ID A0A197JWY7_9FUNG Unreviewed; 1125 AA.
AC A0A197JWY7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:OAQ28789.1};
GN ORFNames=K457DRAFT_1832998 {ECO:0000313|EMBL:OAQ28789.1};
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:OAQ28789.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ28789.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ28789.1,
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; KV442046; OAQ28789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197JWY7; -.
DR STRING; 1314771.A0A197JWY7; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02257; Peptidase_C19; 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 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000078512}.
FT DOMAIN 671..1123
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 124006 MW; 0D43E3A0332BCF5D CRC64;
MVQPTKLAQR MKKDSGSSTT NGDSKKLKGS RSTLWGTAGV DGFGVYGVGD HSDEQDENKD
TGNTDPVPAP RKRKSGGASG GGAKIGGAEV KTKQPREDAP SKKQKSGTTT PNPPVNTAFL
NYFNKVHVND PKKPKESASP ASIPTPSPPS APPRTTSDAQ STKSLKEMFD LPPPPSSLRS
KEPPTETSLR EAAKRAIIES IDLTNETPPS SENSSPPDSE SAPQEAEEKN NNVTRSTTSM
NEPRMDESLT DMMDVDDDVP ARSTLAQRKK APTKPRSKAA TSKKSVLKEE SEESPKITPA
KGAGTKKRKP VTIDGQGLET KIDDASEAPK EDPPKEDPPK NRTVLEFFKF QPKPEVKVAD
ALQHKASSGT RIGEVPQLAT TKAAAKEESQ DRTPMHSCPQ SHPSKPVTPS SFSAIEGTMT
TPIDETLKED IKEVVMEEPA PLADEVLFPS QSEKPAQPQR RRLVRASQLQ HNYNETSGSD
DEQELSVKSA RRRLAPKKHK QDAGAERDTD SLPESEAAPE PESEPEAAHL AKSRHFFKSY
FGSTSSLPSI PKVPTEPVPE PNGESKVFDL GVTRPAQKTY SKKAAPVTKK KVQKKRSAFS
GSDESGSDRD SRSDDDLSDF EIKENEKPDP NQKSISSMFA KAPPRPAWAL PTVKSEPRRE
LTPLSQSLLS GGLMNMGNTC YLNSVLQALR NTAGCTDTLY LMMQRILELA EERGRNLNSG
VYRWRIFEQV VTIFQELDQR ERRNEADQIY ERAYCPKQII ETLRGGKSQF NTSGQQDAPE
FLLYLISHFD DIQKSTQRMA ARAAAVQKPD TEMGTQIENE VAPLTAPSIM TTPSTSTSST
SSALFSCSTA STVATSSSSV WEPVNDLFQI STERVQVCDK CNKVTTRDDR EFDLTVQIDT
ANPGLVRDLE WGVTDTMKQE VTTEDNKRFC ERCKSNEHAH ISNFFTSLPK IMILRLQRSN
FMQGAVKIPN GVACSQRMNF RQWMSSTYQG DHPDYELCAI IVHRGREIFA GHYFAYIRKD
VEIETTITEP DGESRTEKKA YRWLKYNDSA VDPVSDEDME KLFSGNVKKL KPATSSNTSG
SGGSPTENNK VHLSGDDNMD LSALTSILDK HVATPYVYLY RRLDT
//
