ID A0A197K374_9FUNG Unreviewed; 917 AA.
AC A0A197K374;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:OAQ30909.1};
GN ORFNames=K457DRAFT_154590 {ECO:0000313|EMBL:OAQ30909.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ30909.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ30909.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ30909.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV442032; OAQ30909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197K374; -.
DR STRING; 1314771.A0A197K374; -.
DR OrthoDB; 1385257at2759; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd02667; Peptidase_C19K; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF39; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 110..252
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 292..917
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 51..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..657
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 100249 MW; AB7EEF48E474A6FB CRC64;
MGKKKKGGRR YSQSDFAGDD AILTEILTSS RKSGRFEDPK VERALAFPPK PIPVTAAIPE
PTAAAAEANP TKEASTSSVS VDNPDLVTDS TTTDVATDPS ESTITPGGGV KCQHVKSAVN
LAKLRKGVAH QKDWDHCLGC KAAESKAKKL AQRIDKSMSK LSLSESEGSA AGADEPLSAE
SLWMCLTCCE INCGRTIRKH AVAHHDGKKN NHPLAINLGT TDCWCYECDD MIVPTKNKNQ
LIQECQVTFE KAFQAKQAKI RAASAAVSKK TKGAAFETII ASPLAKAKVF TPGLQNLGNT
CFFNSVVQVL TETKSLKSIL SEDGGASSGF TKSLAASTDA GLGPLTTTFK DFLFTMWKQQ
GGTIAPRDLF TQIAKKWKVF RGFRQQDSQE LMRYLFDGIK HEELDMIKRH LSEESGSHND
KAEEAKEEKE DGLTGSDEKK EPKFVPFIDS CFSGKLVSVI VCDACKKCSY APEDFFDLSL
PIRGPTQAGA VAGSSLRARL LAQSKKASAA KEEEPTADDT PADEKDPLPE SDRPSETHLR
HVGKLLKSIG PSTSEELSIQ RSLNQFTSVD RLDGENKFAC ENCYKLIQAA KEKEGGSMEQ
GQKPDANNNV SEDVVVEETS KDEPVQEVET TDMPVAAPES DDNESNNDDD EESLGEEQTD
SFGNTIPKKA KKVESKAAES KKPTEEPKYI FRRAFKRYLI SNLPPTLVLH LKRFESSGRF
GQMRKIEDHV DIPVEIDMAP YFVPKNEIEE EEENESETGS EARKEEEANG SKSKKYRLYG
AVVHMGTLGG GHYINYVLSS KVQVAEATKI AAEKAKSKST ISVSGLELPD VPLAAMLAQQ
KETTREKKQG VAVVDKDVSS SSPSTNGKIE EDSEQEVPAV QEEDKRQWIA CSDSSVRLSS
LQEVLASRAY LLFYERC
//
