ID   MOK12_SCHPO             Reviewed;        2352 AA.
AC   Q9UUL4; O13605;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Cell wall alpha-1,3-glucan synthase mok12;
DE            EC=2.4.1.183;
GN   Name=mok12; ORFNames=pi011, SPBC32H8.13c;
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].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10087262; DOI=10.1083/jcb.144.6.1173;
RA   Katayama S., Hirata D., Arellano M., Perez P., Toda T.;
RT   "Fission yeast alpha-glucan synthase Mok1 requires the actin cytoskeleton
RT   to localize the sites of growth and plays an essential role in cell
RT   morphogenesis downstream of protein kinase C function.";
RL   J. Cell Biol. 144:1173-1186(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA21388.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB018381; BAA76558.1; -; Genomic_DNA.
DR   EMBL; AB004534; BAA21388.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CU329671; CAC37503.1; -; Genomic_DNA.
DR   PIR; T43431; T43431.
DR   RefSeq; NP_595619.1; NM_001021514.2.
DR   AlphaFoldDB; Q9UUL4; -.
DR   SMR; Q9UUL4; -.
DR   BioGRID; 276775; 3.
DR   STRING; 4896.SPBC32H8.13c.1; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   PaxDb; Q9UUL4; -.
DR   EnsemblFungi; SPBC32H8.13c.1; SPBC32H8.13c.1:pep; SPBC32H8.13c.
DR   GeneID; 2540243; -.
DR   KEGG; spo:SPBC32H8.13c; -.
DR   PomBase; SPBC32H8.13c; mok12.
DR   VEuPathDB; FungiDB:SPBC32H8.13c; -.
DR   eggNOG; ENOG502QQX3; Eukaryota.
DR   HOGENOM; CLU_000488_0_0_1; -.
DR   OMA; NQDIFRW; -.
DR   PhylomeDB; Q9UUL4; -.
DR   PRO; PR:Q9UUL4; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005619; C:ascospore wall; IDA:PomBase.
DR   GO; GO:0071944; C:cell periphery; IDA:PomBase.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0047657; F:alpha-1,3-glucan synthase activity; IMP:PomBase.
DR   GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR   GO; GO:0070591; P:ascospore wall biogenesis; IMP: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; IPR001296; Glyco_trans_1.
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   Pfam; PF00534; Glycos_transf_1; 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..2352
FT                   /note="Cell wall alpha-1,3-glucan synthase mok12"
FT                   /id="PRO_0000080330"
FT   REGION          1786..1813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1796..1813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2352 AA;  266564 MW;  78ADF9C2F7140BBA CRC64;
     MLFFSIPTIL LIFFLFIQII TAAFLTDENE PWNLNRNWTA QKILDYSAEW NSHEYFPSPS
     NWRALPFYTI ILDKWTNGVP ENDVAEDTVF ESDPYEVTFR AGGDIVGLVT PRSLDYLESM
