ID POM1_SCHPO Reviewed; 1087 AA. AC Q09690; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=DYRK-family kinase pom1; DE EC=2.7.12.1 {ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:25720772}; GN Name=pom1 {ECO:0000303|PubMed:9573052}; ORFNames=SPAC2F7.03c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP FUNCTION. RC STRAIN=972 / ATCC 24843; RX PubMed=9573052; DOI=10.1101/gad.12.9.1356; RA Baehler J., Pringle J.R.; RT "Pom1p, a fission yeast protein kinase that provides positional information RT for both polarized growth and cytokinesis."; RL Genes Dev. 12:1356-1370(1998). RN [3] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11230130; DOI=10.1093/emboj/20.5.1064; RA Baehler J., Nurse P.; RT "Fission yeast Pom1p kinase activity is cell cycle regulated and essential RT for cellular symmetry during growth and division."; RL EMBO J. 20:1064-1073(2001). RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11950884; DOI=10.1242/jcs.115.8.1651; RA Niccoli T., Nurse P.; RT "Different mechanisms of cell polarisation in vegetative and shmooing RT growth in fission yeast."; RL J. Cell Sci. 115:1651-1662(2002). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=14663827; DOI=10.1002/yea.1054; RA Niccoli T., Arellano M., Nurse P.; RT "Role of Tea1p, Tea3p and Pom1p in the determination of cell ends in RT Schizosaccharomyces pombe."; RL Yeast 20:1349-1358(2003). RN [6] RP FUNCTION. RX PubMed=17140794; DOI=10.1016/j.cub.2006.11.024; RA Padte N.N., Martin S.G., Howard M., Chang F.; RT "The cell-end factor pom1p inhibits mid1p in specification of the cell RT division plane in fission yeast."; RL Curr. Biol. 16:2480-2487(2006). RN [7] RP FUNCTION. RX PubMed=16988828; DOI=10.1007/s00294-006-0099-5; RA La Carbona S., Le Goff X.; RT "Spatial regulation of cytokinesis by the Kin1 and Pom1 kinases in fission RT yeast."; RL Curr. Genet. 50:377-391(2006). RN [8] RP FUNCTION. RX PubMed=17077120; DOI=10.1242/jcs.03261; RA Celton-Morizur S., Racine V., Sibarita J.B., Paoletti A.; RT "Pom1 kinase links division plane position to cell polarity by regulating RT Mid1p cortical distribution."; RL J. Cell Sci. 119:4710-4718(2006). RN [9] RP FUNCTION. RX PubMed=17543869; DOI=10.1016/j.devcel.2007.03.015; RA Huang Y., Chew T.G., Ge W., Balasubramanian M.K.; RT "Polarity determinants Tea1p, Tea4p, and Pom1p inhibit division-septum RT assembly at cell ends in fission yeast."; RL Dev. Cell 12:987-996(2007). RN [10] RP FUNCTION, AND INTERACTION WITH RGA4. RX PubMed=18328707; DOI=10.1016/j.cub.2008.02.005; RA Tatebe H., Nakano K., Maximo R., Shiozaki K.; RT "Pom1 DYRK regulates localization of the Rga4 GAP to ensure bipolar RT activation of Cdc42 in fission yeast."; RL Curr. Biol. 18:322-330(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=19474792; DOI=10.1038/nature08054; RA Martin S.G., Berthelot-Grosjean M.; RT "Polar gradients of the DYRK-family kinase Pom1 couple cell length with the RT cell cycle."; RL Nature 459:852-856(2009). RN [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19474789; DOI=10.1038/nature08074; RA Moseley J.B., Mayeux A., Paoletti A., Nurse P.; RT "A spatial gradient coordinates cell size and mitotic entry in fission RT yeast."; RL Nature 459:857-860(2009). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH TEA4. RX PubMed=21703453; DOI=10.1016/j.cell.2011.05.014; RA Hachet O., Berthelot-Grosjean M., Kokkoris K., Vincenzetti V., RA Moosbrugger J., Martin S.G.; RT "A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at RT the plasma membrane."; RL Cell 145:1116-1128(2011). RN [15] RP SUBCELLULAR LOCATION. RX PubMed=22342545; DOI=10.1016/j.devcel.2012.01.001; RA Saunders T.E., Pan K.Z., Angel A., Guan Y., Shah J.V., Howard M., Chang F.; RT "Noise reduction in the intracellular pom1p gradient by a dynamic RT clustering mechanism."; RL Dev. Cell 22:558-572(2012). RN [16] RP FUNCTION. RX PubMed=22684255; DOI=10.1038/ncb2514; RA Grallert A., Connolly Y., Smith D.L., Simanis V., Hagan I.M.; RT "The