CDA1_SCHPO
ID CDA1_SCHPO Reviewed; 320 AA.
AC O13842;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Putative polysaccharide deacetylase {ECO:0000305};
DE EC=3.-.-.- {ECO:0000305};
DE AltName: Full=Chitin deacetylase 1 {ECO:0000303|PubMed:15862318};
GN Name=cda1 {ECO:0000303|PubMed:15862318}; ORFNames=SPAC19G12.03;
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 FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15862318; DOI=10.1016/j.febslet.2005.04.008;
RA Matsuo Y., Tanaka K., Matsuda H., Kawamukai M.;
RT "cda1+, encoding chitin deacetylase is required for proper spore formation
RT in Schizosaccharomyces pombe.";
RL FEBS Lett. 579:2737-2743(2005).
CC -!- FUNCTION: May deacetylate chitin (Probable). Required for spore
CC formation (PubMed:15862318). {ECO:0000269|PubMed:15862318,
CC ECO:0000305|PubMed:15862318}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15862318}.
CC -!- INTERACTION:
CC O13842; O13842: cda1; NbExp=3; IntAct=EBI-7614717, EBI-7614717;
CC -!- SUBCELLULAR LOCATION: Prospore {ECO:0000305|PubMed:15862318}.
CC -!- DEVELOPMENTAL STAGE: Induced during sporulation.
CC {ECO:0000269|PubMed:15862318}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
CC -!- CAUTION: Has low sequence similarity to characterized chitin
CC deacetylases with an apparent lack of conserved active sites and metal
CC binding sites, making its function difficult to predict. {ECO:0000305}.
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DR EMBL; CU329670; CAB10114.1; -; Genomic_DNA.
DR PIR; T37990; T37990.
DR RefSeq; NP_594418.1; NM_001019847.2.
DR AlphaFoldDB; O13842; -.
DR SMR; O13842; -.
DR BioGRID; 278697; 9.
DR MINT; O13842; -.
DR STRING; 4896.SPAC19G12.03.1; -.
DR MaxQB; O13842; -.
DR PaxDb; O13842; -.
DR EnsemblFungi; SPAC19G12.03.1; SPAC19G12.03.1:pep; SPAC19G12.03.
DR PomBase; SPAC19G12.03; cda1.
DR VEuPathDB; FungiDB:SPAC19G12.03; -.
DR eggNOG; ENOG502QQRF; Eukaryota.
DR HOGENOM; CLU_029940_0_0_1; -.
DR InParanoid; O13842; -.
DR OMA; CGFWRIL; -.
DR PhylomeDB; O13842; -.
DR BRENDA; 3.5.1.41; 5613.
DR PRO; PR:O13842; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0042764; C:ascospore-type prospore; IEA:UniProtKB-SubCell.
DR GO; GO:0005631; C:chitosan layer of spore wall; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:PomBase.
DR GO; GO:0034232; P:ascospore wall chitin catabolic process; IMP:PomBase.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Chitin-binding; Hydrolase; Metal-binding;
KW Reference proteome; Sporulation.
FT CHAIN 1..320
FT /note="Putative polysaccharide deacetylase"
FT /id="PRO_0000172745"
FT DOMAIN 69..303
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
SQ SEQUENCE 320 AA; 36207 MW; 9DAD54FEAA8B1A68 CRC64;
MYETRDLTGN AGKPVDTNPW PNNSKIAVSF VVNYEEGGER SLLYEDEGFE TFLTEAGLMP
FPNRPVRERS IESCFEYGSR CGFWRILNLF KKHKVPFTCW AIGQAVEKNP VVVGAMEEAG
CEVGSHSHRW INYEGVPPET EYEHIKKSVQ AIQKASPSNS APRSWYTGRA SLNTRKLVCQ
VYKDLGLPQP FDSDEYNDDY PYWVADPLAS KPGAEDDKGL LIVPYTLEVN DMKYAVAPGF
CNSDDFYTYA RDAFDVLYEE GLEGAPKMMT IGLHCRLTGR PGRFRGLQKL MEHITSKEGV
WVATREQIAQ AWSAKHPYKA
