ID D8LQ45_ECTSI Unreviewed; 666 AA.
AC D8LQ45;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Phosphoesterase, RecJ-like protein {ECO:0000313|EMBL:CBN77425.1};
GN ORFNames=Esi_0059_0033 {ECO:0000313|EMBL:CBN77425.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN77425.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN77425.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|ARBA:ARBA00007265}.
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DR EMBL; FN648807; CBN77425.1; -; Genomic_DNA.
DR AlphaFoldDB; D8LQ45; -.
DR STRING; 2880.D8LQ45; -.
DR EnsemblProtists; CBN77425; CBN77425; Esi_0059_0033.
DR eggNOG; ENOG502R7NG; Eukaryota.
DR InParanoid; D8LQ45; -.
DR OMA; SATCHAT; -.
DR OrthoDB; 36985at2759; -.
DR Proteomes; UP000002630; Chromosome LG27.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd04595; CBS_pair_DHH_polyA_Pol_assoc; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR PANTHER; PTHR47788:SF1; A-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR47788; POLYA POLYMERASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01368; DHH; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..666
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003117377"
FT DOMAIN 516..574
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 579..637
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 29..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 72152 MW; AE8F2B7054A4B845 CRC64;
MCQRLAVPFL LIVQASLGYC PPNALRTTDT SAPSWFNGHP SARQRRSSHS RHQQRPRGTG
RRGSSSNPSA TCHATHLHHQ QGPGRNQRAG SGSAIAAASG SGSGGEGGCR GDGGVTGAAV
GGRRRRTFLT GLRAKRVAGE GVSEEQEKAR AAHRARLAAR PKPPPREHVP PPPNTQALNV
VLTHTTADFD TLAAAVGLAK LWQDERPDDE CCVCLPRGTH PVVKRFLTLH KNLFPIKALR
DIDHDRIFRV GLVDAQKIDR IGTAASLLAN ATEVHVVDHH NEQSSDINAT SIVIEEVGSV
STIITEKLQE RGLQMEEAEA TLLALGVHSD TGSLTFDSAT ARDAVALAWL MEQGSSQQAI
AEYGHAALSQ EQQSTLTECI NNLNRTSLNG ATVSTALVQL DSYVNGMAAV AQNVLDVTDS
DVFMLGAHFP QKLGRDPTHM VVIGRARPRV SKVNLDDLMS NYGGGGHRKA AAASLRLSSV
TMRGGEPATA AGIMQDLVDR IFVEQISELE VAEDIMTAPV QTCGATESIE EVSKVLSRHD
IRGMPVVDEE GKVLGLISCK EVEKTVKLGR QHELVKGWMK EQFPVADAQD PLHEVEEKFI
KGDLGRLPVV REGKLVGLIT RADMLRQHRF YEGLHYENRA FATPVDSPVR KMLANLRKTL
KKYDEE
//
