PPK38_SCHPO
ID PPK38_SCHPO Reviewed; 650 AA.
AC Q9UU85;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein kinase domain-containing protein ppk38;
GN Name=ppk38; ORFNames=SPCP1E11.02;
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 IDENTIFICATION.
RX PubMed=15821139; DOI=10.1128/ec.4.4.799-813.2005;
RA Bimbo A., Jia Y., Poh S.L., Karuturi R.K.M., den Elzen N., Peng X.,
RA Zheng L., O'Connell M., Liu E.T., Balasubramanian M.K., Liu J.;
RT "Systematic deletion analysis of fission yeast protein kinases.";
RL Eukaryot. Cell 4:799-813(2005).
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
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DR EMBL; CU329672; CAB54861.1; -; Genomic_DNA.
DR PIR; T41681; T41681.
DR RefSeq; NP_588555.1; NM_001023542.2.
DR AlphaFoldDB; Q9UU85; -.
DR SMR; Q9UU85; -.
DR BioGRID; 275603; 33.
DR STRING; 4896.SPCP1E11.02.1; -.
DR iPTMnet; Q9UU85; -.
DR MaxQB; Q9UU85; -.
DR PaxDb; Q9UU85; -.
DR PRIDE; Q9UU85; -.
DR EnsemblFungi; SPCP1E11.02.1; SPCP1E11.02.1:pep; SPCP1E11.02.
DR GeneID; 2539030; -.
DR KEGG; spo:SPCP1E11.02; -.
DR PomBase; SPCP1E11.02; ppk38.
DR VEuPathDB; FungiDB:SPCP1E11.02; -.
DR eggNOG; KOG1989; Eukaryota.
DR HOGENOM; CLU_011638_3_1_1; -.
DR InParanoid; Q9UU85; -.
DR PhylomeDB; Q9UU85; -.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9UU85; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030479; C:actin cortical patch; ISO:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0000147; P:actin cortical patch assembly; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; ISO:PomBase.
DR GO; GO:0023052; P:signaling; IC:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..650
FT /note="Protein kinase domain-containing protein ppk38"
FT /id="PRO_0000256833"
FT DOMAIN 33..315
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 344..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 72000 MW; 07963A6D4E959E12 CRC64;
MNETNNTSLL PVSSLPSGLL PVGFSCTVEK FSVTVKRYLA EGGFSHVYLV QLVFPGKPPF
EAVLKRIFAT DAMALRAVHE EVRTMKLVSN QKRCVSYYGS EFFRTSKNQF EVLVLLEYCP
CGGLIDFLNT RLQVRLSEQE ILKIASDVTE AVAVMHYLKP PLIHRDLKIE NVLLAAPNSY
KLCDFGSACH PIPGAKTAAE AKQLEYDIEK FTTWQYRCPE MINVHKGFGI DEKSDIWALG
VLFYKLCYYT TPFEHQGLAA IMNVSYAFPT FPPYSDRLKR LISTLLQQYP WQRPNIYQTF
CEICKMRNVP IHIYDIYNGK NVSSCNPSGS EYLQHASKLE NSGIHQSKSS VFPQPASAMK
PMASPMLPNV NSMPYLSNGD HNNNGNTSSP VSRFSYGQHT SNVPSTQKLP SNFRVTQGAP
PSHTYGPPPP VQPKPKISPT TPRLSTLALA DDMFSSTAKE TVPTNEAVFT GDVKSFDSQE
SNIIESEPLS ASNASGKPRT SVNRLVDRYN HTSSLNKVAA APAPVPKPVN LKSVENPQNN
ISAPTPSSLQ SSNAPVGLGE VESKSVPPTN MATERGVVGR RASMSIAVNA RRVSKPEKEH
TNPNAEQGDV IPEKPMSIKE RMNMLMTKTD YEKPKVEGYG RYTDVQQTKK