ID B6BJ33_SULGG Unreviewed; 1646 AA.
AC B6BJ33; H1FWX2;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=SMGD1_2025 {ECO:0000313|EMBL:EHP30548.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP30548.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP30548.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP30548.1,
RC ECO:0000313|Proteomes:UP000006431};
RX PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA Labrenz M., Jurgens K.;
RT "Genome and physiology of a model Epsilonproteobacterium responsible for
RT sulfide detoxification in marine oxygen depletion zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
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:EHP30548.1}.
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DR EMBL; AFRZ01000001; EHP30548.1; -; Genomic_DNA.
DR RefSeq; WP_008336623.1; NZ_DS995286.1.
DR STRING; 929558.SMGD1_2025; -.
DR PATRIC; fig|929558.5.peg.2015; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG0514; Bacteria.
DR HOGENOM; CLU_002862_0_0_7; -.
DR OrthoDB; 9757917at2; -.
DR Proteomes; UP000006431; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000006431}.
FT DOMAIN 282..463
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 493..654
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1062..1408
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT BINDING 1083..1090
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1646 AA; 191442 MW; 56BB420D47AE354F CRC64;
MHNIAYIDIE VIVNSGKIDR LGLLLNDIQK STTSINDIKT TLEQNQPNYI CGHNFIDHDK
KFLSQTSLNQ IVEKTPIIDT LFLSMLLFVN KKTHKLDKPY KTEINIENEP LGDAQETKSL
FILLDKKFTN LERELQNIFV SLLYDDKYFS SYFKYKNVVP ASVNIYDIIK NKIYSSKEKF
EDIKINHPTE LSFAISYLYL DNKASVSSVI LKRYPNVVEV LKALTFNEAS IDLEKFALDE
FKIPSFRPFE KESNLVNKDQ VDLFSEESSA EVNNTISQRD IIASALGSDS ILTILPTGGG
KTFTFQMPAL IKAKAYKGLT VVISPLQALM KNHVDSFKDA NQNFSVVAIS GYLSPIERMN
IITEVENGVV DILYIAPEAL RSNSVFKALQ KRIIERFVID EAHCFSSWGH DFRHDYYFVA
NSIKELEESS EFQPKIPVSC FTATAKPEVL KDIKQYFADK LDIELKEFIA SSKRYNLEYR
AIEVNSKKDK YEQLIKELMR IGKKPTIIYI PQNARECREL SETLNHDERL HELDLVIEPF
YSKIDDEIES GKREGRDKGA ILNDFIDNKI DIVIATTAFG MGIDKPDIQT VIHYEQSDSL
ESYLQESGRG ARSDKLKAEC IVLYSKDDFN RTFSQLNHSR LEYHEIERVV RELKKEKRDE
IYLSPKQIAE KMGIDTEDSK IDYETMIKTA LLELEQAGII VRGRNSYKIF ATSIDKEKRS
MEHVHNVLDP KQEEYEKIYE YMIVVMQNII QRSKVDAIEV DDLADIVGVK KNIIFDVLYG
LQKEKLLEYD NDISIYVKNS VQKDFQKYFE MEKLIFNQLK YLPEYETKLD LREINSFTSS
DSTNDIKTIK KIIQSWTHLS KLKFNIFNAH FHKDICSFEL DKFDINKLEK LINIRKQTCE
FIIKNILKEL SGKEDGEIEI STNKLKVEYD AIQELTLNGF HHSIVYLHEL MKDSFNLRRG
RLIYYQSFKI DKQKDIENRT PYKKREHYNK SLKPYYERKI ESIHIQIAFL EKLIKDGWNK
TSEFVEDYFG MEYSKFKKKY KFNDKEIQLP ITKERLKEII HDLNDEQKRI FEDNKSSSIM
VLAGPGSGKT KSLVHKIASL VTIENNKAEY FLMLAHSRVA VAEFKNRLKK LIGNQVYAMK
IYTFHSFAIE LLGTNIKNDQ SALHSVIALA SNMLKNDEIN LPYIQMLVLD EYQDVGKDTY
EFIQAIYSKM SNDKKIIAVG DDDQCINNFG KDKADIVYIK HFKNDFEVIQ EETKDLVTTE
ESNYSQYELS TNYRSKKNII EYANSYSEIL SNRLKTKKLL SNSNENGEIN FIKYQNSSYI
HNIVQHVSHD SSETIAILAR NNDEILTIYS QLIANNIKAK YITSKDGFSL GNLIELQDFL
FFWKENDIDK ALDKLEAIYS NSKNYRLAQS VIKRFMDEYE DNIQYSQKHF ITVFEEYLEE
ITFEEFEISR ADVIVSTMHK AKGKEFDSVY ICIDENFIKD DYDKRLIYVA ITRAKNKLSI
HIKNNFLDFL TNYCDDVTEY DKNDQEPDRL VFLMALGDIA LSNEYSVDGI SRSNPIAGET
VNIKFIFNGF GIYKNNDQIV RLAAADNDKP ERLSSKILQK QSEGYTLEKN ADIDNIVLWQ
NKNTGIFLKQ VLCKVYMCKN NNIQEK
//
