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Database: UniProt
Entry: A0A091TXR2_PHALP
LinkDB: A0A091TXR2_PHALP
Original site: A0A091TXR2_PHALP 
ID   A0A091TXR2_PHALP        Unreviewed;      1036 AA.
AC   A0A091TXR2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   Flags: Fragment;
GN   ORFNames=N335_05945 {ECO:0000313|EMBL:KFQ83199.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC   Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ83199.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ83199.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ83199.1};
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|ARBA:ARBA00000707};
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DR   EMBL; KK468345; KFQ83199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091TXR2; -.
DR   PhylomeDB; A0A091TXR2; -.
DR   Proteomes; UP000053638; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02665; Peptidase_C19I; 1.
DR   CDD; cd14355; UBA_UBP28; 1.
DR   CDD; cd20487; USP28_C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:KFQ83199.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053638}.
FT   DOMAIN          146..636
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          95..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          389..416
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        97..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ83199.1"
FT   NON_TER         1036
FT                   /evidence="ECO:0000313|EMBL:KFQ83199.1"
SQ   SEQUENCE   1036 AA;  117928 MW;  B765A0D302B8A220 CRC64;
     DCQMLLNQLK EITGIQDSAF LQAALKAANG DLMEAVTFLT EEHAHEPTQD AAAAEPSAWE
     GSAVGKQLPQ NVATALIPNN RDDLPAADAF RPLESPKAQA ADRDAAERPQ DAHSAENKNR
     SKRKRCEVWG ENPKQNDWRR VGDWPVGMKN IGNTCWFSAV IQSLFQLPEF RRLVLGYSLP
     QNVLESCRSR AGKRNIAFMQ ELQCLFALML GTRRKFVDPS AALELLRDAF RSAEEQQQDV
     SEFTHKLLDW LEDAFQLAVN LKSPGDKSEN PMVQLFYGTF LTEGVHEGNT FSKIETFGQY
     PLQVNGYRNL NECLEGAMVE GEMDQATASQ SVKYGQERWF TKLPPVLTFE LSRFEFNQSL
     GQPEKIHTKL EFPQTIYMDR YLYCSKELIQ MKREEMKRLK EKMVILQQKL ERYMKYGSGP
     ARFPLPDMLQ YVLEFIATKP AAVVPSAQGS RTTLLQPQAE PHVLDVLAQP DGVLERKGSR
     TEDAAFFLAN PSPQQKSRTP LQPSGSLAEM SECPAPHVVS KEELNLVRTC LQRWRNEIEQ
     DMRDLKESIA SINLSIEQMY CDPLLQQVPY RLHAVLVHEG QANAGHYWAY IYDQPRKSWL
     KYNDISVTES SWEELERDSF GGLKNASAYC LMYISDKVSR FVADKDDGSE VGQFQKEVEA
     LSPELRHYIQ EDNWRLEQEA EEWEEEQSCK IPQMEPSAAS ESQDLSSESG PDQASVCEQS
     VRSLSSEHAM IAKEQTAKAI ANTADAYEKN GVEAALCEAF HEEYSRLYLL AKETPTPQND
     ARLQHVLVYF LQNNAPQQVV ERTLLEQFAD KNLSYDERSI SIMKVARAKL REIGPDDVDM
     EEYKRWHEDY SLFRKVSVYL LTGLELYQNG KYQESLTYLV YAYQSNTKLL MKGTSRGVNE
     SLIALYRRKC LLKLNEVAAS LFVSCEEARV AEGISILNEL IIPCMHLMNN FEISKEDLDA
     IEVMRNRWCS YLGREDMDAE LQMKLGELLP RLLDCSTEVI VLKEPPKIRP NSPYDLCSRF
     AAVMESIHGA STVTVK
//
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