TASP1_SCHPO
ID TASP1_SCHPO Reviewed; 345 AA.
AC Q9P6N7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Putative threonine aspartase;
DE Short=Taspase-1;
DE EC=3.4.25.-;
DE Contains:
DE RecName: Full=Putative threonine aspartase alpha chain;
DE Contains:
DE RecName: Full=Putative threonine aspartase beta chain;
DE Flags: Precursor;
GN ORFNames=SPAC823.09c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB90154.3; -; Genomic_DNA.
DR RefSeq; NP_593836.3; NM_001019265.3.
DR AlphaFoldDB; Q9P6N7; -.
DR SMR; Q9P6N7; -.
DR BioGRID; 279959; 13.
DR STRING; 4896.SPAC823.09c.1; -.
DR MEROPS; T02.A06; -.
DR iPTMnet; Q9P6N7; -.
DR MaxQB; Q9P6N7; -.
DR PaxDb; Q9P6N7; -.
DR EnsemblFungi; SPAC823.09c.1; SPAC823.09c.1:pep; SPAC823.09c.
DR GeneID; 2543542; -.
DR KEGG; spo:SPAC823.09c; -.
DR PomBase; SPAC823.09c; -.
DR VEuPathDB; FungiDB:SPAC823.09c; -.
DR eggNOG; KOG1592; Eukaryota.
DR HOGENOM; CLU_021603_5_0_1; -.
DR InParanoid; Q9P6N7; -.
DR OMA; RLWCAFT; -.
DR PRO; PR:Q9P6N7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; ISS:PomBase.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; ISO:PomBase.
DR CDD; cd04514; Taspase1_like; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR InterPro; IPR037464; Taspase1.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Threonine protease; Zymogen.
FT CHAIN 1..175
FT /note="Putative threonine aspartase alpha chain"
FT /id="PRO_0000420552"
FT CHAIN 176..345
FT /note="Putative threonine aspartase beta chain"
FT /id="PRO_0000420553"
FT REGION 322..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 204..207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 175..176
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 36833 MW; 325A73EAB007825F CRC64;
MSNGLVILHA GAGLYSGQRE IQAKKTCSDA CKAAIQALKV GQSALSAAIQ AAKIMEDSPV
TNAGVGSNLN IDGKVECEAG VMDSESGLTA SVACCNCCRH PSEACLYILN KRKVMSQHGL
VPPAMLVGNG IEKLLLHSNI KLVPESHLIT ERSMKTQIKW KEILYQNPIN LSSQDTIGVI
CVDKNGRIAV VSSSGGLLLK PAGRIGSSPI PGHGFWIESF DNKSHSSTCA VATSGTGEHI
SNTCFACRSS QLLVSEDNVV SSLNKLINDF HEHPSATLYS DLQVGIIFAK VETSNSHNKR
IIFGLAHSSP DMVFGFMKGD HSKPTTEISR KGSKRSSVQL YAERL
