ID A0A094KLK2_ANTCR Unreviewed; 1090 AA.
AC A0A094KLK2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Ubiquitin carboxyl-terminal hydrolase 8 {ECO:0000313|EMBL:KFZ50255.1};
GN ORFNames=N321_09388 {ECO:0000313|EMBL:KFZ50255.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ50255.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ50255.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ50255.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL336588; KFZ50255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094KLK2; -.
DR Proteomes; UP000053620; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR048498; WW_USP8.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF27; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 8; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR Pfam; PF20625; WW_USP8; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KFZ50255.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053620}.
FT DOMAIN 199..317
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 749..1081
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 123..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 125360 MW; D1264EDE226255A2 CRC64;
MPAVASVPKE LYLCTSLKDL NKKTEIKPEK TSTKSYVQSA LKIFKAAEES RLDRDEEKAY
ILYMKYVTVY NFIKKRPDFK QQQDYFHSIL GPTNLKKAIE EAERLSDSLK LRYEEAEVRK
KLEERDRQEL QKKQEQKDDG KSSAKNSSES AADSKGKSQR VNGERKHSLE RKDQSDSLSA
FVFQGAVTAE KLFAMMSDKN IELIIMDARR LKDYQESCIP RSISVPEEAI SPGVTASWIE
ARLPEDSRDP WKRRGHFDYV ILLDWFSSAE DLKIGTTLQS LKDALFKWES KTILQNEPLI
LEGGYENWLL CFPQYTTNAK VTPPQHSRSE AVTVSLNFTY PSLEEPPPVP PVVAIKPSPT
EAIENEEMGD NLEERLKSLN RPSVQDAAVP KSDSSLVVNP ASITRSIPEV DRTKKPSLKI
PDENRPKSES TAGDSQPGES GRIVPDRSTK PLRDAKSILT EEEKNRVHAE TAALLEKNRR
EKELRERQQE EQKERLKREK EEQEQKAKEE QKEKEHKEKL QQSKEDREQK EREEQIKKEQ
EEKEQERARK EAIEAKKQNK NELETIGAKR IEIDKISVEE REKGTRTPEA QRRALGDTPQ
TFSQREPLIR ARSEEMGRII PGLPAGWAKF LDPITGTFRY YHSPTNTVHM YPPEMAPSST
PPSTPPTHKP KPQVTVERER EHSKLKRSYS SPDITQAIQE EEKKRIPVTP AVNRDNKPVC
YTKAEISRLS ASQIRNLNPV FGGSGPALTG LRNLGNTCYM NSILQCLCNA PHLADYFNRN
LYQDDINRSN FLGHKGEVAE EFGVIMKALW TGQYKYISPR DFKITIGKIN DQFAGYSQQD
SQELLLFLMD GLHEDLNKAD NRKRYKEENN DHLDDLRAAE LAWHKHKQLN ESIIVALFQG
QFKSTVQCLT CLKKSRTFEA FMYLSLPLAS TSKCTLQQCL RLFSKEEKLT DNNRFYCSHC
KTRKDSLKKI EIWKLPPVLL VHLKRFSYDG RWKQKLQTSV DFPLETLDLS QYVIGPKNNL
KRYNLFSVSN HYGGLDGGHY TAYCKNASKQ RWFKFDDHEV SEISASSVKS SAAYILFYTS
YEQRAVDMAT
//
