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Database: UniProt
Entry: A0A1U8DK66_ALLSI
LinkDB: A0A1U8DK66_ALLSI
Original site: A0A1U8DK66_ALLSI 
ID   A0A1U8DK66_ALLSI        Unreviewed;      1675 AA.
AC   A0A1U8DK66;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 2.
DT   27-MAR-2024, 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=USP32 {ECO:0000313|RefSeq:XP_014378124.2};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014378124.2};
RN   [1] {ECO:0000313|RefSeq:XP_014378124.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_014378124.2; XM_014522638.2.
DR   STRING; 38654.A0A1U8DK66; -.
DR   KEGG; asn:102384323; -.
DR   eggNOG; KOG0044; Eukaryota.
DR   eggNOG; KOG1870; Eukaryota.
DR   InParanoid; A0A1U8DK66; -.
DR   OrthoDB; 5474185at2759; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 3.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028135; Ub_USP-typ.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF13202; EF-hand_5; 2.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00695; DUSP; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000313|RefSeq:XP_014378124.2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705}.
FT   DOMAIN          280..315
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          316..351
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          421..637
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          800..1638
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1410..1514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1426..1469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1491..1505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1675 AA;  189833 MW;  1D0F30FF45C40B3A CRC64;
     MTTITGAISV ASVPRVRVQP AFLQERVIRS GKRRFRAMKT PFLRIILGWC NHSGSSRLRI
     MSLAYTRSKF ALTDVELKRL KDAFKRTCGL SCYMSQQCFI REVLGDGVPP KVAEVIYCSF
     GGTAKGLHFN NLIVGLVLLT RGKEEEKAKY IFSLFSNESG SYVVREEMER MLHVVDGKVP
     DTLKKCFSEG EKVNYEKFKN WLLHNKDAFT FSRWLLSGGV YVTLTDDSDT PTFYQTLAGV
     THLEESDIID LEKRYWLLKA QSRTGRFDLE TFGPLVSPPI HPSLSEGLFN AFDENRDNHI
     DFKEISCGLS ACCRGPLAER QKFCFKVFDV DRDGVLSRTE LKEMVVALLE VWKDNRTDKI
     PELDKDLSEI VEDILNAHDT TKIGHLTLED YQIWSVKSAL ANEFLNLLFQ VCHIVLGLRP
     ATPEEEGQII RGWLERESRY GLQPGHNWFL IAVSWWQQWK EYVKYDANLV MIESSFVLNG
     GKNAVIAAST HASEQGEEKM GGLNYFSATE EKISDNISTA SEASETTSSN TLYSIAPGTD
     MCFARQHNTS DNNNQCLLVS NGNTLLQLNP QKPGAIDNQP LVTQEPVKAA SLTMEGGRLK
     QSPHLVEGRD YIMVPEPVWR ALYHWYGANL SLPRPVIKNS KTNMPELELF PCYLLFLRQQ
     PATRTQQSNI WVNMGMMSLR VFPQHLPRGN VPSPNAPLKR VLAYTGCFSR MQTIKEIHEY
     LSQRLRIKEE DMRLWIYYSE NHLSLLDDED HRLEYLKIKD EQHLVIEVRN KDMSWPEEMS
     FIANSSKIDR HKVPTEKGAT GLSNLGNTCF MNSSIQCVSN TQPLTQYFIS GRHLYELNRT
     NPIGMKGHMA KCYGDLVQEL WSGTQKNIAP LKLRWTIAKY APRFNGFQQQ DSQELLAFLL
     DGLHEDLNRV HDKPYVELKD SDGRPDWEVA AEAWENHLRR NRSIVVDLFH GQLKSQVKCK
     TCGHISVRFD PFNFLSLPLP MDSYMHLEIT VIKLDGTTPV RYGLRLNMDE KYTGLKKQLS
     ELCGLKPEQI LLAEVHGSNI KNFPQDNQKV RLSVSGFLCA FEIPVPGSPT SASSPVQTDF
     STGPSTNGML NIMMNGDLPR PTLIPNGMPN TVVPCGTENN LANWTLNGHV SLLPDSPFIG
     YIIAVHRKMM RTELYFLSSQ KNRPSLFGMP LIVPCTVHTR KKDLYDAVWI QVSRLASPLP
     PQEASNHAQD CDDSMGYQYP FTLRVVQKDG NSCAWCPWYR FCRGCKIECT EDRACVGNAY
     IAVDWDPTAL HLRYQTSQER IVEEHESVEQ SRRAQAEPIN LDSCLRAFTS EEELGEDEMY
     YCSKCKTHCL ATKKLDLWRL PPILIIHLKR FQFVNGRWIK SQKIVKFPRE NFDPSAFLVQ
     KDPSLCQRKQ LTPQVDDLCE PRILQGESRK ADLQNTCPAG EGDVLNRSPS SLNTTSILNN
     IKASPSPGRR SGTSCPSSKT SSPNSSPRTL GRGKGRLRLP QLGKNKLSSS KENLDASKDN
     GTDPEQKFTS DQGDAFSRGH ILGGSQNELF AAQDNEVTVA NGYFCEQNAY SNGSINGQMD
     NHSEEDITDD QREEVGVNPI YNLYAISCHS GIMGGGHYVT YAKNPNNKWY CYNDSSCKEL
     HPDEIDTDSA YILFYEQQGV DYAQFLPKID GKKMADTSSM DEDFESDYKK YCVLQ
//
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