ID A0A0D9NUH6_METAN Unreviewed; 1601 AA.
AC A0A0D9NUH6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=H634G_07416 {ECO:0000313|EMBL:KJK77677.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK77677.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(2014).
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}.
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DR EMBL; KE384738; KJK77677.1; -; Genomic_DNA.
DR STRING; 1291518.A0A0D9NUH6; -.
DR Proteomes; UP000054544; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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:UP000054544}.
FT DOMAIN 246..365
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 598..1421
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 25..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1181
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1601 AA; 176500 MW; 24E240BC1C36EE2B CRC64;
MGYHLSLPAP SPAFVHELLG QLTVKTSSSK KRRLARPPPS TKQVLDAPAS PSPDSALPSC
EVEPDDDPVL SFSAELSSVI ASRESEAPRY LLRSEPLPVA TASSLPPRLQ HTHAASLVSA
DYASSTASSP CASAYAELSL ESDRGGDETG SARNPGRSQS PFVVPRRAMM NGDADLPQRS
SSPLKRRASS MDPDAAPTKN GTTMDTDASQ PSQQIDPSST EFPRAMSVDA PDVNGHEASP
SQLAPPPLLE QVKIIEMLLK AFAEAPPQEG SVAYLVSRTW VDKALSLRTG SKPAAAGAES
ISLGPVDNTD IIQETIKDSS GRDFVRLIPG LGNESFELFP EDAWKMVMDW YGIKEGQQPI
ARIAVNTADS KQAPPNILYE FHPPIFHVHR LWSDVSTIPI EQSLKAKNPP PLIVARSSTT
HAQSFLREIK TLAGVGLERK VRLFTIPASA QVTRQETDAA SALTPPDSPG RARGGNENRS
VWPTLLVDVV SFSQVRDIRV SVPLIDYTAD DKFNGQSTLQ HYELTTDQTL VLDEAIGNFF
VSNYTGRMKA ADKSTPSRLL GSTISSKTSS NRSSPVFDGP MTRGRVQKKR HGRSIGAVGL
HNLGNTCYMN SALQCVRSVE ELTKYFLTES YFTEINKTNV LGFEGRVAIA YGNLLREVYE
EGRGSVSPRD FKSTVGRCRP TFSGWSQQDS QEFLGFLLDA LQEDLSRIKK KPYIEKPDST
DDMINNPEAI KEMADKVWDI TCRRDDSVIA DLFTGLYKST LKCPECGKIS ITFDPFNNLT
LPLPLENMWS KSVKFFPLND VPVKIEVELS RHSSMESLKQ FISVRTGVPV ERLMGAEEFK
DRFFKIYDNT QDVSEEIQSS DTPTIHELEA VPTNWPSKKP HKKYRSMLDI DTPPESAEWS
EEECHTMVVP VLHRRPQIPG RGPEGISPPH FITLTREQAS DYDVIKRKIL QKVATFSTWS
KFKDTQETDA SDGVDADLVI TTASDADSSG DSKIASNSVE GEDDMVDITM RDAVDNISNR
ATISSIAQPT ILKQFNTQAP KFADPANFLN PELQNLFDLC YFKNDTDGPV PTGWSNVDNT
RTLPRLADRI PEPRVKDGDA SSPGSSNSTG SGNEESGDED EATPESTQTR MIEESSEEDA
HQAAKINGRS GRHNSKYNQG SRKKFKGHKG YGKKGNKRRD KQTRASKLSQ RANIVAPQPM
PPAVSDGGPL IRLFEGIVVD WTEDAWDAVF GNNTNKPDPA RGSRTFVDVQ TLHDPALKIT
QRRRVTRKTR GITLEECLDE FERAEILSEQ DMWYCPRCKE HRRASKKFDL WKTPDILVAH
LKRFSSSGWR RDKLDVLVDF PIEGLDLTSR VIQKEDGKAE IYDLIGVDDH YGGLGGGHYT
AYAKNFVDGR WYNYNDSSVH VVSDPTSVIT SAAYLLFYRR RSSGPLGGPR FKEIFDKFDK
ESVHSDNEAT ESGEEVMTQR STKTTVTPLT GMDDDDDELP IYDGNTIRRS IEDEGNYHSG
SKGALDMTQS WSFTSLNGNG VNGNRDTDCA SDDAQFDSSG DDRSKALSEQ DTDMASAAPF
EEGASWDERG VISVPADGAG EGASEEVTEI HLEGDKMTRS A
//
