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Database: UniProt
Entry: E1QK74_DESB2
LinkDB: E1QK74_DESB2
Original site: E1QK74_DESB2 
ID   E1QK74_DESB2            Unreviewed;       911 AA.
AC   E1QK74;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=DEAD/DEAH box helicase domain protein {ECO:0000313|EMBL:ADK85967.1};
GN   OrderedLocusNames=Deba_2613 {ECO:0000313|EMBL:ADK85967.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK85967.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK85967.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
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DR   EMBL; CP002085; ADK85967.1; -; Genomic_DNA.
DR   RefSeq; WP_013259406.1; NC_014365.1.
DR   AlphaFoldDB; E1QK74; -.
DR   STRING; 644282.Deba_2613; -.
DR   KEGG; dbr:Deba_2613; -.
DR   eggNOG; COG4581; Bacteria.
DR   HOGENOM; CLU_002902_4_1_7; -.
DR   OMA; WYATPLK; -.
DR   OrthoDB; 9807155at2; -.
DR   Proteomes; UP000009047; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF8; HELICASE SKI2W; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ADK85967.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT   DOMAIN          62..222
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          280..479
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   911 AA;  100511 MW;  8487859C132B5558 CRC64;
     MTAHRTKTTG RRPTAKGPPR RRPEKPVRDQ EPSIHPKLLP VLEHIGVPQA TAFAADPFQA
     EAVEKLAEGD VVVSAPTGSG KTWIAEQAIA QALAQGQRAW YASPLKALSN AKYHEFGAIF
     GPERVGILTG DRKENSQAPL IVGTTEILRN QLYDAMHRGE NIDSSLVVLD EAHYLGDPDR
     GVVWEEVIIY LPPRVRLLLL SATVENAEQL ARWLMFVRGN QCRTVRSDQR PVPLFPVFMF
     PDGELAPLKT RRGLLGKISH FLEQEARQPK GGRQINSTPQ FANILSALDH AAMLPAIFFL
     KSRADCDNAL AHAAGARLAV DQAQGQRLNR FVDDFLAEYP FLADHPQLEP LRRLRVAAHH
     AGHLPHWKLL VERLMQTGLL RAIFSTSTVA AGVNFPARTV VVTQSDRFNG REFVDLRATD
     LLQMTGRAGR RGMDNIGFAL IVPGPYQNVP LLAGLLNANP EPIESQLHIN FSMALNLLLS
     QRPAEIKQLL GCSLATFQRL ERRGAKAAGE GGMAELMRQL APLLAGSNCH GPEEAVVRRK
     RRRQLDGLRR RLAHELESME QEQGLWAALT RGRVFIDMFG AMAAVLRREG RGEDAGVLAV
     SLIPDRRLQR GRPRLDFVPI DEIAGVFHEV IDLPVAGGGR VLAQAVLEQI PDAPRALSGP
     ELENLGLRER DETKLRLQEV ESQIDSLACV GCAIEGKCLH GGPEIEPLLQ RAEQMLSQVR
     EESHAFWYDF VRHLEFLRSE GFVDSQGGLT QDGLWASKLR LDQPVLIAQA IRSGALPQND
     PVLLAALLAL FVDDRERESD SPYLSQRLRE GLATLLADIE PLLERLRQWG FHTPALPMPA
     ASAMFAWALG QEFADVVALY GGAEGDLAAL IYRTADNLRQ IASLHDTHPA LSASAREAVE
     LLLRPPVVLP T
//
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