ID A0A151MJ60_ALLMI Unreviewed; 414 AA.
AC A0A151MJ60;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=OTUD3-1 {ECO:0000313|EMBL:KYO24546.1};
GN ORFNames=Y1Q_0023238 {ECO:0000313|EMBL:KYO24546.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO24546.1};
RN [1] {ECO:0000313|EMBL:KYO24546.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO24546.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO24546.1}.
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DR EMBL; AKHW03006061; KYO24546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151MJ60; -.
DR eggNOG; ENOG502QUTD; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd22770; OTU_OTUD3; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12419:SF7; OTU DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000050525}.
FT DOMAIN 12..136
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 227..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 47211 MW; 05AE1D2AB0FF03F1 CRC64;
MTVRFKLQAL GLRLREVPGD GNCLFRALGD QLEGHSRNHL KHRQETVDYM IKQREDFEPF
VEDDVPFEKH VSNLAKPGTF AGNDAIVAFA RNNQMNVVIH QLNAPLWQIR GTDESNVREL
HIAYRHGEHY DSVRRTNDNS EAPANLQTQM LCKNETNKKE KIEPKKDESE EEVEDEVEDA
IQKVRNATGC SDLHLISQIL EVENYNIDSA IFAILQVNEV KRINAEEQCG SQAKGQKPRS
SALWEENGSG SRIFGNQGLP PGGTENNKAQ VRPVEETRAS KNHFPKVSNK QRKEQQRLEK
KRRQEERHRQ KALTNKSNNA NNNRNETDSN TQEDSFKLRA LCRDHASIIK PNAKYLASQE
LSRTPAEGSL LFILIHVTPR LHQIPEVLAA FWKHAAGVLS HSQIIFSQLF QAEK
//
