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Database: UniProt
Entry: A0A2G9I0V3_9LAMI
LinkDB: A0A2G9I0V3_9LAMI
Original site: A0A2G9I0V3_9LAMI 
ID   A0A2G9I0V3_9LAMI        Unreviewed;       882 AA.
AC   A0A2G9I0V3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000313|EMBL:PIN23230.1};
DE            EC=3.4.19.12 {ECO:0000313|EMBL:PIN23230.1};
GN   ORFNames=CDL12_04053 {ECO:0000313|EMBL:PIN23230.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN23230.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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:PIN23230.1}.
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DR   EMBL; NKXS01000601; PIN23230.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9I0V3; -.
DR   STRING; 429701.A0A2G9I0V3; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02661; Peptidase_C19E; 1.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR002893; Znf_MYND.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF685; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:PIN23230.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          76..113
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   DOMAIN          417..723
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          176..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..827
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   882 AA;  98894 MW;  91191E33CC2D055F CRC64;
     MLQPRETDIP ALFLVFVVLP LVSYFLLGKW SETARRKERI SLIADEAAEE SLLVNDMAVG
     SVMPVVHFPN SGIRQCARCF VPAATRCSQC KSVWYCSGRC QIVHWRHIHK LECQQLGKDC
     HRSSPKPIAN EGSSRRVLYA ETTEQCSYEY NVQQPSADIA SSLDAFSPPL TTVVSPTTSG
     VTLSKSGNFV TNQRSAETST LPKGNRDSSG RADRAVLRSS EELSGIGFTH PTFSQSLEEA
     DLRKGDFTAN IPSISENGDG DPRGRGTNAD ETQMDLIKGE YSSQKKIPCN DETKGSNCSS
     ERTSTKRSNK SRHNSRSHGV EQYKSPKSRV KVSKEPSSDT NVKVQAANES RLIAMTDAIP
     LQENNRVANL GMKKSVTIDC RQHSEDIANR QKKVKMIFPY EEFVKYFQFE VFNVTPRGLV
     NCGNSCYANA VLQCLTCTKP LIIYLLHRSH SRSGCSKDWC LMCELEQLVM MLRESGGPLS
     PINILMYIRS LNSQIGDGSQ EDAHEFLRLL VASMQSICLE GFGGENKVDP RLQDTTFIQH
     TFGGRLRSKV KCLRCNHESE RYENMMDLTL EIFGWVESLE DALTQFTSTE DLDGENMYRC
     TRCGAYVRAR KQLDIQDAPN ILTIVLKRFQ EGNYGKINKC ITFPEMLDMV PFMTGTDDIP
     PLYMLYAVVV HLDTSNASFS GHYISYVKDL QGNWFRVDDT EVRPVALSQV MSEGAYILFY
     MRSHPRPVKS CNGKATRART PSVPKHSSLK TQRSARPPQG KREPSSNHRP ETNADHPNIS
     RGIFIRENRS KPSTLNNYAE FSDTTSSDRS SLFTSSDDSS FTTESTRDSF SADIPFSSVF
     QSLYPVESTS RRTISCSVFP SSKPQTRFVC EEKGFVLLSD CR
//
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