ID S4R6R4_PETMA Unreviewed; 958 AA.
AC S4R6R4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000000894.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000000894.1}
RP IDENTIFICATION.
RG Ensembl;
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; S4R6R4; -.
DR STRING; 7757.ENSPMAP00000000894; -.
DR MEROPS; C19.053; -.
DR Ensembl; ENSPMAT00000000898.1; ENSPMAP00000000894.1; ENSPMAG00000000806.1.
DR GeneTree; ENSGT00940000158091; -.
DR HOGENOM; CLU_012557_0_0_1; -.
DR OMA; CGEVVNK; -.
DR Proteomes; UP000245300; 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 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 Pfam; PF02809; UIM; 2.
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 Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000245300};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 338..945
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 104..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 107629 MW; 4977CF1075700ED4 CRC64;
SGEISVAGEI RIFTEQTGMT KWKDGVVEVV EKDTKSTLVI RFKAGGPTKT FTLTENVKSV
RVSDHKEHSR IMITLLDSSN ITVQYAMLGQ VQWLSQYLKD VEKNPNRGSS PLSGVLGKRT
SQRDSKRHFD TENRTPNKRP TAEGSAETPV KRTQGPPGRT PRVQHLSGSQ GNVQGSKGLP
SLSPNNTATS STARASLSEP RNDKRKRTLT PDEEITNDYP KENDSSSNSR PCGEQQAKRL
FPSHAKQEDV KGKGMFLGVM PLQTTTSFYG QTGTREYSSP SPLLNRSCLG SQFPAAKRSL
GLVTPHAATA CKKIKSTSDF VGWNKSKPFL STQQPQLQGF SNLGNTCYMN AILQSLFALH
SFTSDMLRQG IPWNRVPPNS LLRRLAHLLS KKDVCTMDYK KELLKRVKTA ISASAERFSG
YAQNDAHEFL SQCLDQLKED VERLNKKWRL EPGQGESPKP SQTDSASDMP YTCPVAANME
FEVLHTITCR VCGEVVKKKE QFNDLSIDLP RKKSDTAWSI QDSLDLFLRA EDVEYACEKC
ESRNATVTHK FIKLPRVLIL HLKRYSFDVQ LAVNNKVGQQ VIIPLYLTLQ AHCVEGTRSA
LSLRSSKHTH GNMQPLRSSQ SMNAPSTSSN RKRYTFKPRV LSISESDTDE DQLKRALNLS
KQVREARDNT QVNEDLLMQM CDQEPTNSSP DTGFCDEVDF PDVAEVQEVE SEPCSEVTAH
VEEPVYSSII VPTENWEEDD IPVWSKMDIG PKKEEDYAGK KEEGAEKNEQ KASGDEDKEN
RTPAEPEPDW MDQYSLDRER EERELQEALA QSLRDQEARE QREEDELKRA TELSLQEFQH
SLAEVMGSDE DSGNEGSVEL ERSEAEALEL KCNAETGDLP HSFQLLSVVS HIGSDSSAGH
YISDTFDVKK QSWFTYDDTD VTRTSEATVR DTRERSGYIF FYIHKEILEQ LLESDGTV
//
