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Database: UniProt
Entry: D7FS17_ECTSI
LinkDB: D7FS17_ECTSI
Original site: D7FS17_ECTSI 
ID   D7FS17_ECTSI            Unreviewed;       332 AA.
AC   D7FS17;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Nucleoside phosphorylase domain-containing protein {ECO:0000259|Pfam:PF01048};
GN   ORFNames=Esi_0226_0037 {ECO:0000313|EMBL:CBJ30958.1};
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:CBJ30958.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBJ30958.1, 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).
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DR   EMBL; FN648405; CBJ30958.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7FS17; -.
DR   STRING; 2880.D7FS17; -.
DR   EnsemblProtists; CBJ30958; CBJ30958; Esi_0226_0037.
DR   eggNOG; ENOG502RXRP; Eukaryota.
DR   InParanoid; D7FS17; -.
DR   OMA; IFHLHLK; -.
DR   OrthoDB; 22563at2759; -.
DR   Proteomes; UP000002630; Chromosome LG26.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd17769; NP_TgUP-like; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR43691:SF14; URIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT   DOMAIN          87..326
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   REGION          58..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  35040 MW;  8DD56AC0D9645116 CRC64;
     MSATDLYLLH ANAVPLTADG RVLHLELRSG EVANNIVTVG SEGRGEILAS LLDGTTTTAA
     GTPKDDNNDN INDHDNNTKN GSSSTTTTTT RRSKRGFVTH TGTYNGVPVS IVLINMGYPN
     MDFFVREVRA VTTGPLRIVR LGSCAGLRPD LPVGSVAVAS EGSVMIRQNP DAWEGTAARG
     ETQGEPYLFH GVAPADEELS EALLKELKRS LDGKAGGSDG GGGTAVVGCL NASADSFYSS
     QGRLDPSFED RNSDILSSLL ERHPSAGSFE METFQLLHLA RLCRKSKVQA SAATIVLANR
     IADDAIAIDR ISRIERAAGE AALRAVTSFG DP
//
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