ID K1Y7U9_MARBU Unreviewed; 1506 AA.
AC K1Y7U9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=MBM_00272 {ECO:0000313|EMBL:EKD21159.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD21159.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD21159.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD21159.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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; JH921428; EKD21159.1; -; Genomic_DNA.
DR RefSeq; XP_007288161.1; XM_007288099.1.
DR STRING; 1072389.K1Y7U9; -.
DR GeneID; 18756207; -.
DR KEGG; mbe:MBM_00272; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_9_1_1; -.
DR InParanoid; K1Y7U9; -.
DR OMA; KPRGCTG; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000006753; 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 SMART; SM00695; DUSP; 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 Hydrolase {ECO:0000313|EMBL:EKD21159.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 92..212
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 458..1263
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1032
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1506 AA; 165587 MW; A3D59E5CFCA56E4A CRC64;
MGGAADLPQR SSSPLKRRAS DLETDASSSQ KDDVDMVQVP PSDPTEVDEL SISSRTRTHS
VDALANGVEV NVAALPAAEQ QISPARRSTD IPPIESQITT ITTLIKAEDE KQLKEGDVTY
LVSNLWLNRV ISRGAEARQK SKVEPEGEIG PIDNSDIIQQ TLTDSAGVEF VQLKRGLVAL
ADYTYFTVDA WTLVVEWYGL TPGSIPIRRV AHNTSPKGSP ENIQFEIYPP VFTIHRLYGD
HTNIKIPNEI KDMDPAAPVY VLSTSTSCVE FLKTIKTKAG IEHEKKVRLW RVPRLQPAAN
PIPATSIAAT TPPTSEPSSP TGVLMGPETR APQDSWKLLV DVATFLKLEK GVQRELIGFD
DHSANAKYNG SSTLAMNGLA ADDNIVLDEK TDGQSDTFVS TYTQGGKANS TTLAGNSSSS
YIGPSSQSNS GRNSPALSGP ITRGRAQKSG SRKPPGTIGL ANLGNTCYMN SALQCVRSVE
ELTKYFLTGH GKEEINPHNP LGNNGNVARA YGDLLAQFYN DSGSSAVRPV NFKNTIGKYA
PSFSGYGQQD SQEFLGFLLD GLQEDLSRVL KKPYIEKPDS TDEMVNNPEA IREMAAKVWD
ITKQRDDSVI ADLFTGMYKS TLVCPSCNKI SITFDPFNNL TLQLPIESRW SHQVYYFPLN
DKPILVTIDI DKNASIGSLK DFVSKRVGVP ADRLFVCEEY KSKFYTFYKD LAVASEKIGT
NDHVAVYELE AKPTNWPPRA AKKLQAKSFG NESDAEDEIP PWDDPMAERM LVPVFHRVPN
SRGFSGKPAW EVTCTPHFIM LTPDEARSED MVKRKILEKI STLTTSSQFL DMDVDASVSD
CLDPDIVLTT GSDADSSGGS KVVASSVDGD DEIVDVSMKD AAAAPGPLGK FNTRRPKFIL
PDSHLNPSLQ NMFEIGYFGT RKNLINTGWQ IVTENKVFPK ISSRSPQPQA DDGSVSGYEG
SRTSSENPED SVVNSGPAKV TRMNDESESE EDATPKDISR VKVLPVRSRV GSTRGRKSKL
KTYSKKGNKR MARKAKPEQT IFDDDEDSAD GGPLVRLGEG LVVDWVPEAW DALFCGDSSD
DIRGIPTWQN VPTLEDSELQ ALKSYRMKRK KNGITLEDCL DEFGKEEILS ESDTWYCPRC
KEHKRASKKF ELWKTPDILI MHLKRFSSSG WRRDKLDVLV DFPLTDLDLS SRVIESEDGK
QEIYDLFAVD DHWGGLGGGH YTAFAKNYDD QQWYEYNDSS VTKVTDLSRI VSSSAYLLFY
RRRSDVPLGG PRFKQILHEY NSSRQSSEDQ YSESGEGKGL VGNSSPRGSS SAWFGVGAAR
PQLNPGSSSG EEMMTINPSD LESGLPPAYE EDEAISLVPS VEKDDSGYST RPTWGFGGLN
SETEGYVLGA NSRQIVSGAG SDAGDAGSDV AEHNSSASDS SLIQRKRDLA SSEAFDEDFE
QAFVPDMTEE QEAASYDLRS EVVEHVHGKV LYRRTLSNGG NVEHFEEVDE PVVEIHVTDN
DDLNIE
//
