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G11A_ORYSI
ID   G11A_ORYSI              Reviewed;         589 AA.
AC   A2YBX5; P47997; Q5Z583;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein kinase G11A;
DE            EC=2.7.11.1;
GN   ORFNames=OsI_021818;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 54-584.
RC   STRAIN=cv. IR36; TISSUE=Leaf;
RX   PubMed=2541432; DOI=10.1073/pnas.86.9.3140;
RA   Lawton M.A., Yamamoto R.T., Hanks S.K., Lamb C.J.;
RT   "Molecular cloning of plant transcripts encoding protein kinase homologs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3140-3144(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 327-434.
RC   STRAIN=cv. IR36; TISSUE=Seedling;
RX   PubMed=2026273; DOI=10.1016/0014-5793(91)80453-a;
RA   Feng X.H., Kung S.D.;
RT   "Diversity of the protein kinase gene family in rice.";
RL   FEBS Lett. 282:98-102(1991).
CC   -!- FUNCTION: May play a role in the regulation of metabolism and signal
CC       transduction processes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CM000131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; J04556; AAA33905.1; -; mRNA.
DR   PIR; B30311; B30311.
DR   AlphaFoldDB; A2YBX5; -.
DR   SMR; A2YBX5; -.
DR   STRING; 39946.A2YBX5; -.
DR   PRIDE; A2YBX5; -.
DR   Proteomes; UP000007015; Chromosome 6.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..589
FT                   /note="Protein kinase G11A"
FT                   /id="PRO_0000300872"
FT   DOMAIN          195..533
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         201..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        215
FT                   /note="N -> S (in Ref. 2; AAA33905)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="K -> E (in Ref. 2; AAA33905)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   589 AA;  64825 MW;  E686A223D4DC60FF CRC64;
     MASKAMPRAP PAAPNLQSLK LCSQNDSSLE TTSPSKRSAL VPGRSAESSK PNSEVVQKEQ
     KSTQHQNESI DLTGSNDPAE VKAEGNLVPK RLADEEKGVV EDGIANGSLK SSSALGKEHG
     IASASGSARL VGRSETGERG FSSSRCRPST SSDVSDESAC SSISSVTKPH KANDSRWEAI
     QMIRTRDGIL GLSHFKLLKK LGCGDIGSVY LSELNGTKSY FAMKVMDKAS LASRKKLLRA
     QTEKEILQCL DHPFLPTLYT HFETDKFSCL VMEFCPGGDL HTLRQRQRGK YFPEQAVKFY
     VAEILLAMEY LHMLGIIYRD LKPENVLVRE DGHIMLSDFD LSLRCAVSPT LIRSSNPDAE
     ALRKNNQAYC VQPACVEPSC MIQPSCATPT TCFGPRFFSK SKKDRKPKPE VVNQVSPWPE
     LIAEPSDARS MSFVGTHEYL APEIIKGEGH GSAVDWWTFG IFLYELLFGK TPFKGSGNRA
     TLFNVIGQPL RFPEYPVVSF SARDLIRGLL VKEPQQRLGC KRGATEIKQH PFFEGVNWAL
     IRCASPPEVP RPVEIERPPK QPVSTSEPAA APSDAAQKSS DSYLEFDFF
 
 
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