ID G4UYY6_NEUT9 Unreviewed; 1046 AA.
AC G4UYY6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=NEUTE2DRAFT_96223 {ECO:0000313|EMBL:EGZ68070.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ68070.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ68070.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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};
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DR EMBL; GL891269; EGZ68070.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UYY6; -.
DR STRING; 510952.G4UYY6; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_005922_0_0_1; -.
DR OMA; PFVHTYE; -.
DR Proteomes; UP000008513; 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; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 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; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT DOMAIN 357..487
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 635..1044
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1046 AA; 114936 MW; 44F7E0CC96CD2180 CRC64;
MVNHATPAHS VNGQNGHITG GLDGTQDGGQ NRIINGGGGG GGGGGGGHGP GTGGSKRPPM
PHLDDLKAVT VSIDPATPID SALRLAEEAL QQAKAFQSFG RIDMAFKSYI KANIIALDII
PKNKDWALLD RSRPNVYMRH QHLLRQIKSL TYALPDQSWP SPGRSKPAVH PKPQALHGHT
LQHSGGPATT STNNAAQDLA LRFAKLRAYT ASTPSPANAT TIQDPRIRTQ PIPQPIMPIN
PPAPRDPPRS QVPSVPPATA LADLPRVPAA IYNPPRGTVS NEAAELPSSA PRAIFTRKGS
TASATGMNRN GRPRTSDESL VSGPPVTSPK MRPKPAIPDG DTISAEELER YMRVGARDVS
ILVIDIRSRD EYDEGHVMSQ ATICVENEVL MRPDISASDI AESMVLAPQA EQQRFERRHD
FDLIVFYDQR SKRLVSSPQT PEERAVLTFY NALTAYDYAG GSSSQQRLKL LKGGIEAWTD
LVGTGALQTS STSAAARSQP RPPLTHNLTS RLRRNVTRPI QDLAEVQKWE ENIDIVTPVR
TTEDFLRRYP SVSTIQESMT SPINPAAARP ASPLPRHIVH EQNLYSSLPS PPTRPAPTVP
RRSYSGLAET DTSTTATSTR SSLKSGIEKV RKFRTGLVNP GVFCFANSSL QAMFATPGFA
RELYTGVWKD VYKVPLKADE KNENPQLLTK YLAGLFHWLD EGTLRSLEAK HLMAYIHFIH
SKNADGRKKP ETEIFGGPAQ QDAQEFYSFI IDNIHDETNV HRDRKPPKEE KPYTPKNGTV
IQNAIDYWRD YSTASASIID KYFRGLEVFI SRCQNGECRQ EIRMFQPCDV WILNIAAETG
GEGHGYGVTD LDRLLASHQA TEHFPDLKCE TCNQPGRTRR AKFARLPDRL AFCLNRFNSS
FGQSRNSFSS ILSGGGSNKI HTKVRFPIRD LDLTKYCAEP DPDMATTDDA HYAGRMKYDC
YAVTVHVGQG INGGHYYTYV QDEQSKDPTD WFKCNDDLVE RVKIGSGGPG LNGNGNGNGG
MPDLTEAMYA NGNTSAYMVY YRRQGT
//
