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Database: UniProt
Entry: A0A1U7SSC1_ALLSI
LinkDB: A0A1U7SSC1_ALLSI
Original site: A0A1U7SSC1_ALLSI 
ID   A0A1U7SSC1_ALLSI        Unreviewed;       809 AA.
AC   A0A1U7SSC1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   31-JUL-2019, entry version 19.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
GN   Name=USP5 {ECO:0000313|RefSeq:XP_006037113.2};
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_006037113.2};
RN   [1] {ECO:0000313|RefSeq:XP_006037113.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-2019) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|PIRNR:PIRNR016308,
CC         ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025,
CC       ECO:0000256|SAAS:SAAS01045498}.
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DR   RefSeq; XP_006037113.2; XM_006037051.2.
DR   STRING; 38654.XP_006037113.1; -.
DR   GeneID; 102377231; -.
DR   KEGG; asn:102377231; -.
DR   CTD; 8078; -.
DR   KO; K11836; -.
DR   OrthoDB; 556111at2759; -.
DR   Proteomes; UP000189705; Genome assembly.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd14383; UBA1_UBP5; 1.
DR   Gene3D; 3.30.40.10; -; 3.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR041432; UBP13_Znf-UBP_var.
DR   InterPro; IPR041812; UBP5_UBA1.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   Pfam; PF17807; zf-UBP_var; 1.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000189705};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR016308-4};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01044238,
KW   ECO:0000313|RefSeq:XP_006037113.2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|PIRSR:PIRSR016308-3, ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|PIRSR:PIRSR016308-3,
KW   ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN      151    223       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      280    807       USP. {ECO:0000259|PROSITE:PS50235}.
FT   DOMAIN      605    646       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   DOMAIN      673    713       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   ZN_FING     151    223       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION      175    178       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR016308-2}.
FT   COILED      446    466       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    289    289       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   ACT_SITE    769    769       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   METAL       153    153       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       156    156       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       173    173       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       186    186       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   BINDING     163    163       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR016308-2}.
FT   BINDING     213    213       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR016308-2}.
FT   BINDING     215    215       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR016308-2}.
FT   BINDING     218    218       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR016308-2}.
FT   DISULFID    149    767       {ECO:0000256|PIRSR:PIRSR016308-4}.
SQ   SEQUENCE   809 AA;  90770 MW;  828BC25DAD77F339 CRC64;
     MNTFLGFGKQ YVEKHYQKTG QRVYLHLKRT RKLKEEDANS TAGDPPRKKP TRLAIGVEGG
     FDIPEEKFEY DEDVKIVIFP EHLDIPRDGL EGLPDMVRDR IASAVEAILT ADSASRKQEV
     QAWDGEVRRI SKHAFSLHQL QNDIRIPPCG WKCSKCDMRE NLWLNMTDGA ILCGRRYFDG
     SGGNNHAVEH YRETGYPLAV KLGTITPDGA DVYSYDEDDM VLDPNLAEHL AHFGIDMLKM
     QKTDKTMTEL EIDMNQRIGE WELIQESGVQ LKPLYGPGYT GIRNLGNSCY LNSVMQVLFS
     ISDFQRKYVD KLEKIFQNAP ADPTQDFSTQ VAKLGHGLLS GEYSKPASAD GEQPDQKGVQ
     NGIAPRMFKS LVGKGHPEFS TNRQQDAQEF FLHFINMVER NCRSSENPNE VFRFLVEEKL
     KCLATEKVKY TQRVDYIMQL PVPMDAALNK DELLEYEEKK RQAEEEKQPL PELVRAKVPF
     SSCLEAYGAP EQVDDFWSTA LQAKSVALKT TRFASFPDYL VIQIKKFTFG LDWVPKKLDV
     SIEMPEELDI SALQGTGLQD GEEEMPDIAP PLVTPDEPKG SLGFYGNEDD DSFCSPHFSS
     PTSPMLDESV IIQLVEMGFP MDACRKAVYY TGNSGVEAAM NWVMSHMDDP DFANPLVLPG
     SSGPGSTIIC PDPPSEDSVA TIVSMGFSRD QAMKALRATN NSLERAVDWI FSHIDDLDAE
     AAMDISEGRS AAESISESVP VGPKVRDGPG KYQLFAFVSH MGTSTMCGHY VCHIKKDGRW
     VIFNDQKVCA SEKPPKDLGY IYFYQRIPS
//
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