ID A0A388KPG8_CHABU Unreviewed; 1647 AA.
AC A0A388KPG8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CBR_g10897 {ECO:0000313|EMBL:GBG71960.1};
OS Chara braunii (Braun's stonewort).
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG71960.1, ECO:0000313|Proteomes:UP000265515};
RN [1] {ECO:0000313|EMBL:GBG71960.1, ECO:0000313|Proteomes:UP000265515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S276 {ECO:0000313|EMBL:GBG71960.1,
RC ECO:0000313|Proteomes:UP000265515};
RX PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA Rensing S.A.;
RT "The Chara Genome: Secondary Complexity and Implications for Plant
RT Terrestrialization.";
RL Cell 174:448-464(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBG71960.1}.
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; BFEA01000156; GBG71960.1; -; Genomic_DNA.
DR STRING; 69332.A0A388KPG8; -.
DR EnsemblPlants; GBG71960; GBG71960; CBR_g10897.
DR Gramene; GBG71960; GBG71960; CBR_g10897.
DR Proteomes; UP000265515; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02661; Peptidase_C19E; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
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; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000265515}.
FT DOMAIN 477..790
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 21..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1647 AA; 173351 MW; DD54D8EC1DE05EE0 CRC64;
MMGQPAAGAV VSIMVGGGGA MGGQGAGKPP PAAAAGGGGG GGGGGGGGGG GGGGGGCGGG
GAGAAVDVAS DAVCAGALAG QVSADRDRGR GGIAAAAAIA TDIAASASAS ASAQGGTTSR
AAAGHNHTHM RDAFVRDLGL ASSSSHVPSS GGLASTPRRR GGGSSSADVE ATAIGRLTES
CHPTAGGDAH TVGCASTGAE VAGSNTTGAG KMRMAAGNGA LLAAPAAAIA AKLDGRQQKH
LSPPAAAAAA AATTNNRSSL GSVEEVTGPA QSKAIHSPSG SLGKDRDKPS PTWEGERRRG
KRGRGDGSEE TGEKPSGGER KKLGKEDKGE RAIRSTRVKK DVFPHKEGDA EEKGVRGDKY
QQGQDCRLVE GKEGRGGPSH SAGGGGSLKR EGGGGGGARG EMPSSMNGSD GLISDRKGPQ
LSPRNDSCKS DSKSKRDAAK AWDGCGGSGG GGRGGVTTGE DRSGGCKAEC PQIRIGAGLR
NMGNTCFLNS VLQCLTYTAP LVQFLESGRH RDSCNAAGRF CAMCAMGGHV KRALCSPGGV
VVPTQLVKNL QSVSRCFRVG RQEDAHEYLR YLIDNLHKSC LPLSKLTKKG KNGTQASAEL
NSFVYEAFGG QLRSQVRCTQ CQYCSNTYET FLDLSLEITR SPSVGKALQH FTSPEVLDGD
NKYKCDKCKR KVKALKQFTI NKAPHVLTVH LKRFDHSGRG GVKIDRKIEF LPTLDMRPFM
SNKKEANTIY QLYAVLVHAG HSTHSGHYYC FVRPSPNAST WHAMDDSNVR QVSEKMVLDQ
RAYMLFYIRL HPSRSTESPK PSLPVSDANG PGKKDLVSAG ATGATAANGS HQKSPDICTR
SANANGAQKQ ALKRGPSGQF NNSAVVQVLS NGTGLTQRSV EASASENGDL GDVTRISSAS
VQPFSRHDVE KSENAGGGRN KAAQNGAETV AKKVDSFIKT PAVKSVPVPD KMKKAHGEEE
AEEEGDAQWA ERQEGVRKFA RKMESAVSAS SIGKGVAKDD QKTEMVDELE KAARNKLVTA
TDCAMGVPKK DPAEGLCGSV VDSGVSGKQA NLKVLGAERE SGRGVDEEPS RSPASTERSM
KRKRVGEGAT PVVMINRFYS MDAAQGLEES GLAKGSSSPS EQEQAKECRS GRKMSPFLSK
TDRKTETLGV RSVGSLDRQF ENCQRKVAVD KTSADAPNEC RASESSNDDL AHQNGVPDNI
LDQGASVPCH DESRGTSGCD RGCFSLTTTH VVGRMTDGRG CRIRNGCGHR AGKLLIRGRA
KVRKKIIGVR LMVRLSRLLH SKFRRKMPIV WGLARMTKRR SAVRVEGDGS CNVAENHCQT
TRESEKPHPR LTQGGGDKER VPEESLRKRD AAGKGAEEKT ANCKKRSSSV DVNAMSLSGK
EGRREQEEMW TSCETLSVAN GDRKQFHQAK TQDRSVVLPA SDMAASGRTV NFRAEDDDGV
AETAQMSDRS ETCSSDSDVV EMLSARREYD SPGNNQRMRA TALDANGTKE KPKASKFKPP
PQNVRGAYGV EVGTWENDVE ERPESLLQPD TRSHKKRRYD DWDAEYDQGK VKKVRNKHGK
SEAFPDAGNP FQEFVDDAGQ HQHGGRNRHG GGRWSGGRGR GGGRGRGRSE GNRGGNFQMW
ANGEKGRGRG GIGRRGGFGN RHGWGDG
//
