ID A0A067E1L5_CITSI Unreviewed; 982 AA.
AC A0A067E1L5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=CISIN_1g036229mg {ECO:0000313|EMBL:KDO48988.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO48988.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO48988.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; KK785125; KDO48988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067E1L5; -.
DR PaxDb; 2711-XP_006468119-1; -.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF585; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 10.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 6.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..982
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001636085"
FT TRANSMEM 724..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 958..977
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 782..982
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 982 AA; 108354 MW; 2A6463E08A5DA4D4 CRC64;
MERVHSLSMM SRFLFLHCLI LISLLTAAAT ANTSSITTDQ DALLALKAHI THDPTNFLAK
NWNTSTPVCN WTGVTCDVHS HRVKVLNISH LNLTGTIPSQ LWNLSSLQSL NLGFNRLSGS
IPSAIFTLYT LKYVNFRGNQ LSGAFPSFIF NKSSLQHLDF SYNALSGEIP ANICSNLPFL
ESISLSQNMF HGRIPSALSN CKYLEILSLS INNLLGAIPK EIGNLTKLKE LYLGYSGLQG
EIPREFGNLA ELELMALQVS NLQGEIPQEL ANLTGLEVLK LGKNFLTGEI PPEIHNLHNL
KLLDLSHNKL VGAVPATIFN MSTLTGLGLQ SNSLSGSLSS IADVQLPNLE ELRLWSNNFS
GTIPRFIFNA SKLSVLELGR NSFSGFIPNT FGNLRNLRLM TLHYNYLTSS NLELSFLSSF
SNCKSLTYIG LSNNPLDGIL PRMSMGNLSH SLEYFDMSYC NVSGGFPKEI GNLTNLIGIY
LGGNKLNGSI PITLGKLQKL QGLHLEDNKL EGPIPDDICR LTKLYELGLS GNKLSGSIPA
CFSNLASLGT LSLGSNKLTS IPLTIWNLKG MLYLNFSSNF FTGPLPLDIG NLKVLIGIDF
STNNFSDVIP TVIGGLTNLQ YLFLGYNRLQ GSISESFGDL ISLKSLNLSN NNLSRSIPIS
LEKLSYLEDL DLSFNKLKGE IPKGGSFGNF SAKSFEGNEL LCGSPNLQVP PCKTSIHHKS
RKNVLLLGIV LPLSTIFIIV VILLIVRYRK RVKQPPNDAN MPPIATCRRF SYLELCRATN
RFSENNLIGR GGFGSVYKAR IGEGMEVAVK VFDLQCGRAF KSFDVECEMM KSIRHRNLIK
VISSCSTEEF KALILEYMPH GSLEKSLYSS NYILDIFQRL NIMVDVATTL EYLHFGYSAP
VIHCDLKPSN VLLDDNMVAH LSDFGIAKLL IGEDQSITQT QTLATIGYMA PGLFHVKYIL
FVVNFLTSYS FLMIFIGRGN YY
//
