ID A0A091LW86_CARIC Unreviewed; 793 AA.
AC A0A091LW86;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE Flags: Fragment;
GN ORFNames=N322_02494 {ECO:0000313|EMBL:KFP63451.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP63451.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP63451.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP63451.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KK511994; KFP63451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LW86; -.
DR MEROPS; C19.019; -.
DR Proteomes; UP000054116; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006282; P:regulation of DNA repair; IEA:InterPro.
DR CDD; cd02671; Peptidase_C19O; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033815; USP1.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF905; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 1; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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, ECO:0000313|EMBL:KFP63451.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 82..793
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 793
FT /evidence="ECO:0000313|EMBL:KFP63451.1"
SQ SEQUENCE 793 AA; 88550 MW; 9D5E05667F352290 CRC64;
MPGVLPSDST GPARGSPSKK NRLSLKLFQK KEAKRALDFT ESQENEQKSS EFRGSEIDQV
VPAAQPPSLV SCEKKDNMLP FVGLNNLGNT CYLNSVLQVL YFCPGFKTGV KHLYNIISKK
KESLKDEGEQ KAEKGNCKED PLASYELICS LHSLILSVEQ LQASFLLNPE KYTDELATQP
RRLLNTLREL NPMYEGYLQH DAQEVLQCIL GNIQETCQLL KKEELNKLPV EEPTAKLEEK
LNQNTESNGT GNPAEEEDNL PSSHAGAIAE DKLPKGNGKR KSDAEGGNAK KKSKVSKEQI
AAEENQRQTR SKRKATGEKL ENQTDAIAKC SSENESAKPT QKKSRLRLNW LKSSCKQPSI
LSKFYSLGKL TTNLGSRDPG KEYGDCELEE SSVKCENGNN IKEEYHEPAS PVESHNEKGT
EKEPKKEGTE LAVFELVEKL FQGQLVLRTR CLECECFTER REDFQDISVP VQEDELSKTE
ESSEISPEPK TEMKTLKWAI SQFASVERIV GEDKYFCENC HHYTEAERSL LFDKMPEVIT
IHLKCFAASG LEFDCYGGLS KINTPLLTPL KLSLEEWSTK PTNDTYGLFA VVMHSGITIS
SGHYTASVKI TDLNSLELDR GNFITDQMYE TIKPEPLNEE EARTVAEDYD DGEVSFRVNG
NAQPGKVLNK KNMEAVGLLG GQKSKSDCDL YNKQPANPEK FLNVVTENRN PESSSSNGSA
ECSIGHSEQN GVASSGLENK ALYVLQSLKE YEGKWLLFDD SEVKVTEEKD FLNSLSPTSS
STSTPYLLFY KKI
//
