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Database: UniProt
Entry: A0A150G0E5_GONPE
LinkDB: A0A150G0E5_GONPE
Original site: A0A150G0E5_GONPE 
ID   A0A150G0E5_GONPE        Unreviewed;       874 AA.
AC   A0A150G0E5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=CRAL-TRIO domain-containing protein {ECO:0000259|PROSITE:PS50191};
GN   ORFNames=GPECTOR_94g636 {ECO:0000313|EMBL:KXZ43314.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ43314.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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:KXZ43314.1}.
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DR   EMBL; LSYV01000095; KXZ43314.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150G0E5; -.
DR   STRING; 33097.A0A150G0E5; -.
DR   OrthoDB; 5472443at2759; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   PANTHER; PTHR12411:SF929; CATHEPSIN Z; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT   DOMAIN          557..707
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          287..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..559
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..742
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..830
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  89447 MW;  146D2EC78A94C3D8 CRC64;
     MNIKQRGSWP GVYLSVQNII DCGEAGSCNG GDDRMVYAYA AKYGIPPDTC NLYVAENQKC
     HDKEQCYTCW PDEGCKPVYD YNRLTVSEHG KLKGIHQMKA ELFQRGPISC GIDATDNMDS
     YTGGVYAEYK ERIGINHVVS VVGWGVEDGD EYWIIRNSWG EPWGEAGFMK LVTSNYKDGE
     GELYNLGIET ECSFGVPDRW VPAKELGFGP DSDEYDGVVT LPSSGKAKAV SNRKILPGMT
     LKKVDEHELG GTPTTSAEQL LEDYRTAAAA GLVSPELASI LGLAPPPAHS SGFGSREVAL
     PDAGENPDGE GGSEEDFSEA TVATVEEPPV SASQSAAVQP DADNEDEEEE LEEGRVAFGT
     VESSDIVLDL IVGGATGAGA AVGATALASS TVEDPRATTG APEAATGLSL QAASGAGDAA
     QSAGAAPASR GHDPFYAGDS DDDEGFVVEP LRDPAPRVSH DYDPAAASGG ALLPSPAAAA
     GGQWPPQPRL QQGSAGAPLG AGAAAAAVAV GAGVAALAAG AVSMGQRPPM APPGPRPPMG
     PLGPGAPPGP PPPPSPYPGL LYTEGRDTLG RPVVVLNTAM LPAKAKKNDV LQYVLQQLQP
     MVQRDYVLVV LSLAMGVKAS SVSTTWALGA YRSLAKPYRK HVKHIILVQP SAWARALLAL
     AQPFVSKKAA HKVKKVDNLV QVAEATGGEV RLESLGARFI REIQYGLGAP PLAGLVPNGG
     PPPPAGPAGP RGPGPRPVGP PVNGGPRAGA SGHGGPPRPM QQPGALLSQP LLSPQSSPAG
     PAQRGPRPPM GSAASTPLYI PGGPAAAGPQ GYGQPQPRPQ LFPPGPGGPQ GALGPAGIQG
     GMQVARAGPP GQVGAPGAPQ PQVGRMPGAH GMAQ
//
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