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Database: UniProt
Entry: A9TSD3_PHYPA
LinkDB: A9TSD3_PHYPA
Original site: A9TSD3_PHYPA 
ID   A9TSD3_PHYPA            Unreviewed;       418 AA.
AC   A9TSD3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   26-FEB-2020, entry version 65.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ53700.1};
GN   ORFNames=PHYPA_003572 {ECO:0000313|EMBL:PNR60779.1}, PHYPADRAFT_149790
GN   {ECO:0000313|EMBL:EDQ53700.1};
OS   Physcomitrella patens subsp. patens (Moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218;
RN   [1] {ECO:0000313|EMBL:EDQ53700.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S., Yamaguchi K., Sugano S., Kohara Y., Fujiyama A.,
RA   Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L.,
RA   Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A.,
RA   Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K.,
RA   Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B.,
RA   Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.H.,
RA   Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J.,
RA   Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S.,
RA   Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
RN   [2] {ECO:0000313|EMBL:PNR60779.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727};
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA   Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA   Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT   structure and evolution.";
RL   Plant J. 93:515-533(2018).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000256|RuleBase:RU003633}.
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DR   EMBL; DS545193; EDQ53700.1; -; Genomic_DNA.
DR   EMBL; ABEU02000002; PNR60779.1; -; Genomic_DNA.
DR   RefSeq; XP_001781520.1; XM_001781468.1.
DR   STRING; 3218.PP1S304_59V6.1; -.
DR   eggNOG; ENOG410IIN2; Eukaryota.
DR   eggNOG; COG3424; LUCA.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   InParanoid; A9TSD3; -.
DR   OMA; TIMAIGR; -.
DR   Proteomes; UP000006727; Chromosome 2.
DR   GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR012328; Chalcone/stilbene_synth_C.
DR   InterPro; IPR001099; Chalcone/stilbene_synthase_N.
DR   InterPro; IPR011141; Polyketide_synthase_type-III.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11877; PTHR11877; 1.
DR   Pfam; PF02797; Chal_sti_synt_C; 1.
DR   Pfam; PF00195; Chal_sti_synt_N; 1.
DR   PIRSF; PIRSF000451; PKS_III; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003633};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW   Transferase {ECO:0000256|RuleBase:RU003633}.
FT   DOMAIN          39..256
FT                   /note="Chal_sti_synt_N"
FT                   /evidence="ECO:0000259|Pfam:PF00195"
FT   DOMAIN          266..417
FT                   /note="Chal_sti_synt_C"
FT                   /evidence="ECO:0000259|Pfam:PF02797"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000451-1"
SQ   SEQUENCE   418 AA;  45325 MW;  54CD061B0F0F95FA CRC64;
     MASRRVEAAF DGQAVELGAT IPAANGNGTH QSIKVPGHRQ VTPGKTTIMA IGRAVPANTT
     FNDGLADHYI QEFNLQDPVL QAKLRRLCET TTVKTRYLVV NKEILDEHPE FLVDGAATVS
     QRLAITGEAV TQLGHEAATA AIKEWGRPAS EITHLVYVSS SEIRLPGGDL YLAQLLGLRS
     DVNRVMLYML GCYGGASGIR VAKDLAENNP GSRVLLITSE CTLIGYKSLS PDRPYDLVGA
     ALFGDGAAAM IMGKDPIPVL ERAFFELDWA GQSFIPGTNK TIDGRLSEEG ISFKLGRELP
     KLIESNIQGF CDPILKRAGG LKYNDIFWAV HPGGPAILNA VQKQLDLAPE KLQTARQVLR
     DYGNISSSTC IYVLDYMRHQ SLKLKEANDN VNTEPEWGLL LAFGPGVTIE GALLRNLC
//
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