ORB6_SCHPO
ID ORB6_SCHPO Reviewed; 469 AA.
AC O13310;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Serine/threonine-protein kinase orb6;
DE EC=2.7.11.1;
GN Name=orb6; ORFNames=SPAC821.12;
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 [GENOMIC DNA].
RX PubMed=9636183; DOI=10.1073/pnas.95.13.7526;
RA Verde F., Wiley D.J., Nurse P.;
RT "Fission yeast orb6, a ser/thr protein kinase related to mammalian rho
RT kinase and myotonic dystrophy kinase, is required for maintenance of cell
RT polarity and coordinates cell morphogenesis with the cell cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7526-7531(1998).
RN [2]
RP INTERACTION WITH MOB2.
RX PubMed=12456722; DOI=10.1242/jcs.00206;
RA Hou M.-C., Wiley D.J., Verde F., McCollum D.;
RT "Mob2p interacts with the protein kinase Orb6p to promote coordination of
RT cell polarity with cell cycle progression.";
RL J. Cell Sci. 116:125-135(2003).
RN [3]
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).
CC -!- FUNCTION: Interacts with pak1/shk1 and coordinates cell morphogenesis
CC with the cell cycle. It is essential for maintenance of cell polarity
CC and is involved in mitotic control.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBUNIT: Interacts with mob2. {ECO:0000269|PubMed:12456722}.
CC -!- INTERACTION:
CC O13310; O74558: mob2; NbExp=4; IntAct=EBI-1563264, EBI-1563284;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF009512; AAC32420.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB57446.1; -; Genomic_DNA.
DR PIR; T41723; T41723.
DR RefSeq; NP_593165.1; NM_001018563.2.
DR AlphaFoldDB; O13310; -.
DR SMR; O13310; -.
DR BioGRID; 279861; 18.
DR IntAct; O13310; 1.
DR STRING; 4896.SPAC821.12.1; -.
DR iPTMnet; O13310; -.
DR MaxQB; O13310; -.
DR PaxDb; O13310; -.
DR PRIDE; O13310; -.
DR EnsemblFungi; SPAC821.12.1; SPAC821.12.1:pep; SPAC821.12.
DR GeneID; 2543441; -.
DR KEGG; spo:SPAC821.12; -.
DR PomBase; SPAC821.12; orb6.
DR VEuPathDB; FungiDB:SPAC821.12; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_2_1; -.
DR InParanoid; O13310; -.
DR OMA; PERYSEN; -.
DR PhylomeDB; O13310; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:O13310; -.
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:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0035838; C:growing cell tip; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0071472; P:cellular response to salt stress; IDA:PomBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0097248; P:maintenance of protein location in cell cortex of cell tip; IMP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:2000247; P:positive regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:PomBase.
DR GO; GO:0062200; P:RAM/MOR signaling pathway; IMP:PomBase.
DR GO; GO:2000100; P:regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IMP:PomBase.
DR InterPro; IPR000961; AGC-kinase_C.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..469
FT /note="Serine/threonine-protein kinase orb6"
FT /id="PRO_0000086455"
FT DOMAIN 93..392
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 393..467
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 99..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 469 AA; 54691 MW; 1BFF2905E81FBF6C CRC64;
MDKNDYLHFE RNPSLFPKST LDKVQKTKKY IEHYYKVAVD HAVERNQRRI NLEQRLATER
GSEERKNRQL RASGEKESQF LRFRRTRLSL EDFSTIKVIG KGAFGEVRLV QKLDTGKIYA
MKSLLKTEMF KRDQLAHVKA ERDLLVESDS PWVVSLYYAF QDSLYLYLIM EFLPGGDLMT
MLINYDTFSE DVTRFYMAEC VLAIADVHRM GYIHRDIKPD NILIDRDGHI KLSDFGLSTG
FYKQDQSASY MKPRTGNTVK RGQMVDAIWL TMSSKDKMAT WKKNRRVMAY STVGTPDYIA
PEIFLQQGYG QDCDWWSLGA IMFECLIGWP PFCSENSHET YRKIINWRET LTFPNDIHLS
IEARDLMDRL MTDSEHRLGR GGAIEIMQHP FFTGIDWDHI RETAAPFIPN LKSITDTHYF
PVDELEQVPE QPVTQQPASV DPQTLEQTNL AFLGYTYKKF NYLTMKGAL
