ID A0A0K9NTF6_ZOSMR Unreviewed; 1219 AA.
AC A0A0K9NTF6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=ZOSMA_69G00340 {ECO:0000313|EMBL:KMZ59337.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ59337.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ59337.1}.
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DR EMBL; LFYR01001802; KMZ59337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NTF6; -.
DR STRING; 29655.A0A0K9NTF6; -.
DR OrthoDB; 47962at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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:UP000036987};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 941..1203
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 972
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1219 AA; 136509 MW; 31E0CCFE5CD81060 CRC64;
MESKLEQVRP ANQSFVQIPS SSTNEYPSSE FDASNSCQTI LNYSIQTGEE FSLEFIRERA
NVTKASRENA SANQDIGICK DKNRIIGTLQ SGLENETKVG LKGFAAIDDT RDSESGKWEM
AVTPGVPASD SNERGISNRH ASSVPSDHSA SNVRFFCSFG GKIMPRPSDG KLRYVGGATH
IIRLRNDISF SEVMRKTTSI YNKQHTIKYQ LPGEDLDSLI SVSCNEDLQN MMEECNFLEV
DSSQKLRMFL FASGDTNDVQ FGLGGIEIGS EIQYVAAVNG LEFGFDRGYS NHVLSKTTSS
VSGLDHLLNF GNEDGNTAMN RVELMPIRVN PVPLGELMYP QISIYDNSPS LYLHRTHAEH
AGGDDTFSQL AMLPMHTNGN QSNVDRIFPA HSPSLSMFNR KNDNQQSGRN LVSLAISQSL
LVENVEDQDI KKDDPKLPKH KSDGEQFQSL ENTLVSSTGH QYDVSAKFEE KSYSNMSEFV
TPKLLSQKVL DPEKKSSEFE VNNVKEFRNL HGDDRSCNCT SPCSSRAYQS EGIPREPFRD
ASLSIVRSKS HDSIGCQFLI PNSHSDLASE DSICEPLNKL QFKESPSLTQ QSILLAKLEC
PSSLEIKNGV TKIENSSKIH DLSQMNTHHE LVSDLNGKKY PYIFSYVGVN ESSTSQNRHN
KSSEITHIPC NLEDTESGNI ECPSTPIGDS KIDVIKPSIE TTFKQQVDSD SFPPYLNWAD
GYDLTYSNNI DYEPQLRDVL ADINNRFPPG MVSGIFKARN NKESSILHPL YKDKVALSVN
VHNPDKKNWS YFQNLAQDQF RKDVSLIDPD HDDQYFPNTT NEEVSPQQYN SAPQKSEYFE
LDHDDSQIGL GEVIQRGGSG INDDNDNPLH QGFLSPCIRM GMDGEGMQVE NPFLKAGDNL
RDPLPDDEEG KLESKNADCP SFLVSGDCHL NNLQSIKNED LEELRELGSG TFGTVYHGQW
RGTDVAIKRI KKSCLTCHLS EQERLTMEFW REAEILSNLH HPNVLAFYGV VTDGLDSTLA
TITEFMVDGS LSNVLRNGRS LDYRKELIIA MDTTFGMEYL HSKNIVHFDL KCDNLLVNLK
DPLRPICKVG DFGLSKIKQN TLVSGGVRGT LPWMAPELLN SSKVSEKVDV FSFGIVMWEI
LTGEEPYSDM HYGAIIGGIL NNILRPPIPE SCNPEWRMLM ERCWDADPMR RPSFTEIATH
LRLMYAAHRD KPLRMKAVK
//
