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Database: UniProt
Entry: A0A087R9C0_APTFO
LinkDB: A0A087R9C0_APTFO
Original site: A0A087R9C0_APTFO 
ID   A0A087R9C0_APTFO        Unreviewed;      2552 AA.
AC   A0A087R9C0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=AS27_04935 {ECO:0000313|EMBL:KFM10074.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM10074.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM10074.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM10074.1};
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   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   EMBL; KL226222; KFM10074.1; -; Genomic_DNA.
DR   RefSeq; XP_009281310.1; XM_009283035.2.
DR   STRING; 9233.A0A087R9C0; -.
DR   MEROPS; C19.017; -.
DR   GeneID; 103902035; -.
DR   KEGG; afor:103902035; -.
DR   CTD; 8239; -.
DR   OrthoDB; 6206at2759; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR021905; DUF3517.
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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF827; UBIQUITINYL HYDROLASE 1; 1.
DR   Pfam; PF12030; DUF3517; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KFM10074.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT   DOMAIN          1557..1955
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1595..1619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2474..2552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..993
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1604..1619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2501..2515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2522..2552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2552 AA;  290232 MW;  D1658112C61ABCE3 CRC64;
     MTATTRGSPV GGNDSQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE QGQGDAPPQL
     EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA AIDLSKKSLD VKSEACQRFF
     RDGLTISFTK ILTDEAVSGW KFEIHRCIIN NTHRLVELCV AKLSQDWFPL LELLAMALNP
     HCKFHLYNGT RPSETVPAGV QLAEDELYAR PPDPRSPKGW LVDLINKFGT LNGFQILHDR
     FMSGSALNVQ IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DDELKKEAKN
     EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG KMNALNEVNK
     VISSVSYYTH RHGNPEEEEW LTAERMAEWI QQNNILSIVL RDSLHQPQYV EKLEKILRFV
     IKEKALTLQD LDNIWAAQAG KHEAIVKNVH DLLAKLAWDF SPEQLDHLFD CFKASWTNAS
     KKQREKLLEL IRRLAEDDKD GVMAHKVLNL LWNLAHSDDV PVDIMDQALS AHIKILDYSC
     SQDRDTQKIQ WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQT QRSPHVFYRH
     DLINQLQHNH ALVTLVAENL SAYMESMRQY AKEHGEYDPQ TVRPGSRYSH VQEVQERLNF
     LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW YSKLMGDEPD LDPDINKDFF
     ENNVLQLDPS LLTENGMKCF ERFFKAVNCR EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ
     GNDDIANRAI DLLKEIYTNL GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSI
     NCARQEAIRM VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHITLVV RFPNQGRQVE
     DLDIWSHTND TIGQVRRCIL NRIKANSAHT KVELFIGGEL VDPADDRKLI GQLNLKDKTL
     ITAKLTQINS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP EVESCLPGVI MSLHPRYISF
     LWQVADLGSS LNMPPLRDGA RVLMKLMPPD NTTVEKLRAI CLDHAKLGES SLSPSLDSLF
     FGPSASQVLY LTEVVYALLM PASAPLGEDA SDFQYNFLKS GGLPLVLSML TRNNFLPNAD
     METRRGAYLN ALKIAKLLLT AIGYGHVRAV AEACQPVVEG TSTISPINQA THDQAVVLQN
     ALQNIPNPTS ECMLRNVAIR LAQQISDEAS KYIPDICVIR AVQKIVWASG CGSVQLVFSS
     NEEISKIYEK TNAGNEPDME DEQVCCEALE VMTLCFALIP TALDALSKEK AWQTFIIDLL
     LHCHSKTVRQ MAQEQFFLMA TRCCMGQRPL LFFITLLFTV LGSTARERAK HSGDYFTLLR
     HLLNYAYNSN INVPNAEVLL NNEIDWLKRI RDEVKRTGET GVEETILEGH LGVTKELLAF
     QTPEKKYHIG CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCSSPATINA
     GFELLVALAV GCVRNLKQIV DTLTEMYYIG TAITTCEALT EWEYLPPVGP RPPKGFVGLK
     NAGATCYMNS VIQQLYMIPA IRNGILAIEG TGSDVDDDMS GDEKQDNESN VDPRDDVFGY
     PHQYEDKPAL SKTEDRKEYN IGVLRHLQVI FGHLAASRLQ YYVPRGFWKQ FRLWGEPVNL
     REQHDALEFF NSLVDSLDEA LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL
     NVDIRNHQNL LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF
     DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDDV NPENQIIQNE QSENEHSGST
     KYRLVGVLVH SGQASGGHYY SYIIQRNGGD GEKNRWYKFD DGDVTECKMD DDEEMKNQCF
     GGEYMGEVFD HMMKRMSYRR QKRWWNAYIL FYERMDTIDK DNELIKYISE LAITTKPHQI
     KMPSAIERSV RKQNVQFMHN RMQYSLEYFQ FIKKLLTCNS VYLNPPPGQD HLLPEAEEIT
     MISIQLAARF LFTTGFHTKK IVRGPASDWY DALCILLRHS KNVRFWFAHN VLFNVSNRFS
     EYLLECPSAE VRGAFAKLIV FIAHFSLQDG PCPSPFASPG PSSQAYDNLS LSDHLLRAVL
     NLLRREVSEH GRHLQQYFNL FVMYANLGVA EKTQLLKLNV PATFMLVALD EGPGPPIKYQ
     YAELGKLYTV VSQLIRCCNV SSRMQSSING NPPLANPYGD PNLSQPIMAL QQNVADILFV
     RTSYVKKIIE DCSNSEETIK LLRFCCWENP QFSSTVLSEL LWQVAYSYTY ELRPYLDLLL
     QILLIEDSWQ THRIHNALKG IPDDRDGLFD TIQRSKNHYQ KRAYQCIKCM VALFSNCPVA
     YQILQSNGDL KRKWTWAVEW LGDELERRPY TGNPQYTYNN WSPPIQSNET SNGYFLERSH
     SARMTLAKAC ELCPEEEPDD PDAPDEHESS PPEDAPLYPH SPGSQYQQNN HVHGQPYTGP
     AAHHMNNPQR TGQRAQENYE GSEEVSPPQT KD
//
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