ID A0A0V0WVL9_9BILA Unreviewed; 1061 AA.
AC A0A0V0WVL9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=cps-6 {ECO:0000313|EMBL:KRX79721.1};
GN ORFNames=T06_4850 {ECO:0000313|EMBL:KRX79721.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX79721.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX79721.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX79721.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {ECO:0000256|ARBA:ARBA00010052}.
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:KRX79721.1}.
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DR EMBL; JYDK01000049; KRX79721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WVL9; -.
DR STRING; 92179.A0A0V0WVL9; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018524; DNA/RNA_endonuclease_AS.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR040255; Non-specific_endonuclease.
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; PTHR13966:SF5; ENDONUCLEASE G, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13966; ENDONUCLEASE RELATED; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:KRX79721.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:KRX79721.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR640255-2}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 50..154
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 196..754
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 423..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..443
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 908
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-1"
FT BINDING 940
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-2"
SQ SEQUENCE 1061 AA; 121290 MW; F58C73F6E311C719 CRC64;
MEKISKKYEE VYNKYFSGSK NGFSENEGKL AAERDVILCP HIYSSLNLSP IQKHLQSSPL
FQCHICAQEQ CRRAGTTENI QSEFLLCLGC GYQFCTDRSF HHALRHFQKA ESHCLTLSLT
TLEILCFRCG KFVDTGQSSQ LIEVRSLVEK CKKAESSSEN SSSHLEKYFA VEERNSNITF
SKRKMAKNSG ISLPVSGLIN FGNTCYFNAV LQVLMRTKSF CLLLAKCMSD ENSQLLDPES
VWQYLSFYFK WDDMQPFHPV QVFMDWKSRT LCKAFLELKN ASTLTRNHVL DPSNILHVLT
NKAIQFRGNQ QHDSHELLRY FLDELRDEEL VCMKDGIKQC CELTEDEEGK EKLKAYMLCC
KTTAVDQVFG GQLLQSIRCL TCNHRSYKLD PFLDLSLALQ NDDCDDNDFQ ACNTAKTVPM
SKHRMKKLKR QKKKEKRGKI RRQRVSSGTG EQQFLKDSVK NDQMNTVNNV NGDVSSLCED
MNDLTVEDKE NCNDDDSGSF YLESDDGGDS SQFESDDYDE LMEKLQPGPK HPVMRSSLKS
VDACLNNFMI EELLTGSSKF ACDNCAEISG DKDETKLSDA KKSSLIFSPP AVLTLHLKRF
ENNGKTNRKI YGHVVFSTEL DMSRFCCRKG RRIFDSRVLY SLYGVICHSG SMYGGHYIAY
VKVEDRDDAS WKRFLEKVSQ VETIIFDPDD VGWQTKQRRR KTPSGSGNHK RSVSDGRRLS
RAPTWYMLND NITSKVPESA VLKAEAYMLF YEPCIASGAS CAAIAGCFGF WLGNKQENKN
TRVFPYLVAS AASAIDARLP DVVPLIQAPA KPDSVAEKVD IPSRVSEIMR FGFPGFDNLR
TFEDFVVSYD RKTRTVHWVL EHLTPDRMTY DPSVDRSKCM FREDESIHSY FRSTNEDYKA
RSGYDRGHMA AAGNHRRTQN AIDQTFLLSN MAPQVGKGFN RDKWNELEKH VRRMARKNKN
VYICTGPLYL PKRDLDGKMR VTYEVIGKQH VAVPTHFFKV ILVENPESRY FIECYVMPNQ
SIDDSIPLNK FYAPLESVER SAGFFIFSNM PRNKLISING K
//
