ID   Q108E4_RUBV             Unreviewed;       313 AA.
AC   Q108E4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   05-FEB-2025, entry version 33.
DE   SubName: Full=Nonstructural protease protein {ECO:0000313|EMBL:AAZ03625.1};
DE   Flags: Fragment;
OS   Rubella virus (RUBV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Hepelivirales; Matonaviridae; Rubivirus; Rubivirus rubellae.
OX   NCBI_TaxID=11041 {ECO:0000313|EMBL:AAZ03625.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AAZ03625.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4861_MILAN_ITALY_1993 {ECO:0000313|EMBL:AAZ03625.1};
RA   Zhou Y., Zheng D., Zhao H., Suppiah S., Ushijima H., Frey T.K.;
RT   "Genomic Analysis of Diverse Rubella Virus Isolates.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00047984};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01237};
CC       Note=Zn(2+) is necessary for the protease activity. The protease can
CC       also function efficiently with Cd(2+) and Co(2+). {ECO:0000256|PROSITE-
CC       ProRule:PRU01237};
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm, host perinuclear region
CC       {ECO:0000256|ARBA:ARBA00004407}. Host membrane
CC       {ECO:0000256|ARBA:ARBA00004551}.
CC   -!- PTM: Non-structural polyprotein p200: Specific enzymatic cleavage by
CC       its own cysteine protease yield mature proteins p150 and p90.
CC       {ECO:0000256|PROSITE-ProRule:PRU01237}.
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DR   EMBL; DQ085356; AAZ03625.1; -; Genomic_RNA.
DR   MEROPS; C27.001; -.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR008738; Peptidase_C27.
DR   InterPro; IPR022245; Rubi_NSP_C.
DR   InterPro; IPR044070; RUBV_NS_PRO.
DR   Pfam; PF05407; Peptidase_C27; 1.
DR   Pfam; PF12601; Rubi_NSP_C; 1.
DR   PROSITE; PS51889; RUBV_NS_PRO; 1.
PE   4: Predicted;
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01237};
KW   Membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01237};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01237,
KW   ECO:0000313|EMBL:AAZ03625.1};
KW   Thiol protease {ECO:0000256|PROSITE-ProRule:PRU01237};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01237}.
FT   DOMAIN          2..303
FT                   /note="Peptidase C27"
FT                   /evidence="ECO:0000259|PROSITE:PS51889"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..185
FT                   /note="Interaction with host CALM1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   REGION          195..230
FT                   /note="EF-hand-like"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   ACT_SITE        154
FT                   /note="For cysteine protease activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   ACT_SITE        275
FT                   /note="For cysteine protease activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   SITE            303..304
FT                   /note="Cleavage; autocatalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01237"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAZ03625.1"
FT   NON_TER         313
FT                   /evidence="ECO:0000313|EMBL:AAZ03625.1"
SQ   SEQUENCE   313 AA;  33359 MW;  84DC65F4B48EE5FD CRC64;
     PLAPRPASDP GPLTQRSASP PAAPSGEAAA PESRGCQGCE LCRYTRVTND RVYVNLWLER
     DRGATGWAMR IPEVVVYGPE HLAAHFPLNH YSVLKPAEVR PPRGMCGSDM WRCRGWQGMP
     QVRCTPSNAH AALCRTGVPP RVSTRGDERD PNTCWLRAAA NVAQAARACG AYTSAGCPRC
     AYGRALSEAR THEDFAALSQ RWSASHADAS ADGTGDPLDP LMETAGCACS RVWVGSEHEA
     PPDHLLVSLH RAPNGPWGVV LEVRARPEGG NPTGHFVCAV GGGPRRVSDR PHLWLSVPLS
     RGGGTCAATD EGL
//