S. pombe cytokinesis NDR kinase Sid2 activates Fin1 NIMA kinase to RT control mitotic commitment through Pom1/Wee1."; RL Nat. Cell Biol. 14:738-745(2012). RN [17] RP FUNCTION. RX PubMed=24047646; DOI=10.4161/cc.26462; RA Wood E., Nurse P.; RT "Pom1 and cell size homeostasis in fission yeast."; RL Cell Cycle 12:3228-3236(2013). RN [18] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24316795; DOI=10.4161/cc.27411; RA Bhatia P., Hachet O., Hersch M., Rincon S.A., Berthelot-Grosjean M., RA Dalessi S., Basterra L., Bergmann S., Paoletti A., Martin S.G.; RT "Distinct levels in Pom1 gradients limit Cdr2 activity and localization to RT time and position division."; RL Cell Cycle 13:538-552(2014). RN [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=24508166; DOI=10.1016/j.cub.2014.01.009; RA Deng L., Baldissard S., Kettenbach A.N., Gerber S.A., Moseley J.B.; RT "Dueling kinases regulate cell size at division through the SAD kinase RT Cdr2."; RL Curr. Biol. 24:428-433(2014). RN [20] RP FUNCTION. RX PubMed=24982431; DOI=10.1083/jcb.201311097; RA Rincon S.A., Bhatia P., Bicho C., Guzman-Vendrell M., Fraisier V., RA Borek W.E., Alves F.L., Dingli F., Loew D., Rappsilber J., Sawin K.E., RA Martin S.G., Paoletti A.; RT "Pom1 regulates the assembly of Cdr2-Mid1 cortical nodes for robust spatial RT control of cytokinesis."; RL J. Cell Biol. 206:61-77(2014). RN [21] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=25720772; DOI=10.1074/mcp.m114.045245; RA Kettenbach A.N., Deng L., Wu Y., Baldissard S., Adamo M.E., Gerber S.A., RA Moseley J.B.; RT "Quantitative phosphoproteomics reveals pathways for coordination of cell RT growth and division by the conserved fission yeast kinase pom1."; RL Mol. Cell. Proteomics 14:1275-1287(2015). RN [22] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=26150232; DOI=10.15252/msb.20145996; RA Hersch M., Hachet O., Dalessi S., Ullal P., Bhatia P., Bergmann S., RA Martin S.G.; RT "Pom1 gradient buffering through intermolecular auto-phosphorylation."; RL Mol. Syst. Biol. 11:818-818(2015). CC -!- FUNCTION: Polarity factor involved in localization of polarized growth CC and cytokinesis (PubMed:11230130, PubMed:11950884, PubMed:14663827, CC PubMed:17077120). Forms an intracellular gradient that serves to CC measure cell length and control mitotic entry (PubMed:19474792, CC PubMed:19474789, PubMed:21703453, PubMed:24047646). Controls the timing CC of mitotic commitment by regulating the inhibitory impact of cdr1/cdr2 CC on wee1 activity (PubMed:19474792, PubMed:22684255, PubMed:24316795). CC Directly phosphorylates the tail of cdr2 which inhibits cdr2 activation CC by ssp1 (PubMed:19474792, PubMed:24508166). Cdr2 phosphorylation by CC pom1 also modulates cdr2 association with membranes and inhibits cdr2 CC interaction with mid1, reducing its clustering ability, possibly via CC the down-regulation of cdr2 kinase activity (PubMed:24982431). Acts as CC a negative regulator of mid1 distribution, excluding mid1 from non- CC growing ends, which prevents division-septum assembly at the cell ends CC (PubMed:17140794, PubMed:17077120, PubMed:17543869). The pom1 polar CC gradient also mediates mitotic entry by regulating cdk1 CC (PubMed:19474789). Plays an essential role in proper localization and CC phosphorylation of a GAP for cdc42, rga4, which ensures bipolar CC localization of GTP-bound, active cdc42 involved in F-actin formation CC (PubMed:18328707). Phosphorylates multiple other substrates that CC function in polarized cell growth, including tea4, mod5, pal1, the Rho CC GAP rga7, and the Arf GEF syt22 (PubMed:25720772). CC {ECO:0000269|PubMed:11230130, ECO:0000269|PubMed:11950884, CC ECO:0000269|PubMed:14663827, ECO:0000269|PubMed:16988828, CC ECO:0000269|PubMed:17077120, ECO:0000269|PubMed:17140794, CC ECO:0000269|PubMed:17543869, ECO:0000269|PubMed:18328707, CC ECO:0000269|PubMed:19474789, ECO:0000269|PubMed:19474792, CC ECO:0000269|PubMed:21703453, ECO:0000269|PubMed:22684255, CC