ID A0A061AW39_CYBFA Unreviewed; 1053 AA.
AC A0A061AW39;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=BON22_5093 {ECO:0000313|EMBL:ONH65040.1}, CYFA0S_03e05006g
GN {ECO:0000313|EMBL:CDR39584.1};
OS Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=36022 {ECO:0000313|EMBL:CDR39584.1};
RN [1] {ECO:0000313|EMBL:CDR39584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YJS4271 {ECO:0000313|EMBL:CDR39584.1};
RX PubMed=25103752; DOI=10.1128/genomeA.00638-14;
RA Freel K.C., Sarilar V., Neuveglise C., Devillers H., Friedrich A.,
RA Schacherer J.;
RT "Genome sequence of the yeast Cyberlindnera fabianii (Hansenula
RT fabianii).";
RL Genome Announc. 2:E00638-E00638(2014).
RN [2] {ECO:0000313|Proteomes:UP000189513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
RN [3] {ECO:0000313|EMBL:ONH65040.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65 {ECO:0000313|EMBL:ONH65040.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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; LK052888; CDR39584.1; -; Genomic_DNA.
DR EMBL; MPUK01000014; ONH65040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061AW39; -.
DR STRING; 36022.A0A061AW39; -.
DR VEuPathDB; FungiDB:BON22_5093; -.
DR OMA; NAWDCPK; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000189513; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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 {ECO:0000313|EMBL:ONH65040.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189513}.
FT DOMAIN 629..1052
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 162..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 119746 MW; A710456D0EA7A056 CRC64;
MAAASPYTPE YSEELLALVL SLYREEVAPV LGELRLSKML DLLEVAQWNL EQYHKQLASG
NHIPLLKHYV VGLLYLYYVV PTSIQFQIKN KNYEVYVALK QLYERETHMS NVRSVVADYI
SYINDQTLLS QQLASLEIKN RTKRSSTLPS STLESDLAQY LKPPSINSDK SQNQSLHGSS
RKQSTTDLDS LASTNSSVVE DLWSPPELDP NDQLKLATDH DIGSTDELSI PPVPSFPPPV
PTNPQQEVPY TASQHRFSAP QMRLQHAKSF PTGDEEDDVH TEIPDFRTIP EDRYKEFFEP
KGGHRKDSYH SIVAEDDEGA LGVPTISTKA MYELLKEGVM SCLIFDVRPL KRFNINHIHF
QNLINVDPSL VLNSESFQEF QDVVGSVVER ESFVMFRNMS KYDVVVVYTD NKTSLSTEQG
ILGKFVSLLA ERKIKSRVLR GGFDSWTKYL SKSDIRSSDL KFVAKQPYIV PLPPSMPPPP
VPETGVSPRS TRESTPVSHH ETTSRIPSIP QVAPPVPPHH MTYPKVYEHQ HQSRPYPLQQ
SFYNSAHSSS GPYFQAPTPP PPSPPPPPPP QVYPQYPQQQ GTVYARPQAG TPQQYPHPVQ
RKHYQQRLDS SYIPTIQRNP NPFTHLSITG LRNMGSTCYI NSMLQCLFAT NMFRQMLVDY
KFQEYTNSKF QKPPLSPALA NLFEKMYLNG GCSIVPSRFL RTCIQLRPDL RIPSEQQDTQ
EFLMFMLDHL HDELSNSEAV VNDYPELMEH ADCGGEYEKW FEGLIKQGFS PISKIFQGQL
QDSLQCKACG YKSSNYSTFY MLSLSIPKST NLLRKQKKVA LEECIEMFTN DEILTGDNAW
DCPKCSKKRE QLTSVMSNDS VASMPKERKH RLHFSNNFRF RGRSSSPAPK KDKDKDKESR
WKKSSGLHAP SGGSTSETDN VFSHQRNKSI TVKSLTFVVL PPVLIVHLSR FLFYDISQKD
TTIVQYPLIL EIPHKGETVR YKLFGVVNHS GTLKSGHYTS IANKSLDHDL VHPNWYYFDD
ENVKLTDHGS LSGKDASHMS SSEVYVLFYE KIE
//
