ID   UBP16_EMENI             Reviewed;         624 AA.
AC   P0CAQ1; Q5B9A7;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 16;
DE   AltName: Full=Ubiquitin thioesterase 16;
DE   AltName: Full=Ubiquitin-specific-processing protease 16;
GN   Name=ubp16; ORFNames=AN11684;
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA63444.1; Type=Erroneous gene model prediction; Note=The predicted gene AN2873 has been split into 2 genes: AN2873 and AN11684.; Evidence={ECO:0000305};
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DR   EMBL; AACD01000051; EAA63444.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_660477.1; XM_655385.1.
DR   AlphaFoldDB; P0CAQ1; -.
DR   STRING; 227321.P0CAQ1; -.
DR   EnsemblFungi; EAA63444; EAA63444; AN2873.2.
DR   GeneID; 2873795; -.
DR   KEGG; ani:AN2873.2; -.
DR   VEuPathDB; FungiDB:AN11684; -.
DR   HOGENOM; CLU_011238_0_0_1; -.
DR   InParanoid; P0CAQ1; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..624
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 16"
FT                   /id="PRO_0000376621"
FT   DOMAIN          46..620
FT                   /note="USP"
FT   REGION          453..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        424
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   624 AA;  69446 MW;  0023FD124DCA2A7C CRC64;
     MQEKPTTVAA YAAGASLAAV ALFYVFGPNY TIDGDEAGGN RKKSIVGLSN PANDCFINSV
     LQALAGLGDL RLYLIRELHR RELDGPEIYN QLPGPEEADQ LREKRPDRIR ELQQGTITRA
     LKEMLDRLNE RPIYKKTISA RAFIQALEFA YRTRISRNQQ DAQEFLQIVA ERLSDEYHAG
     VKARQRAEKS IEFNPYQERE EAPSEIEVRL DDGTENGLPA IIDTKLKEID NEYGFPFEGK
     LESQIECQFC HYKYKPNQTS FVNLTLQVPQ RSSTTLNACF DGLLKTEYID DFRCDKCRLL
     HAIEVKSNAL VKAGSATDRQ RLEAEIEKIQ LALSSDPENA LDGVTLPPAE LAPKRRIARH
     MRITVFPKII AIHLSRSMFD RSGSTKNAAK VAFPERLPLG GILSQKWFKL LAIVCHKGSH
     NSGHYESFRR NHLYPPYSTP SVFSSYAQSR AASENPSRVA SPRLPASSSS TEPPALNISP
     PASTSTNSPL SLTPDSPSRP PSATDLKSPR PTTSSSRVSF QSTHSSSKQT ISPTSAARNS
     SSLDTARLSS PASRSSLAER NASATDTEAS ASASLASRIR RRRKTADRWW RISDEKIKEC
     KTSDVLGMQK EVYLLFYEIE KSGS