ID R1BI32_EMIHU Unreviewed; 1032 AA.
AC R1BI32;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=EMIHUDRAFT_216860 {ECO:0000313|EMBL:EOD09042.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD09042.1};
RN [1] {ECO:0000313|EMBL:EOD09042.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD09042.1};
RG DOE Joint Genome Institute;
RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT "Genome variability drives Emilianias global distribution.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [3] {ECO:0000313|EnsemblProtists:EOD09042}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (JUL-2023) to UniProtKB.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
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DR EMBL; KB868759; EOD09042.1; -; Genomic_DNA.
DR RefSeq; XP_005761471.1; XM_005761414.1.
DR STRING; 2903.R1BI32; -.
DR PaxDb; 2903-EOD09042; -.
DR EnsemblProtists; EOD09042; EOD09042; EMIHUDRAFT_216860.
DR GeneID; 17255185; -.
DR KEGG; ehx:EMIHUDRAFT_216860; -.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_294139_0_0_1; -.
DR OMA; EYQDNSE; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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}; Helicase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000013827}.
FT DOMAIN 90..518
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 519..896
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 274..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1032 AA; 113530 MW; F91F8050CCDC636B CRC64;
MPKRKPEGAE FDLPLPDASN SLAPQQRLLR LEFERFCASR VGAGGVVGAS GDDGGENSSA
DGRHLASILQ REAAKFNEGD DELLCAALDA TCEAHSAAVA DSTASELSVR AGAGTGKTHT
MIQRAVRLVR LGVPPNCVLM VTFSVKAAEE LCSRVGHAFA ALGVPPRLLP VGKTFHALAF
FWVRRYWRAL ELGAAPAPLT GDAGVRKFMQ RVLEEQVAEK RLEWCVAALR KHLLRPGGAD
ADGAPPSWEE VLAFARQSLP ASWRRACEAA EREVPFDEAQ AAPARKKRRG GRDAADVAAE
EEEARARRAE LEAARMVARR AHVYLELRGA QRRSSRARAP PAQRATGEGE EEEGGPMPPG
EDPIARLWLG ASKKERRDKV AFYLELVRRG RQQRQGYSEY LKDDADVWRR YDAMQRREGR
LDFDAMLLHF HRLLGEHEGA RRAFHAAHSH LIVDEYQDNS EMQAKLLELM VNQADPQVTV
VGDDDQCIYC FRGAEPGNFS RLPQRYEHCT LVDNYRSTAN ILRVAHVLLE ECARREAKTL
APTRETGAPV ELWKVATPAE QASELVRAMR ARHEEGVPWG EMACLFRCFK AGEMGSLHKP
LQQELSLRRV PYTLLGGKGL FELAAVLDAL AYLRLAALGS GEHDDEAFVR ILNRPKRRLP
EESVLRVVEH QRRALVEARR GLPVGLEAAA RQMVASGVGV KKSQRASLGS LLALLDELRD
ACVMAELPAM LLRVWSAAGL DAMHQRKERS QRRALAPLQG TARDRGDEGV ADAGGQGAGG
GDSSAMRLPS EVSSLVEVAT AFSTEYAARE RAAAGSERSL FALCRTYVLD HAAELQLSAL
PDCVVDELFA SRGRGRSVMR AFLTEVAMRS SAADAQDAAA EGSSKVSIST IHRAKGLEWC
DVYVPFLNDG LLPMGYREET GNTAQRHKPQ CAARRANGHC DLNCARAYRE ADAHARGTPE
ERHADEERRL AHVAATRAKD RLVFITVQLR REGAFAARNA MEPSPYERSL RAALPEETLV
TRVRGELQDA EE
//