ECO:0000269|PubMed:24047646, ECO:0000269|PubMed:24316795, CC ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:24982431, CC ECO:0000269|PubMed:25720772, ECO:0000269|PubMed:9573052}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CC Evidence={ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166, CC ECO:0000269|PubMed:25720772}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.12.1; Evidence={ECO:0000269|PubMed:19474792, CC ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:25720772}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; CC Evidence={ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166, CC ECO:0000269|PubMed:25720772}; CC -!- SUBUNIT: Interacts with rga4 (PubMed:18328707). Interacts with tea4; CC this interaction triggers pom1 plasma membrane association CC (PubMed:21703453). {ECO:0000269|PubMed:18328707, CC ECO:0000269|PubMed:21703453}. CC -!- INTERACTION: CC Q09690; P87050: cdr2; NbExp=2; IntAct=EBI-4319163, EBI-4319869; CC Q09690; O60132: tea4; NbExp=5; IntAct=EBI-4319163, EBI-1099982; CC -!- SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:11230130, CC ECO:0000269|PubMed:11950884, ECO:0000269|PubMed:14663827}. Cell CC membrane {ECO:0000269|PubMed:21703453}; Peripheral membrane protein CC {ECO:0000269|PubMed:21703453}. Note=Forms an intracellular gradient CC that serves to measure cell length and control mitotic entry CC (PubMed:19474792, PubMed:19474789, PubMed:21703453, PubMed:22342545, CC PubMed:26150232). Localized to the cell division site at the time of CC cytokinesis (PubMed:14663827). Tea4 recruits pom1 to the cell cortex CC from where it then moves laterally at the plasma membrane, which it CC binds through a basic region exhibiting direct lipid interaction CC (PubMed:21703453). Pom1 autophosphorylates in this region to lower CC lipid affinity and promote membrane release (PubMed:21703453). Tea4 CC triggers pom1 plasma membrane association by promoting its CC dephosphorylation through the protein phosphatase dis2 CC (PubMed:21703453). {ECO:0000269|PubMed:14663827, CC ECO:0000269|PubMed:19474789, ECO:0000269|PubMed:19474792, CC ECO:0000269|PubMed:21703453, ECO:0000269|PubMed:22342545, CC ECO:0000269|PubMed:26150232}. CC -!- PTM: Autophosphorylates at the cell cortex to lower lipid affinity and CC promote membrane release (PubMed:21703453, PubMed:26150232). CC Dephosphorylation by dis2, regulated by tea4, triggers membrane CC association (PubMed:21703453). {ECO:0000269|PubMed:21703453, CC ECO:0000269|PubMed:26150232}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU329670; CAA90490.1; -; Genomic_DNA. DR PIR; S58147; S58147. DR RefSeq; NP_592974.1; NM_001018374.2. DR AlphaFoldDB; Q09690; -. DR SMR; Q09690; -. DR BioGRID; 278379; 202. DR DIP; DIP-59764N; -. DR ELM; Q09690; -. DR IntAct; Q09690; 3. DR STRING; 284812.Q09690; -. DR iPTMnet; Q09690; -. DR MaxQB; Q09690; -. DR PaxDb; 4896-SPAC2F7-03c-1; -. DR EnsemblFungi; SPAC2F7.03c.1; SPAC2F7.03c.1:pep; SPAC2F7.03c. DR GeneID; 2541889; -. DR KEGG; spo:SPAC2F7.03c; -. DR PomBase; SPAC2F7.03c; pom1. DR VEuPathDB; FungiDB:SPAC2F7.03c; -. DR eggNOG; KOG0667; Eukaryota. DR HOGENOM; CLU_009940_0_0_1; -. DR InParanoid; Q09690; -. DR OMA; MQQFINW; -. DR PhylomeDB; Q09690; -. DR Reactome; R-SPO-6804756; Regulation of TP53 Activity through Phosphorylation. DR PRO; PR:Q09690; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase. DR GO; GO:0032153; C:cell division site; IDA:PomBase. DR GO; GO:0051286; C:cell tip; IDA:PomBase. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0106186; C:cytoplasmic side of plasma membrane, cell tip; EXP:PomBase. DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central. DR GO; GO:0097575; C:lateral cell cortex; IDA:PomBase. DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase. DR GO; GO:0005886; C:plasma membrane; EXP:PomBase. DR GO; GO:0030427; C:site of polarized growth; IDA:PomBase. DR GO; GO:0005524; F:ATP binding; ISM:PomBase. DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:PomBase. