ID A0A091LR78_9GRUI Unreviewed; 687 AA.
AC A0A091LR78;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase BAP1 {ECO:0000256|ARBA:ARBA00039967};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=BRCA1-associated protein 1 {ECO:0000256|ARBA:ARBA00042257};
DE Flags: Fragment;
GN ORFNames=N324_12630 {ECO:0000313|EMBL:KFP45286.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP45286.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP45286.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP45286.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007182}.
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DR EMBL; KK762192; KFP45286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LR78; -.
DR Proteomes; UP000053330; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR Gene3D; 1.20.58.860; -; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE BAP1; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFP45286.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053330};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 2..202
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT DOMAIN 601..646
FT /note="Peptidase C12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18031"
FT REGION 260..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..687
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP45286.1"
FT NON_TER 687
FT /evidence="ECO:0000313|EMBL:KFP45286.1"
SQ SEQUENCE 687 AA; 76242 MW; 473F3871B532D38C CRC64;
GLFTLLVEDF GVKGVQVEEI YDLQSKCQGP VYGFIFLFKW IEERRSRRKV STLVDETSVI
DDDIVNNMFF AHQLIPNSCA THALLSVLLN CNNVDLGPTL SRMKDFTKGF SPESKGYAIG
NAPELAKAHN SHARPEPRHL PEKQNGISAV RTMEAFHFVS YVPIKGRLFE LDGLKVYPID
HGPWADDEEW TDKARRVIME RIGLATAGEP YHDIRFNLMA VVPDRRMKYE SKLHILKMNR
QTVLEALQQL IRVTQPELIQ TQKSQESQPP EEAKPASSKT VTPESTHPDG TDEPASQGHP
AATQSPPSKS KPVAKTSAST INGAPPANPN PIVQRLPAFL DNHNYAKSPM QEEEDLAAGV
GRSRVPVRQH QQYSDDEDDY DDDEEEEVCN TNSAIRYKRK GQVKQEHVAG AADGQLSVLQ
PNTINVLAEK LKESQKDLSI PLSVKTSGGG AAVAVVTHSQ PSPTPSNEST DTASEIGSAF
NSPLRSPIRS ANPTRPSSPV TSHISKVLFG EEDGLLRVDC MRYNRAVRDL GPVISTGLLH
LTEDSVFCPL AVADGGKSSP PSIKPGEEAP VAIKLDEEGS EASDSKEKEL LALLKCVEAE
IANYEACLKE EVEKRKKFKI DDQRRTHNYD EFICTFISML AQEGMLASLV EQNISVRRRQ
GVSIGRLHKQ RKPDRRKRSR PYKAKRQ
//
