ID A0A3B4A946_9GOBI Unreviewed; 672 AA.
AC A0A3B4A946;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 37 {ECO:0000256|ARBA:ARBA00014563};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme 37 {ECO:0000256|ARBA:ARBA00030260};
DE AltName: Full=Ubiquitin thioesterase 37 {ECO:0000256|ARBA:ARBA00029923};
DE AltName: Full=Ubiquitin-specific-processing protease 37 {ECO:0000256|ARBA:ARBA00032476};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000013159.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000013159.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B4A946; -.
DR STRING; 409849.ENSPMGP00000013159; -.
DR Ensembl; ENSPMGT00000014040.1; ENSPMGP00000013159.1; ENSPMGG00000010847.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd02257; Peptidase_C19; 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; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF733; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE-RELATED; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776}.
FT DOMAIN 222..672
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 111..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 76590 MW; 7EB61B5FFAFF9878 CRC64;
MTSLATKLSS GSAVKIRVNS LDLGTTKWKE GTFEIQEKDN KASLCLRFNC GGAARTFQLS
QNVKKVAPLA NKITLTLKDN SVIFLDKLPV TLAQKTKDYL EKLRSEKRKR LMNSESDLTE
DYPKENDSSS NNKATSDPAR KFLQSCKDKL KQQEENRNSG KRRSLYAFVS RPSSTAQSSS
AKRSLLLPNH STPFKKVRPS LDYGGWNKQR PTALAQPQPP LQGFSNLGNT CYMNAILQSL
FSLPSFSNDM LKQSIPWKKV PINALLRRFA HLMAKKDVGC PETKKDLLRK VKSAISSTAE
RFSGNMQNDA HEFLSQCMDQ LKDDVEKMNK TRAEPGEEAD TSRIYTCPVA VNMEFEVQHT
ITCKCCGEVV TKREVFNDLS IDLPRRKKTL PLRSIQDSLD LFFRMEEIEY SCEKCNGKAA
TVTHKFSKLP RVLILHLKRY SFNAQLSLNS KLGQQVVIPR FLTLSSHCTE STRAPVSLSW
TTARVGGRAT GSSLLLDSDG EEELNRKVTL SRKRRLSSCL TEESEERLLL LFLDVLDSLD
LTMDENKENQ TPEAQEIDWV QQYSLEQERE EQELQQALAQ SLQEHVRRKL QIYRHESDHR
PVWKHGQSGA MDQSVNVFSH CESTGGHYIS DVYDMKKQSW LTYNDLDVSR TQEGAVQRDR
DRSGYIFFYM HK
//
