ID R9ZUL4_SHEEP Unreviewed; 357 AA.
AC R9ZUL4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE Flags: Fragment;
GN Name=USP44 {ECO:0000313|EMBL:AGO46302.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|EMBL:AGO46302.1};
RN [1] {ECO:0000313|EMBL:AGO46302.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RM1 {ECO:0000313|EMBL:AGO46302.1};
RX PubMed=24533078;
RA Periasamy K., Pichler R., Poli M., Cristel S., Cetra B., Medus D.,
RA Basar M., A K T., Ramasamy S., Ellahi M.B., Mohammed F., Teneva A.,
RA Shamsuddin M., Podesta M.G., Diallo A.;
RT "Candidate gene approach for parasite resistance in sheep - variation in
RT immune pathway genes and association with fecal egg count.";
RL PLoS ONE 9:E88337-E88337(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. USP44 subfamily.
CC {ECO:0000256|ARBA:ARBA00038113}.
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DR EMBL; KC734724; AGO46302.1; -; Genomic_DNA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF15; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 44; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 1..64
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 232..357
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGO46302.1"
FT NON_TER 357
FT /evidence="ECO:0000313|EMBL:AGO46302.1"
SQ SEQUENCE 357 AA; 40831 MW; 1C21C1B368961C50 CRC64;
WACLSCSHVA CGRSIEEHAL GHFQESSHPV ALEVNEMYVF CYLCDDYVLN DNATGDLKLL
RSTLSAIKNQ NYHCTTRSGK VLRSMATSDD SYFLHDGTQS LLQNEDQMYT ALWHRRRILM
GKIFRTWFEQ SPIGRKRQEQ FQEKLAKREV KKRRQELLEX QANAELESMP PRKSLRLQGL
AQSTTVEIVP VPLQTSALPA KDKVVSTSED VRLKKASDSS VKRRPTVTPG VTGLRNLGNT
CYMNSVLQVL SHLLIFRQCF LKLDLNRWLA VTAXDKTRSS YKHPPVTDTV YQMNECQEKE
PYSVRFRHPS LSSGLSGGAP QSRKMELIQP REPSSQYISL CHELHTLFQV MWSGKWA
//
