ID B7FPD3_PHATC Unreviewed; 742 AA.
AC B7FPD3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=protein-tyrosine sulfotransferase {ECO:0000256|ARBA:ARBA00013262};
DE EC=2.8.2.20 {ECO:0000256|ARBA:ARBA00013262};
GN ORFNames=PHATRDRAFT_42741 {ECO:0000313|EMBL:EEC51154.1};
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC51154.1, ECO:0000313|Proteomes:UP000000759};
RN [1] {ECO:0000313|EMBL:EEC51154.1, ECO:0000313|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC51154.1,
RC ECO:0000313|Proteomes:UP000000759};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2] {ECO:0000313|Proteomes:UP000000759}
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine
CC 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein];
CC Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000411};
CC -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {ECO:0000256|ARBA:ARBA00009988}.
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DR EMBL; CM000605; EEC51154.1; -; Genomic_DNA.
DR RefSeq; XP_002176691.1; XM_002176655.1.
DR AlphaFoldDB; B7FPD3; -.
DR STRING; 556484.B7FPD3; -.
DR PaxDb; 2850-Phatr42741; -.
DR EnsemblProtists; Phatr3_EG02469.t1; Phatr3_EG02469.p1; Phatr3_EG02469.
DR GeneID; 7196127; -.
DR KEGG; pti:PHATRDRAFT_42741; -.
DR eggNOG; ENOG502S5PI; Eukaryota.
DR HOGENOM; CLU_374496_0_0_1; -.
DR InParanoid; B7FPD3; -.
DR OMA; MANMFER; -.
DR OrthoDB; 315927at2759; -.
DR Proteomes; UP000000759; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR026634; TPST-like.
DR PANTHER; PTHR12788:SF10; PROTEIN-TYROSINE SULFOTRANSFERASE; 1.
DR PANTHER; PTHR12788; PROTEIN-TYROSINE SULFOTRANSFERASE 2; 1.
DR Pfam; PF13469; Sulfotransfer_3; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 278..311
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 83397 MW; 63EC31321727BDF6 CRC64;
MMSEDKRSRD APSDLSEGGV TASHSIESLE PRNSLTGAMF LYWVVPVLLF AVFSRLTVDT
NVGTVKTKPL KSIPIQLDQD YIDSTPSVRP TQAPIPVRQA DNPSLPSRWP TSYRATIEKI
ERRRPHWKNK PTLSPSAQPS AADSKKLEDT VTSSPLPNGR NAGGRPRGRA SDPNRLMIIE
KIDAMRQDVV DDPADIYKAI EFADALRFYD LQYREGGTYE TEAIDTYNKV VGLVVAKRNK
LVAANQPTNV SLNGSRTKSV SDEVTLDYAS KSADGLVCAV YTALGKVYYM ANMFERAAKS
YTECLEIAPS YLDAVNARAS TNIILGKYAE AGADFLKVVR EDEQRLFPDS FSGIARVLEA
QEDAIPGGWG PVVELLDQLI PSFEAQWASA PPQTKQIFGN GLNRFHHSLF TYHDKKTKAY
SEAWHHLTEA YQYKMANLPV WQSGQESTKS FQTKQIFKPG FWSPGVGSET ETPIFIIGFV
RSGSTLLERI LDAHPKIVGT GENSVFNGRL DDIRNKIVQV SMGGRREQLG EVTRRLAEEV
VDGMRKRWRI LQATTETSGV RDDIPLRFVD KMLTNYYNVG FIHLLYPKAL ILHVYRNPMD
TIFSAYKHEF PSGTLDYTSD FDALAELYHS YRDIIDHWDD ALPGRVTHVR YEDMVQDMPG
MARAIIDATG LPWDDSVLQF HKQKHAVNTL STTQVRKGIY KDSLKSWAKY ENELQPMVQL
IGGRVHFNIK ATLQPVPTKE EL
//
