ID B5Y5G1_PHATC Unreviewed; 1012 AA.
AC B5Y5G1;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=G-protein coupled receptors family 3 profile domain-containing protein {ECO:0000259|PROSITE:PS50259};
GN ORFNames=PHATR_44133 {ECO:0000313|EMBL:ACI65649.1};
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:ACI65649.1, ECO:0000313|Proteomes:UP000000759};
RN [1] {ECO:0000313|EMBL:ACI65649.1, ECO:0000313|Proteomes:UP000000759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:ACI65649.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00006654}.
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DR EMBL; CP001142; ACI65649.1; -; Genomic_DNA.
DR RefSeq; XP_002186179.1; XM_002186143.1.
DR AlphaFoldDB; B5Y5G1; -.
DR PaxDb; 2850-Phatr44133; -.
DR EnsemblProtists; Phatr3_J44133.t1; Phatr3_J44133.p1; Phatr3_J44133.
DR GeneID; 7203886; -.
DR KEGG; pti:PHATR_44133; -.
DR eggNOG; KOG4419; Eukaryota.
DR HOGENOM; CLU_297629_0_0_1; -.
DR InParanoid; B5Y5G1; -.
DR OrthoDB; 2970339at2759; -.
DR Proteomes; UP000000759; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR017978; GPCR_3_C.
DR PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 937..958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..985
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 846..986
FT /note="G-protein coupled receptors family 3 profile"
FT /evidence="ECO:0000259|PROSITE:PS50259"
SQ SEQUENCE 1012 AA; 111643 MW; 31F1682104CAD507 CRC64;
MTTIHIIDSW ADLLGGITLS DCRNVTDPSC VGGVANVAAF ARHLTRSGAS VTDSPSGGTA
EDIEEPYIVT PRLDRYSPFV QMHPLGWSVN RLIFVEVLQW KFFISSPALL YLSSTARGST
NGSSTISTNS SLMSDLQTDE LPFLLTNVAV PPENDWYPYT KAIYFDETTH LAFLSVADSD
EPLNAPQIES ATGALNYIAR LNKESDCDAF VDDGGGTAVA LGSSWDNRTC WIPVVAFGDS
ENRWNNFLLA MTALENPPSL IMDIEGHDAR FFTPQKYNQT WVSSYKMNST TYRQQSIVLA
EDSRTIVSVT ATAIPLNELP DEFKDNIYTS HVTRMYELGQ EAANKDPIVG TSTFMPIARI
DQYRRCMGGE CEIGNLFTDA LRWYSSADVA FVSSGGLRGQ GWPEGVVQMS NLWESLPFPN
TLCSGTMTGV SLFKLFNYST SVANFEVKET VSGGQLLQVS GARLRYNTKL PQGASRMVRL
EIWDKNANQY APVQRLQLYK FATDNFLCET NIPYPELLGQ NFYIDGEVPG VVRDDLHQNI
VADYLTQLNT TYQATIEGRL INDTTVLDAM NLVQIEGGCG QGTYWVFTQQ SCKVCPNTDQ
VYFGKKELEF ASESGSSKPV EGRFEILNNA GFPVSVGPRS FPFWVTLTVF LCNGTIPIDP
IPAGVTRVLQ SGEKLTVGLS ISSEQLEAGT AVATGSFSVV DGGSFPGCIG NEISFDILVR
VDPSRELNQI GGIRWVGWSL FMVLVFSAMF FYTWVCQHER IAVVRAMHRL FLNTVCLGIV
VLGSVLIPVG FDDGAFSENI CNSACASIPW ISAAGLSTIF AAMYRKLGSI VGKNEDAREF
RGRRVVLTFA VFFGLNASIL VPWSILAPLH WDRTPLVQEE WKSYGRCSTS DTSSLAFVVM
AGVLNVSGFV LICRLAYKAQ QIQDRRDQFD QAKSISLALY SWIQLAVVGI PVLSLISAET
TRARYFMIVA LIFALCISML LSLFIPMQMQ KTMQSVRTLS LGSRFLSSFR SR
//
