITRARRRAE KADLIIVNHH LFFADLSLRS SYPGARVLPE YEAVVFDEAH
     QLEDVMTEHF GVQVSTVRLA QLARDARHSS AGRNGPLFPN AQSSEKASDD DDSPKPSTRP
     METSTERIIA HLERCAEGFF ISVRAALRES PAGDGGRVPL DDSLFADSDR QEAWFRLDSA
     LDELAAHATL RADELASDSA EAAAYAIGED NPGNADERAE ALAAVAVRAE MLRGDLALLA
     ERSERAFVYW GEARATSVGL CAAPVDVSAY LRKYLLPIAP AAIFTSATLR AAGSFDYLRQ
     RLGLDSEIAD ELAVPSPFDY ARQAILYLPR DLPDPRDAGF TAAACARVVE LCAITGGRAF
     VLFTSHRALR EAARRLLGTL PHEVLVQGQM PRAALVEQFR ARPGAVLLGT GTFWEGVDVP
     GDALSLVIVD KLPFAPHTDP LVRARVQRIE SRGGAPFEGY QVPQAALALK QGFGRLIRRS
     DDRGIVAVLD PRIVTRRYGR AFLDTLPADI TRTSVLEQVR RWWQRGPAPV SSSGDGQAGD
     AVAAREKSE
//
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