ID A0A0E1RW17_COCIM Unreviewed; 1128 AA.
AC A0A0E1RW17;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CIMG_06538 {ECO:0000313|EMBL:EAS31059.1};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS31059.1, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704912; EAS31059.1; -; Genomic_DNA.
DR RefSeq; XP_001242642.1; XM_001242641.2.
DR AlphaFoldDB; A0A0E1RW17; -.
DR STRING; 246410.A0A0E1RW17; -.
DR GeneID; 4561005; -.
DR KEGG; cim:CIMG_06538; -.
DR VEuPathDB; FungiDB:CIMG_06538; -.
DR InParanoid; A0A0E1RW17; -.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
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:EAS31059.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 66..196
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 222..547
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 130881 MW; 15D71A5F96292BB3 CRC64;
MDNLEESGMV VDEFDQYSND HTDDVVLVSP SGSPSEPEPE FPLADDYESM ITRVLPELPD
TETLEQTHHT WHIQNWTRME RKEHGPIFEC GGSPWRVLFF PFGNQVTEYA SFYLEHGYEE
APPEGWSRCV QFALVLWSKN NPSIYVSHVA THRFNASDGD WGFTRFCELR KLFHGPFDEN
GSPLIENEEA CLTVYMRVVK DPTGVLWHSF KDYDSKKETG MVGLKNQGAT CYLNSLLQSL
YFTNSFRKAV YQIPTEEDSK ISNSAWTLQR LFYSLQTSDN PVSTQELTSS FGWESKQIFE
QQDVQELCRK LMERLEEKMK GTPVEKALHD LFVGKTKTYI SCINVDYESS RIEDFWDIQL
NVRGNKTLDD SFKDYIQVET LEGENKYDAG DPYGLQDAKK GVIFESFPPV LHLHLKRFEY
DIHRDAMMKI NDRHEFPEEF DASPYLSENA DRSEPWVYQL YGVLVHTGEL NAGHYYAFLR
PTKDGYFYRF DDDRVVRATM KQTLEENFGG DWITLPNGNA GMRQAHFARG YSTKRSMNAY
MLVYLRKSRV DDILVEVMKN DVPCHIEKKI AEERAELARR KKEREEQHLY MNVSLISDES
FKHHHSFDLT SPDLDPNDPA APKAYRILRA TKVGEFAKQV AEEREVAPEQ VRLWVMVNRQ
NKTTRPDQRL RDMEMSMEQA FNEFGTKNNP FRLWLEIGEP GVDGKVSWPD SRGPNAHTLI
FLKYFDVHAQ TLTGVKHVFV RKHAKVSEIS STILELMNWA PGTSFLLYEE IRHSMIDPMK
PKHTFHQSEI QDGDIICFQR SIPESELPPT VIYRNVQQYY DFLLNRILVT FAPIEPNPEQ
TFTLTLSKKM TYEQFSTKVG EHLKVEPTHL RFAPVIISSG APKPFIKRNV AQNLGQILTS
PYPGTGYSHR SDVLYYEILE TSLSEFEMKK NIKITWLSEG IAKEQIHEVL VAKNGVVSDV
IESLQKKANI DDETIRNVRL YEAYSGKIYK ELYDTYSVAG ITDYVTVFAE RIPEDELNMQ
EGEFRINAFN FDKEPQKAYG CPFKFVVKPG EKFKDTKERL SKRTGIKGKQ FERIKFALVS
RTPYSKPLYL EDDHILADLT TDSEQQLGLD HVNKNRNFWG RSESFFIR
//
