MOK13_SCHPO
ID MOK13_SCHPO Reviewed; 2358 AA.
AC Q9Y719; O94638;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Cell wall alpha-1,3-glucan synthase mok13;
DE EC=2.4.1.183;
GN Name=mok13; ORFNames=SPBC16D10.05;
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;
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; AB018382; BAA76559.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB38509.1; -; Genomic_DNA.
DR PIR; T39569; T39569.
DR PIR; T43432; T43432.
DR RefSeq; NP_596500.1; NM_001022421.2.
DR AlphaFoldDB; Q9Y719; -.
DR SMR; Q9Y719; -.
DR BioGRID; 276551; 2.
DR STRING; 4896.SPBC16D10.05.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR iPTMnet; Q9Y719; -.
DR MaxQB; Q9Y719; -.
DR PaxDb; Q9Y719; -.
DR PRIDE; Q9Y719; -.
DR EnsemblFungi; SPBC16D10.05.1; SPBC16D10.05.1:pep; SPBC16D10.05.
DR GeneID; 2540007; -.
DR KEGG; spo:SPBC16D10.05; -.
DR PomBase; SPBC16D10.05; mok13.
DR VEuPathDB; FungiDB:SPBC16D10.05; -.
DR eggNOG; ENOG502QSGC; Eukaryota.
DR HOGENOM; CLU_000488_0_0_1; -.
DR InParanoid; Q9Y719; -.
DR OMA; HSWFLPV; -.
DR PhylomeDB; Q9Y719; -.
DR PRO; PR:Q9Y719; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
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; 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..2358
FT /note="Cell wall alpha-1,3-glucan synthase mok13"
FT /id="PRO_0000080331"
FT REGION 1645..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 120
FT /note="V -> VRRVMLLCSLTNKV (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2358 AA; 269195 MW; A175577C9D8AD731 CRC64;
MRNKNILVLN LILSIPRLVF TAKYDERESL WNLNQNQSAT DPLDYWGKWE NHQYHPSPDD
WQVPFYTVIL DKWKDGDPRN NEANNTIYEY DIYETGFRNG GDIIGLKDSL DYLEIMGIKV
IYIAGTPFLN QPWGADQYSP LDYTILDHHS GTIAQWRDTI EEIHRRGFYL VLDLTISTLG
DLIGFRKYLN STTPFSLFEH EAVWKSNVIY PDWNFTNKYD PKCELPRFWG EDGAPVVIDY
VGCYDSDFDQ YGDTEAFGTH PDWERQLSKF ASVQDRLREW RPSVSEKLKH FACMIIAMLD
VDGFRIDKAT QITVDFLASW AHSVRGCAAT FNKKNFFIPG EVTGSSSYGS IYYGRGRQPD
QRPPSILTSL NSSSLKENYF LREPKANALD ASAFHYSLYR AMTRFLQMDG DLQVGHDLPV
DFTDLWNAMA VNEDFYNPNT HKVDPRHMLG ITNHDVFRWS AIEFGLERLL LGTMITYFLF
PGAPSIYYGD EQGFYVLDNT ANNYLYGRQA MPSSIAWKVH GCYALASDQY PELPVIKAYQ
GCNDDWNIMD HFDFAKPELK MFKIFNFIRE QYPALKSGWK SVKLRNWTEY VHFPNSGKTP
TEVGVWSIVR GALETLQNFD ARNNTAWNGD IWILYTNQNR TTTLDYQCSS SNSVVSPYAS
GLTLKNLIYP FEEYILQESN KYSSNLKSYY GCIPNIEFPP WGFKILIPKK YYVRYPPQIT
SFNPQHDSRI YNHNGKQKLV ISFTETMDCN EITSKLQFSS KTESGKVMKV DKETVKCSVS
NNSADSYYFG LAPARFHWSG DLINIADGIH EIKLQRVHSQ DHQSMSDSMY KLLLRFGKLD
NPMVFSTANR SSSILSQENE KLYINHKAPG ADLFRFSFDY GLHWSEWIDY LSNKTECTEF
ANNISLKTWK GHHVIVQYWS RLTASANYIQ EGGLGSLSSF PHLYMNGPYN QWGFDSGIPN
RLIYKNCSWH KTFISDVFPT KFQFNVYNFD ESGMPDQKKV YGTIGNSTVL VRLPPSELKE
SVTWIKEAPP SNFLTWEIII SDLTRTYHLI PRGSSTVSII LFSLFLVSPL ICALATMLAF
QKFFYQVRLN KGIEKKQEWK EKLLGPFSRI SQSNINQGFS HQVALNNSVK SVHPKISRKL
ILVATLEYDI PDWDIKIKIG GLGVMAELMG KHLTHHDLIW VVPRVGDVNY PDGQELAPLE
VVVLDQVYEV RVYSHNLRNI TYILLEAPVF RKQTSAEPYP ARMDDLSSAI FYSAWNQCIA
GIIRRYPIDV YHINDYHGAL APCYLLPNVI PCVLSLHNAE FQGLWPLRTQ AEKNEVCAVY
NISTKICTKY IQFGNVFNLL HAGVSYIRIH QKGYGVVGVS NKYGKRSKAR YPIFWGLKKV
GKLPNPDPLD TAQLDDPTNI TEEITIDLTA EAEKRAFKRD AQKWTNLELD DSADLLVFVG
RWSMQKGIDL IADIAPTLLQ DFNAQLITIG PIIDLYGKFA AEKLNALMKK YPKRVYCRPE
FTHLPPCIFS GADFVLIPSR DEPFGLVAVE FGRKGALGIG ARVGGLGQMP GWWYSVESNA
TSHVLQQFEE ACRKALSSSA EKRALLRAKS AKQRFPVLEW ISKLDHLMDN CIRLNVGQRQ
QGSSSHSMKF RSKNDLSSIK LSTKEGLENE ENELKDKAPP NEPNVGSLFL FNKSSMGSVG
GPGHYKATDL SQELETNDQD IEYNEFYSQL DTSTSDIFQD TSVDGFPDLQ VSSDINVRND
RLSSFVMSSE DLRSSDGHPE NSDSVLETIS SVHHRSPINQ VVRNLNESQL SLDSVISMNL
NKEFALTKTE NDFTDDNGRA LNYFSQKLEE LDPKNSVNEL CIETFILKMK KEWYDGLRNI
RFGIQRPNLL IYDEDKKFIN TEHFLGSKVN LNSVTSLGNF NGSSPNSFLF LLKNRTMRIK
CFMQMRIGDW PVYSIFLSVG QILAATSYQL VLLSGSSAQF STQLYIVGSI YTVSSVFWWY
LYRMLPSVAS LSLPFLLYCA SFLLIGISSF INENMYLRLW ISHIASWIYA VASASGSLYF
SLNFGDEAGA GVVSWIVRAC IVQGFQQIWA CCLWYWGSYI DRSMQECHSF PHEVYPLGLI
AVFSWPLALV MLLFAILLIF GLPDYYWESP GNIPAFYTAL LRRKLVLWFF VATILQNYWL
STLYGRSWKY LWGGSLLAPW KMLTIAFFLF LSMWIIMLMF LGRKSLTHSW LLPVFGVGLG
SPRWLQMMWG TSNIGVYLPW AGVAGPIVGR ILWIWLGVLD SVQGVGVGMI LLQTLTRRHI
ATTLIAGQII GTLTSMLARA TAPNRLGPGL VFLDLTSWRF EDGAKIFRSA PFWICLISQI
AVSAGYLLFF RRENLSRP