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA. DR GO; GO:0051519; P:activation of bipolar cell growth; IMP:PomBase. DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:PomBase. DR GO; GO:0061245; P:establishment or maintenance of bipolar cell polarity; IGI:PomBase. DR GO; GO:0031569; P:mitotic G2 cell size control checkpoint signaling; IMP:PomBase. DR GO; GO:1903138; P:negative regulation of cell wall integrity MAPK cascade; IMP:PomBase. DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase. DR GO; GO:1903067; P:negative regulation of protein localization to cell tip; IMP:PomBase. DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:PomBase. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:1903617; P:positive regulation of mitotic cytokinesis, division site positioning; IMP:PomBase. DR GO; GO:0008104; P:protein localization; IMP:PomBase. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:PomBase. DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IMP:PomBase. DR CDD; cd14210; PKc_DYRK; 1. DR Gene3D; 3.30.10.30; DYRK; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR042521; DYRK. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1. DR PANTHER; PTHR24058:SF132; DYRK-FAMILY KINASE POM1; 1. DR Pfam; PF00069; Pkinase; 1. 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 1: Evidence at protein level; KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1..1087 FT /note="DYRK-family kinase pom1" FT /id="PRO_0000086579" FT DOMAIN 699..995 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 57..81 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 120..182 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 238..308 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 336..578 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 992..1011 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1017..1056 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 136..182 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..261 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 278..308 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 336..379 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 396..410 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 411..444 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 468..525 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 551..578 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1041..1056 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 825 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 705..713 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 728 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 513 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" SQ SEQUENCE 1087 AA; 121146 MW; 3277E7CA840F8BE2 CRC64; MGYLQSQKAV SLGDENTDAL FKLHTSNRKS ANMFGIKSEL LNPSELSAVG SYSNDICPNR QSSSSTAADT SPSTNASNTN ISFPEQEHKD ELFMNVEPKG VGSSMDNHAI TIHHSTGNGL LRSSFDHDYR QKNSPRNSIH RLSNISIGNN PIDFESSQQN NPSSLNTSSH HRTSSISNSK SFGTSLSYYN RSSKPSDWNQ QNNGGHLSGV ISITQDVSSV PLQSSVFSSG NHAYHASMAP KRSGSWRHTN FHSTSHPRAA SIGNKSGIPP VPTIPPNIGH STDHQHPKAN ISGSLTKSSS ESKNLSTIQS PLKTSNSFFK ELSPHSQITL SNVKNNHSHV GSQTKSHSFA TPSVFDNNKP VSSDNHNNTT TSSQVHPDSR NPDPKAAPKA VSQKTNVDGH RNHEAKHGNT VQNESKSQKS SNKEGRSSRG GFFSRLSFSR SSSRMKKGSK AKHEDAPDVP AIPHAYIADS STKSSYRNGK KTPTRTKSRM QQFINWFKPS KERSSNGNSD SASPPPVPRL SITRSQVSRE PEKPEEIPSV PPLPSNFKDK GHVPQQRSVS YTPKRSSDTS ESLQPSLSFA SSNVLSEPFD RKVADLAMKA INSKRINKLL DDAKVMQSLL DRACIITPVR NTEVQLINTA PLTEYEQDEI NNYDNIYFTG LRNVDKRRSA DENTSSNFGF DDERGDYKVV LGDHIAYRYE VVDFLGKGSF GQVLRCIDYE TGKLVALKII RNKKRFHMQA LVETKILQKI REWDPLDEYC MVQYTDHFYF RDHLCVATEL LGKNLYELIK SNGFKGLPIV VIKSITRQLI QCLTLLNEKH VIHCDLKPEN ILLCHPFKSQ VKVIDFGSSC FEGECVYTYI QSRFYRSPEV ILGMGYGTPI DVWSLGCIIA EMYTGFPLFP GENEQEQLAC IMEIFGPPDH SLIDKCSRKK VFFDSSGKPR PFVSSKGVSR RPFSKSLHQV LQCKDVSFLS FISDCLKWDP DERMTPQQAA QHDFLTGKQD VRRPNTAPAR QKFARPPNIE TAPIPRPLPN LPMEYNDHTL PSPKEPSNQA SNLVRSSDKF PNLLTNLDYS IISDNGFLRK PVEKSRP //