ID R0FU98_9BRAS Unreviewed; 1191 AA.
AC R0FU98;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CARUB_v10022521mg {ECO:0000313|EMBL:EOA26472.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA26472.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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DR EMBL; KB870808; EOA26472.1; -; Genomic_DNA.
DR RefSeq; XP_006293574.1; XM_006293512.1.
DR AlphaFoldDB; R0FU98; -.
DR Proteomes; UP000029121; 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; cd06410; PB1_UP2; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000270; PB1_dom.
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; PTHR23257:SF962; KINASE SUPERFAMILY WITH OCTICOSAPEPTIDE_PHOX_BEM1P DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 908..1173
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 935
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1191 AA; 132095 MW; 0920FCEDCE2B8B68 CRC64;
MDRHLDKENM DQAKGYEHVR YTPPDPRDEG LGSINQRFPH DPSTNFNPNV RPPDYGISTP
ARPVLNYSIQ TGEEFAFEFM RDRVIMKPQF IPSVYGDPSG MPVSVNLTPM GMVHSVSESG
SNATVLNTEE KRLTFEQERK PPSRIEDKTY HELVQSAPVT SSRNETGQSR HSLISSRASD
SSLNQAKFLC SFGGKIIPRP RDQKLRYVGG QTRIIRISKT ISFQELMHKM KEMFPEARTI
KYQLPGEDLD ALVSVSSDED LQNMMEECIV FGNGGSEKPR MFLFSSSDIE EAQFVMEHAE
GDSEVQYVVA VNGMDLSSRK SSLGTNAPGN NLDELLQGNF DRKINRAITE PAVASVAPLA
GNESLSASQT SQPVTAISTG NEPFSQPYLG QQLHFTGLGN HQVYTSAHMA SIGYIDENGS
GPLHVQPQPH YIPYSVNPET PLETLVPHYP QKPEQGLLRE DQIFHVQDSE ASSKEAKMRR
DDSFQKVNDP ANVSIVESNL SAKEPKMKRE SSTPRVSEYS VSSMPDDLIV PDHLVKEEAT
IVTQTSSSTP DLSSSALPDK ILRKSQDHVE KNLSAKEPKM RKENSTTRVN EYSVSSVSSD
SMVPDHALKE EAPNSMKLSN SIPDPKSFVY PEKNLRTPQD YVPKTGALDT ANEGTAKNQD
KPFCLPGGLS ASGHGTSDAN SANLSNVDQP VIHHRVFHSE RTLRDPTETN RLSKSDDSLA
SQFVMAQTTS DAFLPISESS ETSHEANMES QNVHSTAPVR SAPESIWTAD GSMSQSEKRN
LESNVPEHDE FERKDLSLMD QDHPGFPTSL TNTNGVPIDY SYPPLQSEKV ASSQINSQIQ
FDGNIQPEMS TTTIADLNTV NTQEDYGQSQ IKGAESTDVT LNTGVPLIDF MVADSGMRSL
QVIKNDDLEE LKELGSGTFG TVYHGKWRGT DVAIKRIKRS CFIGRSSEQE RLTSEFWHEA
EILSKLHHPN VMAFYGVVKD GPGGTLATVT EYMVNGSLRH VLLSNRHLDR RKRLIIAMDA
AFGMEYLHSK SIVHFDLKCD NLLVNLKDPA RPICKVGDFG LSKIKRNTLV TGGVRGTLPW
MAPELLSGSS SKVSEKVDVF SFGIVLWEIL TGEEPYANMH YGAIIGGIVN NTLRPTVPNY
CDPEWRMLME QCWAPDPFVR PAFPEIARRL RTMSSSAVHT KPHAVNHQIH K
//
