ID A0A0U5E0P6_9GAMM Unreviewed; 1718 AA.
AC A0A0U5E0P6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=THIOKS1160027 {ECO:0000313|EMBL:CRI63860.1};
OS Thiocapsa sp. KS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=610332 {ECO:0000313|EMBL:CRI63860.1, ECO:0000313|Proteomes:UP000198608};
RN [1] {ECO:0000313|Proteomes:UP000198608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS1 {ECO:0000313|Proteomes:UP000198608};
RA Luecker S.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001665};
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DR EMBL; CVPF01000068; CRI63860.1; -; Genomic_DNA.
DR OrthoDB; 9760034at2; -.
DR Proteomes; UP000198608; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase 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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
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; IPR036397; RNaseH_sf.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR InterPro; IPR027785; UvrD-like_helicase_C.
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; PF13538; UvrD_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
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}.
FT DOMAIN 304..480
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 509..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1081..1298
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT REGION 1324..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1102..1109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1718 AA; 191917 MW; 83338D06E67CA652 CRC64;
MSAAPDRPPV ACLCLDIETA KQDALCLREI GLYRPDLDAR ARISAQAPDL VSRVDALTDG
ASFALGHNII AFDGPTLAVL HPGLALHRLP LIDTLELSPI AFPQNPYHRL VKDYHLCTTS
RNDPVRDAEL AYRLFLDQWE TFRTRVVEHP DEMLCLHFLL APQNGIGVAS FFATLRRALR
PSIDEAAAAW SRATAGKVCI TGLRRIIEQW LPDPQWHKPL AYTLAWLRVA GGNSVLPPWV
KLSFPETGEA IAALRDVPCT DPACAWCREQ HDLERMLPHY FPGITDFRPT PATPDGRSLQ
RAIVENGFAG RSTLAILPTG GGKSLCFQLP ALARYYRTGS LTVVISPLQS LMKDQVDNLE
ARGVTCAGYL NSLLTPLERQ AMLEKLRLGD LGLIFVAPEQ FRGTAFGNAL QHREIGAWVF
DEAHCLSKWG HDFRPDYLYV SRFIQRRRKA LPEPVFCFTA TAKPDVVQDI RTHFEQRLGL
SIELIEGGVS RENLIYEVRA VPAQVKYGEV LSLLRETLRE DGGAIVFCAR QKTVEEVAAF
LKQAGLDCGY FHGGMPPADK RAVQEAFIGG SLRVIAATNA FGMGVDKPDV RLVIHLDTPG
SLENYLQEAG RAGRDQAPAR CVLLYDEADL DVQFRLLRNS RLTQHDIHSI LKALRIIERK
DRSEGEVVVT SGEILLEIPE QHRIDPDAKD AETKVRIAVA WLEEARLLER HENHTRVFPG
SLLVGSLDEA RDVLRKKLGP TADIDPYLAI LAELLAADDD ESRSTDDLMR ATGKDSRTLQ
AMLRELDQWQ LLSNETEIGV TLYRDPDTVE RLAELTRIEA ALLGQLREAA PDADTESWQL
LNMRRLCDTL RRDTGVEIDP HRLSRLLKSY AEPFGEGVEH RGFFALRPAG MDNRAIKVLR
SWRDIAHIGE RRLRVAHALV AIFLAARQGN TLLVVLKLGE LERKLRADLT LQDLDIQRWD
TALSAALLYL DANEVLHLAR GKAVFRAALR IELNPEARRR QFKKSDYAEL ALHYKDKIVQ
VHVMAEYAKL ALGKVQAAMR FIVDYFRLDR DELIRRYFAG RQELLENATT EEAHRRILID
LRNPGQQAIV AAPLDGNHLV LAGPGSGKTR VIVHRVAWLL RECMVLPQTI MVLAYNRSAA
AEIRHRLWAL AGPDAAGVTV QTLHGLAMRL TGTSYAVAIE RGDTLDFGAV IRRATADLNR
SDEGTGIGAS VVRDRMLAGL RFLLVDEYQD INGDHYELIS ALAGRTLQTE EDRLSLLVVG
DDDQNIYAFD GASVRYIRRF EQDYQARRYQ LIENYRSTAH IIHCANRIVA RARDRMKAGQ
EIRIDHARRE QPEGGDDSAR DPVASGRVHV LEVPRDARLE AQLALAEIQR LHGLAHAGGA
GQWGRFAVIS RRWDDLEPLA ALCRRRRIPV RMLLDQHQPN LHVTREGRAL LDLLRGQRRR
NPRSRLLLRT GVLSRWFRRR YGVPVDGLIE HPFQAALARF IADTEGAVPA GEQVIGDLVE
SLYEIGTGIK ALAQGGANGP LVLMTAHRAK GLEFDHVLIL DSGGWQSGSD DERRLFYVAM
TRARKTLTLC EALGGKHPFI ADADGLTLRS RAAQPEPEPG LGNRTLIADP EKIVLSWPGY
FPAGAPLHRA LAALDVGSEL VLRERVDGKG GWEIADTQGV AVTRMSSKFR PPVGRIIAVR
VAAILVRDAK AEERQNMRCS RWELVLPEIE YEPKPSSV
//