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Database: UniProt
Entry: A0A2P5G1J4_TREOI
LinkDB: A0A2P5G1J4_TREOI
Original site: A0A2P5G1J4_TREOI 
ID   A0A2P5G1J4_TREOI        Unreviewed;       721 AA.
AC   A0A2P5G1J4;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=TorRG33x02_002240 {ECO:0000313|EMBL:POO03920.1};
OS   Trema orientale (Charcoal tree) (Celtis orientalis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Trema.
OX   NCBI_TaxID=63057 {ECO:0000313|EMBL:POO03920.1, ECO:0000313|Proteomes:UP000237000};
RN   [1] {ECO:0000313|Proteomes:UP000237000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:POO03920.1}.
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DR   EMBL; JXTC01000001; POO03920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5G1J4; -.
DR   STRING; 63057.A0A2P5G1J4; -.
DR   InParanoid; A0A2P5G1J4; -.
DR   OrthoDB; 832546at2759; -.
DR   Proteomes; UP000237000; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR047117; PERK1-13-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47982:SF22; PROLINE-RICH RECEPTOR-LIKE PROTEIN KINASE PERK14; 1.
DR   PANTHER; PTHR47982; PROLINE-RICH RECEPTOR-LIKE PROTEIN KINASE PERK4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:POO03920.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        251..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          367..649
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..189
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   721 AA;  76897 MW;  B49F8684089EB835 CRC64;
     MSSPSPEPLS PAISPATPQP FPPSSSPPPS PLIIAPFPSP LRPSPPTPTS ITPLLPPAIS
     PAADNPQPPA ISPPAPAIPL PPPPSLSPPP PAATENASAS PPPPARPAPL PPPVLTSPPP
     TPKLVPGSPP PTRKTPLKPE LPSSPPPERS PSPATPPSPA TEKPNPLPPA TVEPQTPSTS
     PPLPLTAPGK SPVPVDSAPS PEANSFLKSP TRLASPPAPP LTLPSPSSSS KGSFPAAVEI
     QKPRPNTSPG FIVGFIGAGL VVLAVLVIVL ACICYRSSRR RKGQAHGLPV NHHKVTSLGP
     KGSSFLTQLP NPSLQSAPVK STALNSTPIN SEHELPETHQ STSPPPPTLT NGMVFTYDRL
     EEATGEFSDS NLIGEGGFGF VYKGILPGGK EVAVKRLKMG RGQGEREFQA EVDIISRVHH
     KHLVSLLGYC IRGIERLLVY EFVPNNTLEF HLHGKEQHVM EWTTRLKIAI GSAKGLAYLH
     EDCNPKIIHR DIKASNILLD FRFDAKVSDF GLAKSFSDTN THITHISTRV VGTFGYLAPE
     YASSGKLTEK SDVYSYGVML LELITGLPPI NSTDPMRNQG LVEWARPLLA QALEQGYFET
     LVDPRMQSKY DTVEMTRMVS CAAACVRHSA WLRPRMSQIV HALEGHSSLR DLHEGTTPGS
     SSLYSSSSCN YSVHQHKNDL NQFHLTIADD QDDSTKNWYS GSTSEYGLNP SVSSGEAHQT
     L
//
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