ID   MOK11_SCHPO             Reviewed;        2397 AA.
AC   Q09854; Q9P6K2;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Cell wall alpha-1,3-glucan synthase mok11;
DE            EC=2.4.1.183;
GN   Name=mok11; ORFNames=SPAC1527.01, SPAC23D3.15;
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] OF 1-1204.
RC   STRAIN=972 / ATCC 24843;
RA   Katayama S., Dai H., Arellano M., Perez P., Toda T.;
RT   "Fission yeast alpha-glucan synthase Mok1 localizes closely with actin and
RT   play a role essential for cell morphogenesis and protein kinase C
RT   function.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC         alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-
CC         COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         EC=2.4.1.183;
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AB018380; BAA76557.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB90796.1; -; Genomic_DNA.
DR   PIR; T38290; S62506.
DR   RefSeq; NP_001018282.1; NM_001019981.2.
DR   AlphaFoldDB; Q09854; -.
DR   BioGRID; 280486; 24.
DR   STRING; 4896.SPAC1527.01.1; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   PaxDb; Q09854; -.
DR   PRIDE; Q09854; -.
DR   EnsemblFungi; SPAC1527.01.1; SPAC1527.01.1:pep; SPAC1527.01.
DR   GeneID; 3361410; -.
DR   KEGG; spo:SPAC1527.01; -.
DR   PomBase; SPAC1527.01; mok11.
DR   VEuPathDB; FungiDB:SPAC1527.01; -.
DR   eggNOG; ENOG502QSGC; Eukaryota.
DR   HOGENOM; CLU_000488_0_0_1; -.
DR   InParanoid; Q09854; -.
DR   OMA; LWGTSNI; -.
DR   PhylomeDB; Q09854; -.
DR   PRO; PR:Q09854; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; NAS:PomBase.
DR   GO; GO:0047657; F:alpha-1,3-glucan synthase activity; ISM:PomBase.
DR   GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0070600; P:fungal-type cell wall (1->3)-alpha-glucan biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..2397
FT                   /note="Cell wall alpha-1,3-glucan synthase mok11"
FT                   /id="PRO_0000080329"
FT   REGION          1683..1705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2397 AA;  272024 MW;  AAB4266A2FBC3C74 CRC64;
     MAYPLVVSFF LYIVILDKHA WCAPFNNLLT DWNLNTNVSA LDPSDYWGEW ENHEFFPSPE
     HWRFPIYTIA IDKWVDGDPT NNDFSGTRFE YDIYETEFRN GGDIIGVRQS LDYLQGMGVK
     AVYFAGTPFV NMPWGADQYS PLDFTLLDPH LGTINDWRGT IEEMHSKGMY VIVDLTVATL
     ADLIGFEGFT NTTTPFTFIE HNALWKGEDR YADWNFTNSW DPDCELPRFW GESGEPVVVE
     WTGCYNSDFD QYGDTEAFGS HPDWQRQLSK FASVQDRLRE WKPSVASKLK RLSCLVISML
