ID R9ABM9_WALI9 Unreviewed; 1576 AA.
AC R9ABM9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase CYLD {ECO:0000256|ARBA:ARBA00018699};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme CYLD {ECO:0000256|ARBA:ARBA00030882};
DE AltName: Full=Ubiquitin thioesterase CYLD {ECO:0000256|ARBA:ARBA00031094};
DE AltName: Full=Ubiquitin-specific-processing protease CYLD {ECO:0000256|ARBA:ARBA00032487};
GN ORFNames=J056_001656 {ECO:0000313|EMBL:EOQ99571.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ99571.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}. Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KE007240; EOQ99571.1; -; Genomic_DNA.
DR RefSeq; XP_009269559.1; XM_009271284.1.
DR STRING; 1299270.R9ABM9; -.
DR GeneID; 20374608; -.
DR KEGG; wic:J056_001656; -.
DR eggNOG; KOG0944; Eukaryota.
DR eggNOG; KOG4568; Eukaryota.
DR HOGENOM; CLU_245302_0_0_1; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000014064; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd14297; UBA2_spUBP14_like; 2.
DR Gene3D; 1.10.287.1490; -; 2.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
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:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF00627; UBA; 3.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00165; UBA; 3.
DR SMART; SM00290; ZnF_UBP; 2.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS50030; UBA; 3.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:EOQ99571.1};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 30..75
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 912..1022
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 1064..1576
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 1331..1372
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1389..1433
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1456..1487
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 84..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 285..361
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 411..445
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 84..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 176791 MW; 9B5371A525AF85FB CRC64;
MSEPTQRHYK LNSLVKIDHL NLQGYLKFQG ETHFKQGHWL GLELLPVHHG KGKNDGSIEG
TRYFNCKQGN GIFIQLNKVT QVVQPSLRTP TKPRTSLSTP KPRQSINRLK SVDNMPPPSS
PPTLTRTRLN SMSNTSTPHR RSSSVTSMRT PSQQSIDRPS SRISQRTPSR QSISHRPSFS
RGLNPDDLIS DELSSLKEKH AAQLSQLSDL QSSHSNTSTQ LENTYSQLQD TSTQLHNAST
QLNDTSSHLQ DALAAIKFKE SQIKLSESEH AKLLSDLKYT HTQDIHTHQS RIAQLESEIA
QLNATLARTQ AEFQAEIRSK IAEIHSLETS LASLDARCVQ LTTEKEDLES LAEDLRHAGQ
ETIALYEERL NGTEARKFES DERIRVLESH CASLTAQSHP ASPGTTARRQ ITAAEIDNES
LKEQLAHLNT KLSSSEEAFN ELDRERENML LDTQKQIDKL HQDIRHLHAQ LTEGSRELEA
SQADCTSGTI RIQELEDALT STKELLEAAR AHAESLQSDI DNFENLKVDE DGNERVNELY
RRLETEQSQH AEQIDEIESE LNALNERLKD SENVINVSKR ECDFLRQENS RRGGIDREKV
KEEASLNEIS ILKNKVRQLE DQLEIEQERT RTHSHLTGDA GIVSPKEDMS SLQEQLKQSE
RRRKEVESKS HHDINELESL LEAKIFKEDD MERELVKLRA QLNIPERGTE ANDKEQWNGT
NTSKPSDNSN KENNSKNEDY EDPLIAEFMR DARRPSSNTS KVPSTPHRAE SALAAASGLS
DTSMKGNRGE YCDDCDSEKG VDVCLHCFNG ACESIHQHAY AHARSRHHPL ALNIKRSPKD
SDKAEPPLKK LAIEEQREEE QFSYAYNLRC LLCDVTYPTT SSSTIESQIL AVLASDSQAH
RSEVKAWEEE LSECSHSRSV RSTQPDKKLV KMTDAHCHAC SLNDNLWLCL TCGELGCGRA
QFGGLQGNSH ALSHYENSGH AVAVKLGTIT AEGTADIYCY ACNEERLNPN LADDLSTFGI
EITSQVKTTK SLTELQLEQN SKFDFSMTGD DGAELQPVFG KWLTGFKNLG NSCYMNSTLQ
SFFSYPAIRN HYLDRFNELN GGDVENAAQN LLVQLAKIAD GLGSGRYSTK SLKGQFQDGV
KPAMFKDLIG KGHPEFSTMR QQDSEEFLCH FLDVLKKSDT PSSIKRLFSF VAEQKLTCTA
CHKVRYRYDN HDSISVDIPV REHAQSDNGK VTYEDVSAEE CLDTLKRPDE LDYNCPSCKT
QVKATKTWNL ETFPDALILH TRKFHLVNWV PTKLDIAVQG VDKVDLTQLQ TEGRQEGEVD
LPEDEDGDEI QFDDEALSNL KGMGFSENRA KRSLINTDHT GVEAATAWLF AHMEDEGLDD
PVETKKPKKT TEDVPAELLN MVTDMGFTQN QARKALKNSQ NSVEMAVGWL FENPNDEGEE
APTADTNGGD DLNGVVTGMG FTPNQARKAL RVSSNNVEVA VGWLFDNPSD PGEEEVLNTP
MEEDDVKPGS KATPAQYALK AFISHKGPSV HSGHYVAHVK HDDEWILFND EKVVKESDTN
LNSLIGKGYV YFYEKI
//
