CDC14_EMENI
ID CDC14_EMENI Reviewed; 595 AA.
AC Q5B323; C8V824;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Tyrosine-protein phosphatase cdcA;
DE EC=3.1.3.48;
GN Name=cdcA; ORFNames=AN5057;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP IDENTIFICATION.
RX PubMed=19181872; DOI=10.1128/ec.00346-08;
RA Son S., Osmani S.A.;
RT "Analysis of all protein phosphatase genes in Aspergillus nidulans
RT identifies a new mitotic regulator, fcp1.";
RL Eukaryot. Cell 8:573-585(2009).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=20679430; DOI=10.1083/jcb.201002105;
RA Nayak T., Edgerton-Morgan H., Horio T., Xiong Y., De Souza C.P.,
RA Osmani S.A., Oakley B.R.;
RT "Gamma-tubulin regulates the anaphase-promoting complex/cyclosome during
RT interphase.";
RL J. Cell Biol. 190:317-330(2010).
RN [5]
RP FUNCTION.
RX PubMed=23800192; DOI=10.1186/1754-6834-6-91;
RA Brown N.A., de Gouvea P.F., Krohn N.G., Savoldi M., Goldman G.H.;
RT "Functional characterisation of the non-essential protein kinases and
RT phosphatases regulating Aspergillus nidulans hydrolytic enzyme
RT production.";
RL Biotechnol. Biofuels 6:91-91(2013).
CC -!- FUNCTION: Protein phosphatase which antagonizes mitotic cyclin-
CC dependent kinase nimX, the inactivation of which is essential for exit
CC from mitosis. To access its substrates, is released from nucleolar
CC sequestration during mitosis. Plays an essential in coordinating the
CC nuclear division cycle with cytokinesis through the cytokinesis
CC checkpoint. Involved in chromosome segregation, where it is required
CC for meiosis I spindle dissambly as well as for establishing two
CC consecutive chromosome segregation phases (By similarity). Required for
CC the transcription of the two major endoglucanase genes eglA and eglB
CC and growth on synthetic cellulose as the sole carbon source.
CC {ECO:0000250, ECO:0000269|PubMed:23800192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20679430}. Cytoplasm
CC {ECO:0000269|PubMed:20679430}. Cell septum
CC {ECO:0000269|PubMed:20679430}. Note=Does not localize to the nucleolus
CC as its homologs do in S.cerevisiae and S.pombe. Accumulates within
CC nuclei as they pass through interphase, displays a complex localization
CC in mitosis, and localizes to the forming septum after mitosis is
CC completed.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
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DR EMBL; BN001303; CBF76183.1; -; Genomic_DNA.
DR EMBL; AACD01000085; EAA60051.1; -; Genomic_DNA.
DR RefSeq; XP_662661.1; XM_657569.1.
DR AlphaFoldDB; Q5B323; -.
DR SMR; Q5B323; -.
DR STRING; 162425.CADANIAP00005331; -.
DR EnsemblFungi; CBF76183; CBF76183; ANIA_05057.
DR EnsemblFungi; EAA60051; EAA60051; AN5057.2.
DR GeneID; 2872855; -.
DR KEGG; ani:AN5057.2; -.
DR eggNOG; KOG1720; Eukaryota.
DR HOGENOM; CLU_017787_1_1_1; -.
DR InParanoid; Q5B323; -.
DR OMA; DMGDFNW; -.
DR OrthoDB; 1357618at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:EnsemblFungi.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IEA:EnsemblFungi.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0140602; C:nucleolar ring; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR GO; GO:0030869; C:RENT complex; IEA:EnsemblFungi.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:EnsemblFungi.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEA:EnsemblFungi.
DR GO; GO:0035853; P:chromosome passenger complex localization to spindle midzone; IEA:EnsemblFungi.
DR GO; GO:0051229; P:meiotic spindle disassembly; IEA:EnsemblFungi.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IEA:EnsemblFungi.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:EnsemblFungi.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; IEA:EnsemblFungi.
DR GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IEA:EnsemblFungi.
DR GO; GO:0031031; P:positive regulation of septation initiation signaling; IEA:EnsemblFungi.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0034501; P:protein localization to kinetochore; IEA:EnsemblFungi.
DR GO; GO:1902440; P:protein localization to mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
DR GO; GO:1904789; P:regulation of mitotic actomyosin contractile ring maintenance; IEA:EnsemblFungi.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR026070; CDC14.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF27; PTHR23339:SF27; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; Hydrolase; Meiosis; Mitosis; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..595
FT /note="Tyrosine-protein phosphatase cdcA"
FT /id="PRO_0000425254"
FT DOMAIN 233..381
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 32..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 322
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 595 AA; 66129 MW; 4C2999314618E2B7 CRC64;
MAGSTAGYGQ IIEYIQDKLY LASYDHTPDA KTPFPYPAEQ PKSPSKRRAQ ASPSKKRSPV
YFTVDDTLLY NSFHADFGPL HIGHLYRFAV HFHDLLAANN DRAIVFYSRT DARSRANAAC
LVACYMVLIQ SWPPHLALAP IAQADPPYMP FRDAGYSQAD FILNIQDVVY GVWKAKEQGV
CGLRDFSLEE YEKFERVDMG DFNWISPHFL AFASPQHQPV APIPRDSPEY AALPSTVSEV
RSSRLPLPFK NVLEHFATRG VGLVVRLNSE LYSPSYFTAL GISHIDMIFE DGTCPPLPLV
KKFIRMAHEM INVKHKAIAV HCKAGLGRTG CLIGAYLIYR YGFTANEVIA FMRFMRPGMV
VGPQQHWLHL NQGSFREWWF EDCMKEKLAQ MQPNPVTPGR SPAKHRAAAV TTPPQNGHSK
RSALGEIDNN EATPIYDDNL PAPTPGQPRK SHRKDSRHHP YSRTASGSLV VDKDTRKTRR
STDSSESEEE TQLRMLAKQR SSKSPAASPG QRSISYSATV TASYTLNDDI HEDRENWGGA
AQPPKTPVTS KTSGAVSVSK VRSSSRRVTG ESKGVRKPSG RIGSTGSPVR VKAQA
