ID A0A2I1G1M6_9GLOM Unreviewed; 1107 AA.
AC A0A2I1G1M6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=RhiirA4_436600 {ECO:0000313|EMBL:PKY40523.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY40523.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY40523.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY40523.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PKY40523.1}.
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DR EMBL; LLXI01000106; PKY40523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1G1M6; -.
DR VEuPathDB; FungiDB:FUN_004927; -.
DR VEuPathDB; FungiDB:GLOIN_2v1833492; -.
DR VEuPathDB; FungiDB:RhiirA1_505560; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000234323; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 44..172
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 198..515
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1107 AA; 129921 MW; FE4CE73715994A2E CRC64;
MDVFDQTTID DMSEEEDITP LPVTDYETMA NNIMPDLGQE IEEFKYNTWH VTNWRNLEER
ITGPEFEAGN WKWRILLFPF GNNNQDVVSI YLDFADMRAP EGWHSCVQFA LVLWNPEDPT
QYIYHHAHHR FTAEESDWGF TRFYCLRRLL TPYGSRTRAI IENDSANITA FVRVFKDPTG
VLWHNFINYD SKKETGYVGL KNQGATSYMN SLLQSLYCTT YFRKAVYQIP TKDDVPIKSV
SLALQRIFYQ LQISNTPVKT TELTKSFGWD SAESFVQHDV QEFNRVLQNN LEGKMKNTIA
DGAITKLFVG KMKSYIKCDN VDYESSCVED YYDIQLNVKG CKTLRDSFKD YIQEETLEGN
NKYQAEGHGL QDAKKGVIFE SFPPVLHLQL KRFEYDYQSD TMVKINDRHE FPMEIDLEEF
LSENADRSNP HKYLLHGVLV HCGDSHEGHY FALLKPEKDG KWFKFHDDRI TRVVDKEVLE
DNYGDEYPNA NIIKVRSTKI HKRFTNAYML VYIRESHVDE ILSPVVPEDI PEHLQKRLEQ
ERAVEEQKRK EMEERHLYLT VKIVTTEKFK VHQGFDLANF DDRQYPLSEV YVYKILKSDT
YRSFKDFASR NFNIPPERVR FWVFVNRQNR TVRLDAPIPE LYINTSMEQI HANMTTRRNG
MELYMEVADK PIKRKKWFPT VPKASRIIVF LKYFDPDKQT LEGLGHLYVQ KFGKVGDITR
VLCEKKEFPP DTPLKIYEEV KPNMIEEMHF EFTFQQSEIQ DGDIICFQKA LTEREIQEHR
SVCRCWNIPH FYESLALRIV VSFKPKLEDQ YSKPELTYEQ VSYSEFDLIL NKKWTYDQVS
GAVATHLNTD PLKLRFTTAH STSSTPKSVI KRTTAHTLSE MLQTVYLSPP AYVLFYEMLN
ISIVELETKK FIKVYWLGNT VKDEEAIDLC LPKNAIVNDI KKILKNEKMT LSSPYSRIRL
FEVHHNKIQK EYTGTEPIER IQEHATLYAE EIPHDEIYAN QNDRTIQVYH FTKDPLCLHG
IPFKFVIKNG ETLADTKVRL RHRLGMSEID FLKVNIAIMP RTSYAISTYL FGDDIILSEM
KLSNEDCLGL DHPDKTGRTE KVIFIRG
//
