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Database: UniProt
Entry: A0A2G9GCK5_9LAMI
LinkDB: A0A2G9GCK5_9LAMI
Original site: A0A2G9GCK5_9LAMI 
ID   A0A2G9GCK5_9LAMI        Unreviewed;       524 AA.
AC   A0A2G9GCK5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=NDR serine/threonine kinase {ECO:0000313|EMBL:PIN02935.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:PIN02935.1};
GN   ORFNames=CDL12_24546 {ECO:0000313|EMBL:PIN02935.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN02935.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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:PIN02935.1}.
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DR   EMBL; NKXS01005705; PIN02935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9GCK5; -.
DR   STRING; 429701.A0A2G9GCK5; -.
DR   OrthoDB; 988261at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
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   CDD; cd21742; MobB_NDR_LATS-like; 1.
DR   CDD; cd05599; STKc_NDR_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356:SF346; PROTEIN KINASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 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:PIN02935.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIN02935.1}.
FT   DOMAIN          119..416
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          417..489
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   524 AA;  61018 MW;  9C13AC44DA57CDB8 CRC64;
     MDSARSWFQK FQPRDRFRSS TKKKDSMGSG REDPQPLSTE EASTLTKQRV AAAKQYIENH
     YKEQMKNLQE RKERRNLLEK KLADGDVSEE DQSNLLKFLE KKESEYMRLQ RHKMGVDDFE
     LLTMIGKGAF GEVRVCREKT TGSVYAMKKL KKSEMLRRGQ VEHVKAERNL LAEVDSNCIV
     KLYCSFQDEE YLYLIMEYLP GGDMMTLLMR KDTLTEDEAR FYVAETVLAI ESIHKHNYIH
     RDIKPDNLLL DRQGHLRLSD FGLCKPLDCS TIKEDFSVGE GLNGSSRSDE RSAPKRTQQE
     QLQHWQKNRR MLAYSTVGTP DYIAPEVLLK KGYGMECDWW SLGAIMFEML VGYPPFYSDD
     PMSTCRKIVN WRTHLKFPEE AKLSFEAKDL ISKLLCSVNQ RLGTKGADEI KAHPWFKGID
     WDNIYHMEAA FIPEVKDELD TQNFEKFEES EHHTQTSSRS GPWRKMLSSK DINFVGYTYK
     NFEIVNDYQV PGMAELKKKN TRSKRPTIKS LFEDESETSE TATQ
//
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