ENG1_SCHPO
ID ENG1_SCHPO Reviewed; 1016 AA.
AC Q9UT45; Q9UTZ1;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Primary septum endo-1,3(4)-beta-glucanase {ECO:0000303|PubMed:19542306};
DE AltName: Full=Endo-1,3(4)-beta-glucanase 1;
DE Short=Endo-1,3-beta-glucanase 1;
DE Short=Endo-1,4-beta-glucanase 1;
DE EC=3.2.1.6 {ECO:0000250|UniProtKB:Q09850};
DE AltName: Full=Laminarinase-1;
DE Flags: Precursor;
GN Name=eng1 {ECO:0000303|PubMed:12665550, ECO:0000312|PomBase:SPAC821.09};
GN ORFNames=SPAC821.09 {ECO:0000312|PomBase:SPAC821.09};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-168, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12665550; DOI=10.1242/jcs.00377;
RA Martin-Cuadrado A.B., Duenas E., Sipiczki M., de Aldana C.R.V., del Rey F.;
RT "The endo-beta-1,3-glucanase eng1p is required for dissolution of the
RT primary septum during cell separation in Schizosaccharomyces pombe.";
RL J. Cell Sci. 116:1689-1698(2003).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19542306; DOI=10.1128/ec.00148-09;
RA Encinar del Dedo J., Duenas E., Arnaiz Y., del Rey F.,
RA Vazquez de Aldana C.R.;
RT "{beta}-glucanase Eng2 is required for ascus wall endolysis after
RT sporulation in the fission yeast Schizosaccharomyces pombe.";
RL Eukaryot. Cell 8:1278-1286(2009).
CC -!- FUNCTION: Has a role in cell separation where it is required for the
CC degradation of the primary septum after completion of cytokinesis.
CC {ECO:0000269|PubMed:12665550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans
CC when the glucose residue whose reducing group is involved in the
CC linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6;
CC Evidence={ECO:0000250|UniProtKB:Q09850};
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:12665550}. Note=Localized in a ring-like structure
CC around the septum.
CC -!- DISRUPTION PHENOTYPE: Decreases basal endo-1,3-beta-glucanase activity.
CC {ECO:0000269|PubMed:19542306}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB57443.1; -; Genomic_DNA.
DR EMBL; AB027918; BAA87222.1; ALT_SEQ; Genomic_DNA.
DR PIR; T41720; T41720.
DR RefSeq; NP_593162.1; NM_001018560.2.
DR AlphaFoldDB; Q9UT45; -.
DR SMR; Q9UT45; -.
DR BioGRID; 279801; 17.
DR STRING; 4896.SPAC821.09.1; -.
DR CAZy; CBM52; Carbohydrate-Binding Module Family 52.
DR CAZy; GH81; Glycoside Hydrolase Family 81.
DR CLAE; LAM81A_SCHPO; -.
DR MaxQB; Q9UT45; -.
DR PaxDb; Q9UT45; -.
DR EnsemblFungi; SPAC821.09.1; SPAC821.09.1:pep; SPAC821.09.
DR GeneID; 2543379; -.
DR KEGG; spo:SPAC821.09; -.
DR PomBase; SPAC821.09; eng1.
DR VEuPathDB; FungiDB:SPAC821.09; -.
DR eggNOG; KOG2254; Eukaryota.
DR HOGENOM; CLU_005482_2_1_1; -.
DR InParanoid; Q9UT45; -.
DR OMA; ITFMNKI; -.
DR PhylomeDB; Q9UT45; -.
DR PRO; PR:Q9UT45; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0009986; C:cell surface; IDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0000936; C:primary cell septum; IDA:PomBase.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:PomBase.
DR GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0044347; P:cell wall polysaccharide catabolic process; IC:PomBase.
DR GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0030994; P:primary cell septum disassembly; IMP:PomBase.
DR InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR018909; Eng1_septum.
DR InterPro; IPR040720; GH81_C.
DR InterPro; IPR040451; GH81_N.
DR PANTHER; PTHR31983; PTHR31983; 1.
DR Pfam; PF10645; Carb_bind; 3.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF03639; Glyco_hydro_81; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1016
FT /note="Primary septum endo-1,3(4)-beta-glucanase"
FT /id="PRO_0000012132"
FT REGION 844..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1016 AA; 109743 MW; 9240CA34D35786FC CRC64;
MSSYLRSFIF GLLTISLAQC SPILKDTKDT KFSTGSNISL KKRDTNVFDS VVDTINPASY
FGTVSHPVTP AGVSTDSLSS PIETNKFFDN NLLGSRTNFM YADPFRYWWQ SSDTMGGICI
AHTDDNQRVM DTDDTIPSYY YEPIGICSLG FGASGITSNT DPIVDEIDQM SARFTFSWDS
SSMQLTLTEG MAVTTAVYTN AIPQIFSSTL YINDFVEVPG TSAVQKYRVT MSDNHVWLIY
IYGDSLTLTE STSQMLVGSN TFNGYIQIAK IPLGDGTAEA LYDTYAGVYI TGISISGYVE
DAVGYYSFDF TTAGDTSVEP LFFLLPHQVD TAVSGTKVTS IVLASLVSGD MNAAAGNSIT
FAEAIPQDIG FLPWSPTGGQ IGYSEEALEI IAEVAGTELG EDFSANSNLN SMYYSGKVLA
KYAMLCVTIN DILGDETSSE QCIQKLEAAF ARFVDNQQIY PLTYDNTWKG VVSVAGLSGD
SLADFGNSYY NDHHFHYGYF VFTAAVIGHI DPDWINTGNN KEWVNFLVRD VANPSSNDPY
FPKHRMIDIY HGHGWASGLF ESNDGKDEES TSEDYNFFFG MKLWGQVIGD SDMEDRANII
LGIERNALNK YMLYADGNVQ PTSMQPNYVA GITFMNKITH TTYFGTNIEY IQGIHMLPIT
PISAFIRGPS FVLAEWNALL ASVIDYVDSG WRSLLYANLA IAEPEESYEY FSSSDFNTDY
LDDGASRAWY LAYAAGLWAN DAVYYPVSSS STTTTSTSTG SVTTTSTTAT ASCTLPISYT
STPTTTSISG TCNGATFDAS LYVCDGTVLC PIVNGVSYQN CNGACYNPSQ YGCDNGALGP
VQSSSTTSSI TPTPTTTSSI TPTPTTTSTT TTAQSTGMQL CGSNYYDASS YYCDNDQLCP
IIDGVDYLSC NGACYNPSQY VCSDGSLSPN TVTTTKATTT FTPTPTTTTT PTPTTTSATS
TNVIAQCGSA WYDSQSYICY GNILCPIING SPLLACGNAC YDSSIYGCSN GALVAA
