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
//