ID A0A0G4KED7_9PEZI Unreviewed; 616 AA.
AC A0A0G4KED7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE Flags: Fragment;
GN ORFNames=BN1708_009111 {ECO:0000313|EMBL:CRJ83720.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRJ83720.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRJ83720.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRJ83720.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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};
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DR EMBL; CVQH01000225; CRJ83720.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4KED7; -.
DR OrthoDB; 1353379at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT DOMAIN 1..416
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 424..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CRJ83720.1"
SQ SEQUENCE 616 AA; 69107 MW; FA0D131D29ABE982 CRC64;
FKTTDEPRRK LVTLLRLWVN MLRSGKLIYT DMTKLIQDSL AECGWQDAKE LEQQDTSEAF
AFITETLQLP LLQLQVDLFH QGKNDDDDHK IVNERLLNLA VPPDPEGKGL RLEDCLEEYF
NTQVDVLRDS NQEEKRDARR PTTSRLNTIR VVTQNEETES PTKAVVASPV EFTPVLDRRP
TETANGLING ETAESSRPAA RHRSTSVIQH VLVDGKGRPA ETDNSSLLER ARRKSSTVVK
AVTIPAWQFF RLIPWHSAGN SEPQNDQDVA VKFSQRPVVG ICLKRYGLSE RMVPQRLNTF
IDIPDSLRLP HFMLADEKHL EEDPNGFSTE YKLVLQSVVC HRGESVNSGH YIAFSRVAPK
LLTDNRRHDL DPPPDYEEAQ WAKFDDLHID SRVTYVDDIK QSIKEEMPYL LFYQIVPMME
VVSADETETE PPSYADSKAS IATSTDPSLA DSGHMGTAGS SSGDYFEKAT KAQAPSIRFS
SDIERSSRDS IEDLDPHSKD SRRTSINPLE SVIGTPGRTP DTASPAVTPN EETTRERFSR
AAALFSNKSR SRPPSQAXRA HQPHDGPPRR LHAAKQGDIA RRQCHRSHCK RAARTERGRP
DGGDGQAIGR SATPVV
//
