ID A0A1R3GDY2_COCAP Unreviewed; 946 AA.
AC A0A1R3GDY2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase C19, ubiquitin carboxyl-terminal hydrolase 2 {ECO:0000313|EMBL:OMO56266.1};
GN ORFNames=CCACVL1_26680 {ECO:0000313|EMBL:OMO56266.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO56266.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO56266.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO56266.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:OMO56266.1}.
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DR EMBL; AWWV01014525; OMO56266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3GDY2; -.
DR STRING; 210143.A0A1R3GDY2; -.
DR EnsemblPlants; OMO56266; OMO56266; CCACVL1_26680.
DR Gramene; OMO56266; OMO56266; CCACVL1_26680.
DR OMA; GHGENDR; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
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:SF690; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 17; 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:OMO56266.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..105
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 432..735
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 118..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 104552 MW; BD81FD986CD276D2 CRC64;
MLVPGFLGLN GVVLVSLLVV FLVIRHMLRN AAARKEEVTR LIEMVSHETA VVEAQSTAEY
CYYPKYQCAV CFAPTTTRCS KCKSVRYCSG KCQIMHWRQG HKDECRPPAD FAVMKESGMH
SNDSEVESVF KTSSDTSSVV EEEDDDGNLK PHADTKRTRN GFVLSSSSSL AGVSPSTASH
ESFVDVSSSR TLLSGPNDKP GRELPNNLAT AIPRSKTATK KMEEAISPSS ESSLTYSVNN
PSKLNKKKSP HNDEEVELRM QFAKDNNLMS DDVHPAKVVC KKSTGVVSSE MLVTDASKKI
NLTPQGSSRP KTVTKDREAD LQHYESKQVR TSSCSASVDH SSSAAGGHSL PSSNLGLPAK
CNDSPTLPQT TSNGLKTSMR KVVQQLKASK QSKSSLFGFG NEVNGKHNYK IIFPYELFME
LYSYDALELC PFGLNNCGNS CYANAVLQCL AFTRPLTSYL VRGLHSRACR KKEWCFICEF
ECLILKAKEG ESPLSPIRIL SKIQKIGSHL GPGKEEDAHE FLRYAVDAMQ SVCLKEAKAA
GPLAEETTLV GLTFGGYLHS KIKCLKCLVK SERYERMMDL TVEIDGDIGS LEEALAQFTA
TEILDGENKY HCSRCKSYVK ARKKLTVLEA PNILTIVLKR FQSGNFGKLN KSVQFPEVLD
LAPYMSGTSD KAAVYNLYAV VVHLDVMNAA FSGHYVCYVK SSRGEWFRID DSTVIPVELE
RVLREGAYML LYARHTPKAP TLVRSNLESH GTRVKKRNLE AVPSSHNTSK TRSDSNFSRL
DSSISQRKHK YPSDVSNRKH LFDSEDWRFP SVQRIPPADS SSESSSIFSG SDASSCSTTS
TKDSSRSEDF SDYLFGEMGP EWYSRYGISS DSGAEINGHA RSMNRDGNST ILYTDSSRHR
RSSSSRASDF EQGGWSNLFD VRSSSISFGL MGKKAPELTP NRQISP
//
