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   27-MAR-2024, entry version 115.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 227321.Q5B323; -.
DR   EnsemblFungi; CBF76183; CBF76183; ANIA_05057.
DR   GeneID; 2872855; -.
DR   KEGG; ani:AN5057.2; -.
DR   eggNOG; KOG1720; Eukaryota.
DR   HOGENOM; CLU_017787_1_1_1; -.
DR   InParanoid; Q5B323; -.
DR   OMA; KFERVDM; -.
DR   OrthoDB; 9871at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
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; IEA:EnsemblFungi.
DR   GO; GO:0044732; C:mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0140602; C:nucleolar peripheral inclusion body; 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:0005816; C:spindle pole body; 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:0071470; P:cellular response to osmotic stress; IEA:EnsemblFungi.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006974; P:DNA damage response; 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 maturation; 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: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   CDD; cd14499; CDC14_C; 1.
DR   CDD; cd17657; CDC14_N; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 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; (Phosphotyrosine protein) phosphatases II; 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
//