ID A0A1U7SIU1_ALLSI Unreviewed; 992 AA.
AC A0A1U7SIU1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP37 {ECO:0000313|RefSeq:XP_006036518.1,
GN ECO:0000313|RefSeq:XP_025048528.1};
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|RefSeq:XP_006036518.1};
RN [1] {ECO:0000313|RefSeq:XP_006036518.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-2022) 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,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_006036518.1; XM_006036456.3.
DR RefSeq; XP_025048528.1; XM_025192743.1.
DR STRING; 38654.A0A1U7SIU1; -.
DR GeneID; 102386300; -.
DR KEGG; asn:102386300; -.
DR CTD; 57695; -.
DR eggNOG; KOG1868; Eukaryota.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02257; Peptidase_C19; 2.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 2.30.29.180; Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00726; UIM; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|RuleBase:RU366025,
KW ECO:0000313|RefSeq:XP_006036518.1};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 344..964
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 132..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 110959 MW; AFB547E287D74BD4 CRC64;
MAPLKVHGPV RMRSMQTGIT KWKEGSFEIV EKDNKVSLVV HYNVGGIPKT FQLSHNIKTV
VLRQNGGKLC CLMLTLKDAS FLTIDKVPSK DANEMRMYLD AILQDRVHGA VRPSQGSGSF
GGVLGNRAKQ KEMNRQFPYI ENQTPSKRVT VESKDENSFR KMLGTSGSRA SVKSSLGSAA
PSNRVNIPAS PTSSTPHRTG LLENREKRKR AQPSGSEMNE DYPKENDSST NNKAMTDPAW
KFLSSSREKQ LSLKQAEENR ASGVLPLQSS SFYGSRSSSK DYSTSNSNLD RSSMSSQAPS
AKRSLGFLSQ PAPLSVKKMR SNQDYTGWNK LRVPLSTHPQ QQLQGFSNLG NTCYMNAILQ
SLFSIQSFAN DLLKQGIPWK KIPLNALIRR FAHLLAKKDV CSPEVKKELL KKVKSAISAT
AERFSGYMQN DAHEFLSQCL DQLKEDMEKL NKTWKSEPAL SEDNSPGRAS DALSATKVYT
CPVIANLEFE VQHSIICKVC GETVTKREQF NDLSIDLPRR KKLLPSRSIQ DSLDLFFRAE
EIEYSCEKCN GKSAIVAHKF NRLPRVLILH LKRYSFNVAL SLNHKVGQQV VIPRYLTLLS
HCTEGTRPPL TLGWSAHSAI SRPLKASQMV NSCTMISTST PCRKYTFKSK SSALLCMDSD
SDDEPLKRSV AHSQRLCDVP IRELPQQQQP PPEDPEKGSK RNKAECDKSA DLGSAGFDGM
SEDELLAAVL EISKREASLT LSHDEDKPTS SPDTGFGEDE VQELPENLES VEAEKPKAAT
ESGPANFTKD FDENKENKTP EGSQGEVDWL QQYDMERERE EQELQQALAQ SLQEQEAREQ
KEDDDLKRAT ELSLQEFNSS LLDSVGSDED SGNEDVLDME YSDAEAEELK RNAENGELPH
SYRLISVVSH IGNTSSSGHY ISDVFDIKKQ SWFTYNDLEV SRTQEGTVQC DRDRSGYIFF
YMHKDIFEEL LEAEKNAQPL STEAGRSVRQ PL
//
