ID G1KBF8_ANOCA Unreviewed; 686 AA.
AC G1KBF8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP49 {ECO:0000313|Ensembl:ENSACAP00000002939.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000002939.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000002939.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000002939.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000002939.3}
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|ARBA:ARBA00000707,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; G1KBF8; -.
DR STRING; 28377.ENSACAP00000002939; -.
DR MEROPS; C19.073; -.
DR Ensembl; ENSACAT00000003015.3; ENSACAP00000002939.3; ENSACAG00000002993.3.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00940000157997; -.
DR HOGENOM; CLU_008279_13_1_1; -.
DR InParanoid; G1KBF8; -.
DR TreeFam; TF315281; -.
DR Proteomes; UP000001646; Chromosome 4.
DR Bgee; ENSACAG00000002993; Expressed in forelimb bud and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0140936; F:histone H2B deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF7; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 49; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 2..99
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 260..655
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 310..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 166..195
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 686 AA; 79130 MW; EE645F2D47CE87C0 CRC64;
MDRCKHVGRL RLAQDHSILN PQKWHCMDCN TTESIWACLK CSHVACGRYI EDHALKHFEE
TRHPLAMEVN DFYVFCYLCE DYVLNDNPEG DLKLLRSSLS AIKSQKHDPS ARSGRTLRSM
ALGEDVCNHQ RAPQGRPQML TALWYRRQSL LAKALRTWFD KSSRGQQKLE QKRQMEELEI
KKEMARQRRQ EMKRRLLEEL ASTPPRKSAR LLSHIRRENL IPRKFRDMEA SSPTSRRVQS
SRFKQFYSIR RKPLMTPGVT GLKNLGNTCY MNSILQVLSH LQKFRECFLT LDLCETEELL
AKTVNGKSRM SGKLVSGLGP TESGRNDQLG SYGRQSLPAG LNGGSSISKS LELTQPKEPS
SKHISLCHEL HTLFRVMWSG KWASVSPFAM LHSVWSLIPE FLCELLDKVQ QELESEGTKR
RILIPFSQRK LTKQVLKVVN TIFHGQLLSQ VTCITCNYKS NTVEPFWDLS LEFPERYHSI
NKGIVPVNQT ECMLTEMLAK FTETEALEGR IYACDQCNSK RRKSSPKPLI LSEAKKQLMI
YRLPQVLRLH LKRFRWSGRN HREKIGVHVL FDQVLNMEPY CCRDTLSSLD KETFVYDLSA
VVMHHGKGFG SGHYTAYCYN TEGGFWVHCN DSKLNVCSVE EVCKTQAYIL FYTQRTVQGK
ASISETQLQA QVLSKHNDKD RRLTLP
//
