ID A0A150G2F3_GONPE Unreviewed; 1013 AA.
AC A0A150G2F3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=GPECTOR_75g776 {ECO:0000313|EMBL:KXZ44052.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ44052.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
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:KXZ44052.1}.
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DR EMBL; LSYV01000076; KXZ44052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150G2F3; -.
DR STRING; 33097.A0A150G2F3; -.
DR OrthoDB; 208346at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF69; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 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:UP000075714}.
FT DOMAIN 4..407
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 390..888
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 153..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..726
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1013 AA; 110018 MW; F9FE12C3BD4422AC CRC64;
MRMGLNDEQL RAAISESDKP LLIVAGAGTG KTSTLISRIV HLVRDEVRER LHRNGVNARS
LTAATFHSFC FSILRWYHKV AGFSQCPTVW TDSDLKRAVA LAIRLQNLDV GRVDMAAWLG
LPDVPGWADI LKAVEKKHPD IWESCGKAAQ DLVAKQQKSK RKKGNGADTG AGAAQNTKKG
AKKQRTNNGP AASTNTATGD GAAAGPAGAG ASDGAAEGFT ADADNNLLYR AEFIKLVYSK
LQTQYSPGTE AVIGAKPKAA LINARIQWLD RFKRTGADIS GYGMQFALFY SYVHAYYDAL
LRAANAIDFN DMLLLVDKLI TEHDWILRRL QKKHQYVLVD EYQDCSPQQV RFVELLSGHS
GRLTAVGDDA QSIYRFRGAM PGVFEAFRQF HSGQLQQTLL ERNYRSRPKI LADSAGVTRK
VLRPTKEDTA DKIQELVKEG KVEGPGGVAV LYRCFKMGGA RTHSQLQSAL RSRGIPFVLV
RDKSVFERKE VQDTLAYLRL AANPTDDAAF VRVFNTPPRR LGDQKAGFMT MLRDLQARAA
ARACEALDMQ RRELGAGRGR NGVAPQPDGP AAGPAAQRPP AHSYYGLCCA LLQQAGGGAG
AGGDDDLLGY QLAPSHQGGV RKLVEVVEDL RRAVWQLGPA GAIKRVLDLT GYVEWYAEQK
ATKERLAQDA AEQLAMSPGG AAKAAAEKGA KAMKVQAGQE GNAGGDEDDK DDEEGEEEDD
DDDDLPPLPA GLPPEPVELG ERAQKMLGLK LLFREAKLFA SKWQVPSRAF AMPPHPHTAA
EAPAGGPVVP ELFALAAHAV MSSFSGEDVQ AALHTAHPLT GLPQVTPEVL EQMYAEQRRG
PLVLRDFLAH VALSDREVEA GGAGAAAGAG GAKSRQAVTI STIHAAKGLE FPVVFVARWA
EGYLPTLPRP DKSELNRLSP QEQAEYIERD AEEHREEERR LAHVAVTRAM ERLFITSIRV
HRVQGKSWLV PPSSIELPAD PQVVERRPLP QSAEEAAMEQ EAVRNMRVAG GQQ
//
