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Database: UniProt
Entry: C1MTG3_MICPC
LinkDB: C1MTG3_MICPC
Original site: C1MTG3_MICPC 
ID   C1MTG3_MICPC            Unreviewed;       794 AA.
AC   C1MTG3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EEH57313.1};
GN   ORFNames=MICPUCDRAFT_58059 {ECO:0000313|EMBL:EEH57313.1};
OS   Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN   [1] {ECO:0000313|EMBL:EEH57313.1, ECO:0000313|Proteomes:UP000001876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH57313.1,
RC   ECO:0000313|Proteomes:UP000001876};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC       {ECO:0000256|ARBA:ARBA00007623}.
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DR   EMBL; GG663739; EEH57313.1; -; Genomic_DNA.
DR   RefSeq; XP_003058858.1; XM_003058812.1.
DR   AlphaFoldDB; C1MTG3; -.
DR   STRING; 564608.C1MTG3; -.
DR   GeneID; 9684297; -.
DR   KEGG; mpp:MICPUCDRAFT_58059; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   OMA; FKFARRT; -.
DR   OrthoDB; 1833386at2759; -.
DR   Proteomes; UP000001876; Unassembled WGS sequence.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd14345; UBA_UBXD7; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   InterPro; IPR010666; Znf_GRF.
DR   PANTHER; PTHR10183; CALPAIN; 1.
DR   PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR   Pfam; PF00648; Peptidase_C2; 2.
DR   Pfam; PF14555; UBA_4; 1.
DR   Pfam; PF06839; zf-GRF; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS51999; ZF_GRF; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001876};
KW   Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01343}.
FT   DOMAIN          186..237
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   DOMAIN          260..619
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   REGION          81..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        495
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        563
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   794 AA;  83965 MW;  2BA22728D7FE10BB CRC64;
     MPPRAKRKAP PPVAEVRDAD VEAFVAVTGA DDARARRALL ACGGELQRAV DRHFAVVAPA
     PAPAPAPAAA PLGQTSLHDA AKTREKTETT TPREAPPRFD LDVSTIPTAP SRDADGWVTT
     PSQEDEAEAE TRDATIEWAT RCVRAPRFDD GSFPPDASSI DGRRKGRGKG GKGGEHDEAV
     VVPRWCACDP PRRARVKRAQ RDGPNQGREY YACGLAAARG VFPPPKPCEF FAWADDAPSK
     KSSVETEWRR LTGADGVFDP AHVRQGAVGD CWLLSALAVI AERQDLARRV VGPSAASPAA
     AAAAAASGAY LVRLFLGGRW RGVVVDPCLP VAGRSVEVSR GANGPRPEVN KRRALDDFAP
     AFSRASGNRL WVPVVEKAYA KAHGSYHAIS GGYISEGLLD LTGCPTETIA LLGAGSEHYG
     GETASHTTPF AWCTPFLKDF SRRHSSPALP FQRLTGGGGA FDEARAWEKV LSYCEAGFPM
     GCATSSGGRG LVGGHAYSVL DVRQLHGVAV GRQTKLDGFV EREVEIVDPA PALVSASASK
     YASSAAAADA SSPPPLRLVR VRNPWGRKEW NGEWGAKSET WTSRLGAELG NTRADDGTFW
     MSWHDFLAAF SVVDVCKAHR GWHALSLPGA AHRAEGDGPP GTTRAAVDFG MISSEDGDAF
     EIEVAGDGEG GGGGGGGGSW AYVMALQHTK RGRGGEAFWY ADVGIAVYEK NARANAAAAD
     DAWTPLGAVL GAKERVAQAE LMLERGKRYL ARLFSVGGGA AGPPTAPVTL RVYRRVLSVH
     WSPYDRVGAV NADP
//
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