     DVDGFRIDKA TQMTVDFLVD WAKSVRLCAN RFNKSNFFIP GEVTGPSSFG AIYYNRGRQP
     NQRPANLIDA LNATSSDNVY FLREEGENAL DASAFHYSVY RIILRFLRMD GLMEIPYDLP
     VDLAEAWHQI VINEDSFNPK TEKYDPRHLY GVSNYDVFRW ASVADGSRRL ILGTMMTFFL
     FPGAPLIYYG DEQGLYVLDN SANNYLYGRQ SMAAAPAWYI HGCYSGSSST YPAIDLSPAK
     IGCLDIWNSL DHFDPSRIER QLFIEFQDIR SRYSALTHGW KSELLGNWTN IEYLPNSGIN
     PSNVGTFSMV RGAINSLQNI SSEYNFPGVK TSSSDVWILF TNSNVSVNLK SNCFSKEAIV
     SPFISGTKIK NLVYPYDEYQ LEASSHFSQI SNTEPMGCLP ELGLDGYGYK LFVPINEYIP
     RRPFITKFSP SHDSRLVIPL EKLRIIVEFS EEMDCKSISK SLLITSKTLN GDSPVLDESS
     VTCQKINDKD RVRFSGQSSS LFRWSATFSN IADGIHRISF NNASTADGKD FTHSVDHFLL
     RVGSLNNPIV FSSANYSYDL LQKENNSVYI KHAAIGADMF RYSLDFGSTW TEWQTYDGNN
     TYCNLSGWSQ SSRYGWKGHH IMVQYWSELT GSSNYMQESD LEYPYKRWFP HVFMDSDYTQ
     WTHDSDIRNR MLPLENGSFL GYHIADVYPS ALQFNVWGLN KDGKADKSFI YGSLQNNSFL
     SRVSPSSLEE NVFYIQHPPP KSYLSWSVTF DPQRRRYYIN PSGCVFVSLG IYLSSLIVPL
     LTGVLAVYIF KKKFYHVKFN AFGTSKQNLH FRQHDVLGMK NLFNFSCSNK IKGEEVLNDG
     DKGKRRTVLL ATLEYDIPSL NICIKIGGLG VMAQLMARHL EHEDIIWVIP CVGDVSYSNV
     EEDDPIEVVI IDQTYFINVY KYVIGNIIYI LLDAPIFRRQ TSGKPYPSRA DDLSSAIFYS
     AWNQCIASVI SRNNIDLYHM NDYHGSLAPL YLLPKIIPVA LSLHNAEFQG LWPLRNSSEK
     EEVCSVFNIS KSVCSKYVQF GNVFNLLHAG ASYIRIHQKG YGVVGVSSKY GKRSWARYPI
     FWGLRKIGKL PNPDPADNGT NFKDLDANSM NEFENIKAKH KRSAQEWANL NIDPEADLLI
     FVGRWTLQKG IDLIADITPT LLENFNSQIV VVGPVIDLYG KFAAEKFTAL MKKYPGRIYS
     RPLFTQLPSY IFSGADFALI PSRDEPFGLV AVEFGRKGTL GIGAKVGGLG QMPGWWYTIE
     SNTTAHLLCQ FEEACRQALT SSKSVRTKLR AISTIQRFPV SEWVSKLDTH VRNCIKFSHK
     QNLEEDFIHE PVIDVDEFAI SSSKDIDADE DLEIIGSSDN KAIDSNGEGF LIEKDNIGTG
     SYSNQQSFDF KSSESDSFPQ KSPSVESFSI IDNDNPFHEG QNSSTGYKDI VQGLLAENGV
     SEAGVDVMTS IVSSTIPIVS NHQTEGSQMF NEISSVSSIH VYHDESQPPV EMPAESDTPL
     QNKLYHPGMW SSSDIRIPNN SSQLSIDSVR SGMRPFSLSK VPHQFDDEEG KALQIFREKL
     KDLNCKNSMN EMCIENFLMK CTRKYFDEVR KLRLGTLKPE NLQFVKDPSS LALETNLLPA
     SDTIEEKNDV GNKQVNSHIL DPGFLKEEEC VYEFEQLHGL RKALQVEIYG WPLYTILLAI
     GQVLAATSFQ LNLFSDTPDQ PEYQSYIVCS VYISASLFWY ILHSLVPNIY ALSTPFIIYA
     TAFALAGLTT FSSLGDSRLW ISRVATWIYS IASGSQALFF SLNFGNEGRY DILYWIVRAC
     FIQGSQQVWS AALWYWGSYS TDKPNRMGVS GKLNPQPWMA AITWPIALVL LAIAFVVYRG
     LPNFYRQCPS KIPAFYRSLF RRRLIMWFFI SVFLQNYWMS SVYGRSWAFM WSAHNVHKWA
     MFLLVILFYV AIWIALVALL ASLSRYHSWI LPILGLGFGA PRWLQTLWGT SNIGIYVPFL
     GKGAPYLSRM LWLYLGLLDT VQTVGIGIIL LQTLTREHIT VVLITGQIVG AIASMVGKAS
     SPSKFGPGDV FIDFTHWSVK DGPQILASIP FWVCLICQLS VIIGYFLFFR RENLSRP