ID D7FZ54_ECTSI Unreviewed; 338 AA.
AC D7FZ54;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBJ32671.1};
GN ORFNames=Esi_0355_0017 {ECO:0000313|EMBL:CBJ32671.1};
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:CBJ32671.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ32671.1, 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; FN648548; CBJ32671.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FZ54; -.
DR STRING; 2880.D7FZ54; -.
DR EnsemblProtists; CBJ32671; CBJ32671; Esi_0355_0017.
DR eggNOG; ENOG502QQ8J; Eukaryota.
DR InParanoid; D7FZ54; -.
DR OrthoDB; 118474at2759; -.
DR Proteomes; UP000002630; Chromosome LG15.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR46192; BROAD-RANGE ACID PHOSPHATASE DET1; 1.
DR PANTHER; PTHR46192:SF11; BROAD-RANGE ACID PHOSPHATASE DET1; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT REGION 34..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 209
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 125..132
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 338 AA; 38514 MW; 2DF6042F081A9456 CRC64;
MTTNMFAVSP ACHPRHAFAL ASRVAGGNDC TRKSGLGKGS HARFGTRRAA SGHTPLQFQV
GDSSLSSRRK ASHRPGARMH HPHDQRRFLR GSGQHFPHSD QESLGLFSGD GKRRVVKPER
IIIVRHGESL GNRDESTYVH VPDWKIPLTK KGFGEGQKAG EKIKEYIGDK PLFIYTSPYL
RTKQTLAGMV EAFDTNYIVG VREEPRLTEQ QFGNFQNLAT IVNSKAERAR FGRFYYRFPQ
GESGLDVYNR ATSFIATMFR DFANESIARD DLNVIIVTHG LTLRLLVMRW FQYSIADFEE
TLNPENGSFV VMERKEKEDT DSRFFKDVSA ERRDLRHW
//