ID T2BP03_CRYNH Unreviewed; 1113 AA.
AC T2BP03;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CNAG_05650 {ECO:0000313|EMBL:AGV14889.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AGV14889.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AGV14889.1, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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}.
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DR EMBL; CP003833; AGV14889.1; -; Genomic_DNA.
DR RefSeq; XP_012053906.1; XM_012198516.1.
DR AlphaFoldDB; T2BP03; -.
DR GeneID; 23888948; -.
DR VEuPathDB; FungiDB:CNAG_05650; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000010091; Chromosome 14.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03775; MATH_Ubp21p; 1.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGV14889.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 49..183
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 209..528
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1113 AA; 127967 MW; D0F6A7B12439BF23 CRC64;
MQQPVNDVQD IILDESPAPM EVDDIPNVHD YEAYAAKCMP DLGLEIEDFQ YQTWRIEHWS
QQPKRIVGPE FSCGGHKWRI LLFPQGNANG QPNDMVSVYL DYANPKTAPE GWHACAQFCL
AISNPWDPTI QTSSHAHHRF VAEECDWGFT RFVDLRKLYT ADPVNGKNRP TIENDEVEIT
AFVRVLKDPT GVLWHNFVNY DSKKETGHVG LKNQGATCYM NSLLQSLFCT NYFRKAVYQI
PTEDDIPSES LALALQRVFY HLQTSNQPVG TTELTKSFGW KSLDSFMQHD VQEFSRILQD
KLEIKMKGTP AEGAIPKLFK GQMKNYIKCI DVDFESSVIE DFYDIQLTIK GLKDLRASFK
EYVSVETLDG ENKYQAEGHG LQAAKKGVIF KSFPPVLHLQ LRRFEYDVEK DALVKINDRH
EFPFEIDLGE FLDESADRAQ SHVYKLHGVL VHSGDLHGGH YFALIKPEKD GRWYKFDDDR
VTPVTDKEVL EDNYGGDMLN GLVPPHQRTQ ARTLKKFTNA YMLVYIRETE LDTVLAPFTE
SDTPPHLKAR LDHEREQLEA KKREKDEQHL YLTAKVITDE IFSKHQGFDL ASFEDKNIPA
TDLPTFRVLK NESYPTFKSR IASHFKIPER DFRLWVLVNR QNKTTRPDVP IHENDNTQTM
ENIRNSMAAR ASDLKLYLDY NPDHAKFNEL HAEGKEPPIM IFLKWFDCSR QTLLGQGKVF
VDKHQKVSDL LGIIQERMGW PSSTPIKLYE EIKAGMIEGM KLKQSFIQNE IQDGDIICYQ
VELPEKEIAD LEAQSLYSSV PQFYDFLQNR ILVHFKPRYE DRAASVPEFD LMLSKKMTYD
VMAHRVGEFL KYDPLKLRFT SAHNQNGAPK AIVKRSLNQS VADITQTSYY NQHAHICIYY
ELLDISIIEL ETKKSLKVVW TGRHNKEEAT HSFLLPKTCT FNDVADNMSK LVKLEPNGSG
KIRIFDVSPS GRSPREHTGS EMIGNLPESA ELYAEEIPVE ELQAGEGTKI VNVFHYSRDP
SRTHGVPCKF VLHEGEPFSE TKARLQERVG VSEKEFAKYK FSLVTSTVFK QPSIVEENDI
IYDHKWAPDD ALGLDHIDRR PNKANVEKGI VMR
//
