ID G0MBV0_CAEBE Unreviewed; 831 AA.
AC G0MBV0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN ORFNames=CAEBREN_01169 {ECO:0000313|EMBL:EGT45787.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) 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|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR EMBL; GL379789; EGT45787.1; -; Genomic_DNA.
DR AlphaFoldDB; G0MBV0; -.
DR STRING; 135651.G0MBV0; -.
DR EnsemblMetazoa; CBN01169.1; CBN01169.1; WBGene00139894.
DR eggNOG; KOG0352; Eukaryota.
DR HOGENOM; CLU_001103_9_4_1; -.
DR InParanoid; G0MBV0; -.
DR OMA; WSDPGAC; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR032284; RecQ_Zn-bd.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF159; ATP-DEPENDENT DNA HELICASE Q5; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT DOMAIN 192..366
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 424..577
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 92551 MW; 49DBA390B2E63B08 CRC64;
MSTNKRNLET ITIDDSDEED QKEPVAKKPT TSNYNAWAEI FNKKKAEASA TAAAERVKKE
AEKEQQRQKL RDAVNERKRR EALIANGNKS KIGAEKSEKS MNPDKKPVKD TKTSFKTPIL
SSTKSEDSPG PSDSQVTLDS QDSGDFVANP LAIGTGERLI RGQDIIERRD KVFLELFQHK
KYRSRLQMQA INCILKRKCD VYVSLPTGAG KSLCYQLPSI VHGGVTVVVS PLIALMKDQI
ASLRRKGIPC ETLNSTLTTQ ERSRIWAELG RDKPTIRMLY ITAEGCATEG IKKLLGGLTK
REVLRYIVVD EAHCVTQWGH DFRPDYLTLG SLRDVCPGVP WVALTATANA KAQDDIAFQL
KLRNPESFKA GTYRDNLFYD VCMRDHLPTA PENHMASFIN KCLTIDAKTN GISSNQTKNE
KSGRANHKRT FTGSAIVYCR SRNECEQVAK MLVIAGIPAE AYHAGLGKKD RNDVQEKWMN
NEIPVVAATV AFGMGIDKPD VRAVIHWSPS QNLAGYYQEA GRAGRDGKRS YCRIYYSKQD
KNALNFLVSG ELAKLREKAK KNNADGEKAA MQIKSIQTGL QKMLDYCESA KCRHVSIASF
FDDTDCQPCK TNCDFCRDPA KTQRSAEAFI NSEESTGRSM FRRPGTSSGE SGFGTVYGGG
RRGGETEDEL LSSASTSKDA VERMEHEEAK RVRGIIDNEF AKRRRQAPPP PRAARGSQRV
EPATDVSVIK PEQNVIKNVT LESRENWVRF LIRALETNWI VTGPPAGTTI KQCAEQLEYG
MYSISKNETT YKNKCGHKLA EIKKLTAKCN PFIYTNTAVE QNGFVKAADL A
//
