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Database: UniProt
Entry: A0A061EJG7_THECC
LinkDB: A0A061EJG7_THECC
Original site: A0A061EJG7_THECC 
ID   A0A061EJG7_THECC        Unreviewed;      1659 AA.
AC   A0A061EJG7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Ubiquitin-like protease family profile domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TCM_019956 {ECO:0000313|EMBL:EOY04778.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY04778.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY04778.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the GRAS family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01191}.
CC   -!- SIMILARITY: Belongs to the peptidase C48 family.
CC       {ECO:0000256|ARBA:ARBA00005234}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01191}.
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DR   EMBL; CM001882; EOY04778.1; -; Genomic_DNA.
DR   EnsemblPlants; EOY04778; EOY04778; TCM_019956.
DR   Gramene; EOY04778; EOY04778; TCM_019956.
DR   eggNOG; KOG0778; Eukaryota.
DR   eggNOG; KOG1121; Eukaryota.
DR   HOGENOM; CLU_242206_0_0_1; -.
DR   InParanoid; A0A061EJG7; -.
DR   OMA; FAEIYDM; -.
DR   Proteomes; UP000026915; Chromosome 4.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR045259; DAYSLEEPER-like.
DR   InterPro; IPR025525; hAT-like_transposase_RNase-H.
DR   InterPro; IPR008906; HATC_C_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003653; Peptidase_C48_C.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR005202; TF_GRAS.
DR   InterPro; IPR003656; Znf_BED.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR23272; BED FINGER-RELATED; 1.
DR   PANTHER; PTHR23272:SF132; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN RICESLEEPER 1-LIKE ISOFORM X1; 1.
DR   Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR   Pfam; PF03514; GRAS; 1.
DR   Pfam; PF14372; hAT-like_RNase-H; 1.
DR   Pfam; PF02902; Peptidase_C48; 1.
DR   Pfam; PF02892; zf-BED; 1.
DR   SMART; SM00614; ZnF_BED; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50985; GRAS; 1.
DR   PROSITE; PS50600; ULP_PROTEASE; 1.
DR   PROSITE; PS50808; ZF_BED; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT   DOMAIN          696..750
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          1443..1627
FT                   /note="Ubiquitin-like protease family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50600"
FT   REGION          270..362
FT                   /note="SAW"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01191"
FT   REGION          1349..1408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           200..204
FT                   /note="LXXLL motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01191"
FT   COMPBIAS        1349..1365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1376..1395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1659 AA;  191184 MW;  3B20A6BEE4F51011 CRC64;
     MSSSALDALV ACAKAIQDEN LTVADSLLER IWNLAAAQSW PGESDVVKYF AEALVRRAYG
     ISSASANFNL LSPPPIYFLD NFSCDAINTA CMGKKRFHLI TFLFLPSDDW TYLFRSLANA
     SGNFLSVRVS VIVSPFLEKI VKIQQEKSKH DLTTAAMERG IKLEDLRVVY ANSLGDVDAS
     KADFTRTTDE AVIVYYRYKL HELLADVRVM ERELLKLRQI NPEIVIIEEQ YADHNDSNFI
     KRLEKSFQYY FNRFDFYEVT YCRQIVNIVG CEGTDRLERH QTLAQWRSLL RANGLLPVPL
     APDIWSGEHE DNGCVVFQND DGLLHFTSAW KLTDAVDHFN PISYNPIQGF NPNPALEDTV
     RTLQVDRQAS SLNGLAAFAE IYDMLEDVCL KYELPLALTW VKGTPNGIMS GLNKKRSLSI
     ETAYSYINCC YYYYYDYYVE KISQYRSFMQ ECAIYDIQEG QAIAGQALQS NEPFLFEPNI
     TELRSNPFAE AAQKSGLHAA LAICLVNHYT DDVYILEFFL SSSEEKLEEP KSLALRIFED
     LKKMKTKFVK LRVHGTEVGL QEEAIPNIPW EEMPMRSSSP ATSNDQFLNS NASRSLNVVE
     LKDRHVVEIQ GPNGQEAATS NFHPAYLSIH ASSMAGTEHF NATNLRSYNG LLETHEPQLQ
     EITEKNWISQ TISNIDHEIV KANRENSALP RTKQRKLVSK VWKEFTKFEE NGKQLAKCNH
     CSKEFTGSSK SGTTHLKNHL ERCPRKKNEY QERQLKLSVK TGDLTNRDTS EGNSMFDQEK
     SRLDLVKMII KHQYPLDVAE QEFFKSFVQN LQPMFEFQSQ ATIISDIHHI YEEEKKKLQQ
     CFAQFACKFS LTISLWKDNL RKNAYCCLIA HFVDDDWELR RKILVFKNLE HNYGTGSIIR
     VIQNSISEWN MSEKVCSISV DNSSLNNGIL QQIKESCLSD QVSLPSCHYY SSCTLIQDGL
     HEIDDILLKL RKSIEYVTEL EHGKLKFQEA INQVTLQGGK STDYGPLRLD SNFSILDSAL
     ESRQIFCQLE QIDGHFKVNP SIEEWERALI LHSYLKGFYD NLSSFRQTHS STANTYFPQL
     CDMYKKFLQM EKKNYPFMMK RKFDDHWSLC NLVFAIAALL DPRLKFKFVE FSYGEIYGRD
     SKRQLKRFHR DLMDIYFEYA YEPRNRTTSA SVGCLTRQST ESANDSILDS FSRYASASNF
     NEVSSRKSDL DCYLEEPLLH LDGAFFDVLD WWRVNSERFP TLGRMAHDLL AMPVLVVPPC
     SDFSAVITNP AHNGLNPETM EALVCSHNWL EMPKGNDRAN HAPMQNTAKR KWEEKETREV
     KSCKNWNSEE TNNADKAKAS YKMLTRALPL ENDRQEGRPL KSSEPNHGKD TSGLIEIPNG
     SPSFDNQSEF QCYSSDESDG EIAGREQGEW REDDVRRYLL LPLTEKGRKR LNKWRNHKMS
     GKLIGRDKEF GVLDYKLAPL LTVPHGVETQ VKYYIDDSVV NTFFKLLKKR SDRFPKAYVS
     HYSFDSWIAT YLIEGSRSES QVFSWFKDEK LKDVQILFLP ACLSAHWVLF CVDTKKRTFS
     WLDSNISSRT SNVAEKQAIL GWFKRLLLPA FGYQNANEWP FEIRSDIPEQ KNGVDCGLFV
     MKYADCLTHG EFFPFTQQHM PYFRLRTFLD IYRGRLHSQ
//
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