     GIKAVYIAGT PFQNLPWYPD GYSPLDFTLL DKHTGTLNQW HEAIMKLHER GFYVVVDFTI
     STLSELSYFV NSSMSFANTS APFSTKGYKM KYKHPEYHYT DFQLSNGSSY SCNAPTFWDV
     TGLPINNTED LNSISEVMCL SGDFDHYGDV EAFGNHPPWW RQLSNFASVQ DRLRDWDPIV
     AKKLKHLGCL AVKMLDIDGI RVDKATQITA DFLGDWSAYI RQCAREIGKE NFFIPGEVTS
     GADFGSIYVG RGRQADQRPN NREIALQTGY NESKYFLRKE SDSALDSVSF HYSVYRTLTL
     LLGLQGELFA AFDLNRHDFA AMWNQMLIQD DMINANTKKF DPRHLYGLTN QDIFRWPSIK
     DGRFKQLLGL FVVHLLMPGI PLIYYGEEQN LKLLDNQAAN YIFGRQPITS SIGWQKHGCY
     QIGTTQYTDL DFGPASEACR DDWNSLDHLD PTSPTKHYIA RMNEIRSYFP QVRDGWDLKL
     IGKWTHEGTF PGNELYGESN PTTWGLWSMI RGPLAPYQKF SDQNDYIWLI FTNENTTKTY
     DMDCMRQVDN KFPPYPALLG PYSSGSTVKN LLYPYEEIDL STSTIDSPDI GNIGCIPHLT
     IDAYGSKIFV KKEDWIRPSL YLTKFLPGHD SRIYSATEVT SFKISLGFSE EVDCKDLFKR
     IGFNSRTLNS SFAPKILEDS ISCGYLDQPA PQEYTNAPVT KWFFNATLDS VPNGMHELLL
     NEVKSTSNQT MQSKIARLIF RVGNEENPLV YPNNATFSPS LLYKASNGDL YVNHTGAGAD
     KYRFSLNYGG TYSKWKTVST PSEKLRKPTW NGTNLQKWDG DHLIVQYWSS IALSTAHVQH
     GDTLNYSRQF PNLFVQGAFN RFGYDGSMPS KMSYNLENRT WSYDLISTWP AELVLNVWGM
     NPDNNADQGW VYGDLDNDTI IDRVPPGSSR ISNFIRFLDP PPKPYLSYKM YLNDFTRQLH
     YIPKGSWTVQ IVAIVLLILL PPLFGIFSVA LYSGAFSRVT IFNGSHNRGI KVAKQKIKSI
     MSRIFPFSVH LPLDNSSELL KQLPESEKRL NVLVATLEYD VPDLGIRVKI GGLGVMAQLM
     GQHMEFQDMV WVVPIISGVE YPFDKLCTEP KIAVKIGDDE FVVNCYSYKS GNITYVFLQS
     EVFYKQSSKE PYPLKMDDLA SAIFYSVWNQ CIAEVWKRFP LDIYHVNDYH GALAPLYLLP
     EVIPVAVSLH NAEFQGLWPL RTSAELECVC SIFNIEKDIC TKYVQFGHVF NLLHSIISYV
     RKHQGGYGVV AVSDKYSKQT LSRYPIFWSL VHISGLPNPD PSDLKLLNHL TDDPVDVDFV
     LEAKRKLLKK QTQEWANLDV DPSAQLLVFV GRWSHQKGID LIADLAPKLL TEHNVQLITI
     GPVIDLHGQF AAEKLEQIAK RFPTRVLCKP VFTAVPPFLF AGTDFALIPS RDEPFGLVAV
     EFGRKGVLCI GSRTGGLGHM PGWWFQMASP NTGHLLTQFE NAITKALHSN GELRARLRVE
     ALRQRFPVCI WKQKSENLLK SCIYVHEMET LKHASPTFKA YQFVVRICHY LTSKVKSINK
     DQVFNAFSPD VSERPPLFEV ASCSNETDSV EKLTPELSVS PESDMHFKDG NSSKLEIVES
     KEIYASDSDI SNSTSEDINK DECVSKDIEV DNFALNLQSQ SYEGDSNDFG IREVPLSDAN
     QSSQADSTSI DRYGPYSSQK VNFSKYKDFV ESRPTFFQSS VTFTDADGST RKTFSKRLEN
     LTTSNTLKSL SVDHFIRKHE RKYFNGLRKQ EIDVKLKSRS DKEKSCTVSE SYKQIDCDTY
     EATRLQKLLL HSIGGWPLYT IVLAIGQILG ASSYQLTLLS GESAQSTVSM YILLSIFSFF
     SLFWWFLSRV VQARYILSLP FFFFGISFIL VAITHFFQKT TACSVIQHIA AYVYAISSST
     GSLYFAWNFG AEGGIATHHW ILRACLVHGI QQIWSAILWS WGDLLSKKDL TQNVGPGIFA
     GGLIASFICF GLSYVTFAGL PAFYRQAPSI IPAFYRSLGK RNIVIWFFIS QILINYWLAV
     PYGQAWRFFW NTSNTPLWSI IILLLIFFIV VWAVLLSVIK ILSLNNVWFP VIFGLGLICP
     RWCLEFWSSS GLGINLPWAG KASALLTKSV WLLLALWDGI QGVGVGVMLL QTLARDHVAF
     TLMLAQVISC ITIMIAKPSL PVSDRVFPNL GAWNPSEGPG PCASPCFYIA LICQFVAVGG
     LLYHYRKSQL AL