ID   CTK2_SCHPO              Reviewed;         335 AA.
AC   O59748;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=CTD kinase subunit beta;
DE            Short=CTDK-I subunit beta;
DE   AltName: Full=CTD kinase subunit 2;
DE   AltName: Full=Latrunculin sensitive cyclin knockout protein 1;
GN   Name=lsc1; Synonyms=ctk2; ORFNames=SPBC530.13;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   FUNCTION, INTERACTION WITH CTK1, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17502918; DOI=10.1371/journal.pone.0000433;
RA   Karagiannis J., Balasubramanian M.K.;
RT   "A cyclin-dependent kinase that promotes cytokinesis through modulating
RT   phosphorylation of the carboxy terminal domain of the RNA Pol II Rpb1p sub-
RT   unit.";
RL   PLoS ONE 2:E433-E433(2007).
CC   -!- FUNCTION: Cyclin subunit of the CTDK-I complex, which
CC       hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of
CC       the largest RNA polymerase II subunit. As part of the CTDK-I complex,
CC       involved in RNA polymerase II transcriptional elongation and pre-mRNA
CC       3'-end processing. Together with ctk3, required for ctk1/lsk1 CTD
CC       kinase activation (By similarity). Together with ctk1/lsk1, required
CC       for the regulation of cytokinesis by phosphorylating 'Ser-2' residues
CC       found in the heptad repeats of the CTD. {ECO:0000250,
CC       ECO:0000269|PubMed:17502918}.
CC   -!- SUBUNIT: CTDK-I consists of three subunits, ctk1/lsk1, ctk2/lsc1 and
CC       ctk3 (also called alpha, beta and gamma) (By similarity). Interacts
CC       with ctk1/lsk1. This interaction is dependent on ctk1/lsk1 kinase
CC       activity. {ECO:0000250, ECO:0000269|PubMed:17502918}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear localization is
CC       dependent on ctk1/lsk1.
CC   -!- DISRUPTION PHENOTYPE: Cells are hyper-sensitive to actin depolymerizing
CC       drug, latrunculin A (Lat A). Deletion mutants are unable to complete
CC       septum formation upon LatA treatment, but are able to suppress the
CC       lethal, multiseptate phenotype conferred by the constitutive
CC       hyperactivation of the septation initiation network (SIN).
CC       {ECO:0000269|PubMed:17502918}.
CC   -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA19179.2; -; Genomic_DNA.
DR   PIR; T40529; T40529.
DR   RefSeq; NP_595326.2; NM_001021233.2.
DR   AlphaFoldDB; O59748; -.
DR   SMR; O59748; -.
DR   BioGRID; 277396; 83.
DR   STRING; 4896.SPBC530.13.1; -.
DR   MaxQB; O59748; -.
DR   PaxDb; O59748; -.
DR   EnsemblFungi; SPBC530.13.1; SPBC530.13.1:pep; SPBC530.13.
DR   GeneID; 2540879; -.
DR   KEGG; spo:SPBC530.13; -.
DR   PomBase; SPBC530.13; lsc1.
DR   VEuPathDB; FungiDB:SPBC530.13; -.
DR   eggNOG; KOG0834; Eukaryota.
DR   HOGENOM; CLU_829385_0_0_1; -.
DR   InParanoid; O59748; -.
DR   OMA; GITWIDN; -.
DR   Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:O59748; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0070692; C:CTDK-1 complex; IPI:PomBase.
DR   GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; IPI:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IMP:PomBase.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0023052; P:signaling; NAS:PomBase.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; PTHR10026; 1.
DR   Pfam; PF00134; Cyclin_N; 2.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; SSF47954; 2.
PE   1: Evidence at protein level;
KW   Cyclin; Cytoplasm; mRNA processing; Nucleus; Reference proteome; Repeat;
KW   Transcription.
FT   CHAIN           1..335
FT                   /note="CTD kinase subunit beta"
FT                   /id="PRO_0000310348"
FT   DOMAIN          26..151
FT                   /note="Cyclin N-terminal 1"
FT   DOMAIN          158..241
FT                   /note="Cyclin N-terminal 2"
FT   REGION          269..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  38686 MW;  38EAF74FC5EFDD7E CRC64;
     MAENENHVLS IRMSHPYYSE KEISRILSTR DPKENNLRMQ AFAWISTLSK TLKFPVRTSG
     LAMLLYSRFQ LFFPVNEIPL LECATACLVV ASKIEDTAKK FRDILLAHYL QKHPGSEVDA
     HSQVCYKLIE ENKKRILGLE RMTLELICFD FRVRHPHNYM VKFAKSLKFS SSTASIAWNV
     CTDAYKTYTM LKYPAHIVAV ASISIACKLQ QLPQPIIPRS FFAPPALTEA VIADILDLYM
     HYQPHTCIGN MYTTEKLLGL CVDFQRAQKN SGRPQKPPQI DPHSSSLADE YRESNKRLQE
     SKESCARFIL DCDRKYFNTE FEKRMLEERR NKGTV