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Database: UniProt/TrEMBL
Entry: A9TQU1_PHYPA
LinkDB: A9TQU1_PHYPA
Original site: A9TQU1_PHYPA 
ID   A9TQU1_PHYPA            Unreviewed;       704 AA.
AC   A9TQU1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   29-OCT-2014, entry version 49.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ54241.1};
GN   ORFNames=PHYPADRAFT_224556 {ECO:0000313|EMBL:EDQ54241.1};
OS   Physcomitrella patens subsp. patens (Moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727};
RN   [1] {ECO:0000313|EMBL:EDQ54241.1, 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.,
RA   Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T.,
RA   Kuroki Y., Toyoda A., Suzuki Y., Hashimoto S.-I., Yamaguchi K.,
RA   Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N.,
RA   Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H.,
RA   Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K.,
RA   Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A.,
RA   Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T.,
RA   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.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the
RT   conquest of land by plants.";
RL   Science 319:64-69(2008).
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DR   EMBL; DS545180; EDQ54241.1; -; Genomic_DNA.
DR   RefSeq; XP_001780981.1; XM_001780929.1.
DR   UniGene; Ppa.978; -.
DR   ProteinModelPortal; A9TQU1; -.
DR   SMR; A9TQU1; 12-674.
DR   STRING; 3218.JGI224556; -.
DR   GeneID; 5944167; -.
DR   KEGG; ppp:PHYPADRAFT_224556; -.
DR   InParanoid; A9TQU1; -.
DR   KO; K04079; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:InterPro.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006727};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727}.
SQ   SEQUENCE   704 AA;  80742 MW;  E1628FD5632B2FFC CRC64;
     MADVTMSGPE VETFAFQAEI NQLLSLIINT FYSNKEIFLR ELISNSSDAL DKIRFESLTD
     KSKLDGQPEL FIHIVPDKAN NTLSIIDSGI GMTKADMVNN LGTIARSGTK EFMEALSAGA
     DVSMIGQFGV GFYSAYLVAE KVVVTSKHND DEQYIWESQA GGSFTITRDT SGEPLGRGTH
     IKLYLKEDQL EYLEERRLKD LVKKHSEFIS YPISLWTEKT TEKEVSDDED EDDKKDEEGK
     IEEVDEEKEK DKKKKKVKEI SREWTLINKQ KPIWMRKPED VTKEEYAAFY KSLTNDWEEH
     LAVKHFSVEG QLEFKSVLFV PKRAPFDLFD SRKKQNNIKL YVRRVFIMDN CEELIPEYLG
     FVKGVVDSED LPLNISRETL QQSKILKVIR KNLVKKCMEM FSEIAENKED YQKFYEAFSK
     NLKLGIHEDS QNRSKLADLL RYHSTKSGDE MTSLKDYVTR MKEGQKDIYY ITGESKKAVE
     NSPFLEKLKR RGYEVLFMVD AIDEYAVGQL KEFDGKKLVS ATKEGLVLED TEEEKKKKEE
     KKARFEPLCK TIKDILGDKV EKVVVSDRIV DSPCVLVTGE YGWSANMERI MKAQALRDSS
     MSSYMSSKKT MEINPDNQIM EELRKRAEVD KNDKSVKDLV LLLFETALLT SGFSLEEPNT
     FGNRIHRMLK LGLSIDDDAT DADADMPALE ADVDEEGSKM EEVD
//
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