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Database: UniProt
Entry: R1F869_EMIHU
LinkDB: R1F869_EMIHU
Original site: R1F869_EMIHU 
ID   R1F869_EMIHU            Unreviewed;      1054 AA.
AC   R1F869;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOD31566.1, ECO:0000313|EnsemblProtists:EOD31566};
GN   ORFNames=EMIHUDRAFT_72279 {ECO:0000313|EMBL:EOD31566.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD31566.1};
RN   [1] {ECO:0000313|EMBL:EOD31566.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD31566.1};
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:EOD31566}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; KB864603; EOD31566.1; -; Genomic_DNA.
DR   RefSeq; XP_005783995.1; XM_005783938.1.
DR   STRING; 2903.R1F869; -.
DR   PaxDb; 2903-EOD31566; -.
DR   EnsemblProtists; EOD31566; EOD31566; EMIHUDRAFT_72279.
DR   GeneID; 17276839; -.
DR   KEGG; ehx:EMIHUDRAFT_72279; -.
DR   eggNOG; KOG0948; Eukaryota.
DR   HOGENOM; CLU_002902_0_1_1; -.
DR   OMA; IMLKNYN; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   CDD; cd18024; DEXHc_Mtr4-like; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
DR   Gene3D; 2.40.30.300; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR048392; MTR4-like_stalk.
DR   InterPro; IPR025696; MTR4_beta-barrel.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016438; SKI2-like.
DR   InterPro; IPR012961; Ski2/MTR4_C.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21408; MTR4-like_stalk; 1.
DR   Pfam; PF13234; MTR4_beta-barrel; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01142; DSHCT; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013827}.
FT   DOMAIN          118..274
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          376..569
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          34..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1054 AA;  115844 MW;  8E4235F24279B94D CRC64;
     MDGFDDSLFS AFESAPSAKV SSGLALDEPL LKRPAGAAAE AEDAAAKGKR LRGAPADAEK
     DDAAPALDPG TGRKACKHEV AMPPGLTASS EMVRLPKSTQ PPAREYSFEL DPFQQAAVNC
     IDREESVLVS AHTSAGKTVC AEYAIAVSLR DKQRVIYTSP IKALSNQKYR ELSETFGDVG
     LMTGDYTINV DASCLVMTTE ILRSMLYRGS EVMREVKWVI FDEVHYMRDK ERGVVWEEVM
     ILLPHSVRYV FLSATIPNAL QFAQWIAALH SQPCHVVYTD YRPTPLHHYM FGAGANGFHL
     VVDENSEFKP SGFEKATAKL SGGGGGRGGG KGGKGGGKGG GKGGGKGGRE KGPSDCFKLV
     RTVVSMGMEP LIVFAFGKRK VEKLAEEMGT LELTVHTERE SITQIYENAI QTLSDDDQVL
     PQVEKMLPLL QRGIAVHHSG LLPLLKELVE ILFQEGLVKL LFATETFAMG LNMPAKTVIF
     AELSKFDGAA FRRAPPPSGH TPHASPPAYL SSGEYIQMSG RAGRRGLDAR GTVVTMVDGS
     TDLAKVREML RGEADSLSSR FHLSYNMLLN CVRTETANIE NLIAKSFYTF QLQQAKPDLE
     RRQRELSAQL ASPDLAVDAR LLEVHALRAQ ERSLRKQLRP LLTDPKDTKA VHFLQPGRLV
     RFAREGGAGE EGEAREWGWG AIVSYKRLRP DKKEGKRGGD DLGTADQYHI DVLLRCDAGA
     EAAVEAGGEP APARDEESAE LHVLTLTLDR VDAFSKVKVS LPKDLRSSDG RHAVLKVLRE
     VERRFADGVP ELQHDEDLKV TTAAQEAAKL ARRRAGDERR RLGEEEIAAG LAVLRLRRAA
     EEEEKRVKRQ IREGQVALMK EELRGMRRVL RRLGHLSEDG VIGNKGRVAC EVSTSDELLV
     TELVFAGLFQ DLDPAQLAAL LSCLDGKKED PVAMIRTREM REPVERMREL AKRVATVVLE
     AKLPVDVDEY IARFATGLVD LVFDWCGGAK FADLCKMTDA YEGSIIRAMH RLEELLRQII
     DAAKVVGNEE LQAKCEAAQK LLVRDVVFCP SLYT
//
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