ID A0A167JPC7_PHYB8 Unreviewed; 639 AA.
AC A0A167JPC7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=PHYBLDRAFT_137306 {ECO:0000313|EMBL:OAD66428.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD66428.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KV441003; OAD66428.1; -; Genomic_DNA.
DR RefSeq; XP_018284468.1; XM_018429850.1.
DR AlphaFoldDB; A0A167JPC7; -.
DR STRING; 763407.A0A167JPC7; -.
DR GeneID; 28990756; -.
DR VEuPathDB; FungiDB:PHYBL_137306; -.
DR InParanoid; A0A167JPC7; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000077315; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
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; 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; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 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; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 63..191
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 217..543
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 504..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 72139 MW; 9726F31600AD7F26 CRC64;
MNSHGSALTV TAAPKSLGLD MPVMPSVMQA EPLDLLKKKG IFNEEVMVPR ILPDTSGLQT
VEFKVFHWPV ENWKDAELKS YSPSFIAGGF TWRILLYPKG NGQHDSLSLY LKVEESSANV
PDWHVCAQFG LVISNPDDPT QFYSNQAQHR FCGEEVDWGF TRFYEIKGLT RTHQGKGPFL
INNRSHISVY LRVMKDETGV LWHNLIHYDS RKETGFVGIK NQGATCYMNS ILQSLYCTNS
FRKAVYQIST ETEDPTKSVA LALQRCFYNL QSSNDPVGTT ELTRSFGWDT LDAFMQHDVQ
EFNRVLQDNL EMKMKGTPAG GTVRGLFVGK MKSYIKCLQV DYESSRVEDF YDIQLNVKGC
KDLRESFKEY IAVETMQGDN KYMAEGHGLQ DAQKGVFFES FPPVLHLQLK RFEYDMKRDS
MVKINDHHEF PESINLDAYC SKAGGDEAGP FDYTLYGVLV HSGDLDGGHY FALIKPEKNG
KWFRFDDDRV TPVTLKEVYQ DNFGDEPLRS SNDPSTLDGK MRNGSAQSLK RFTNAYMLVY
IRTSKVDEIL APVVDADIPV HLNRQFREGR EVEKNGKNRE EVHDHVVGFI AKLKRSLGLN
HKQSGTGGAG GAGGVGGIDI AKNNSITHTS NKKSHWGKR
//
