ID   RHBL2_TOXGO             Reviewed;         283 AA.
AC   Q695T9; Q66TP2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Rhomboid-like protease 2;
DE            EC=3.4.21.105;
GN   Name=ROM2;
OS   Toxoplasma gondii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=5811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=RH;
RX   PubMed=15358257; DOI=10.1016/j.mib.2004.06.013;
RA   Dowse T., Soldati D.;
RT   "Host cell invasion by the apicomplexans: the significance of microneme
RT   protein proteolysis.";
RL   Curr. Opin. Microbiol. 7:388-396(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=RH; TISSUE=Tachyzoite;
RX   PubMed=15753289; DOI=10.1073/pnas.0407918102;
RA   Brossier F., Jewett T.J., Sibley L.D., Urban S.;
RT   "A spatially localized rhomboid protease cleaves cell surface adhesins
RT   essential for invasion by Toxoplasma.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:4146-4151(2005).
CC   -!- FUNCTION: Serine protease involved in intramembrane proteolysis and the
CC       subsequent release of polypeptides from their membrane anchors.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad
CC         composed of serine and histidine that are contributed by different
CC         transmembrane domains.; EC=3.4.21.105;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Detected in sporozoites.
CC       {ECO:0000269|PubMed:15753289}.
CC   -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR   EMBL; AY596192; AAT29066.1; -; mRNA.
DR   EMBL; AY704176; AAU11321.1; -; mRNA.
DR   AlphaFoldDB; Q695T9; -.
DR   SMR; Q695T9; -.
DR   MEROPS; S54.020; -.
DR   VEuPathDB; ToxoDB:TGARI_263290; -.
DR   VEuPathDB; ToxoDB:TGCAST_263290; -.
DR   VEuPathDB; ToxoDB:TGCOUG_263290; -.
DR   VEuPathDB; ToxoDB:TGDOM2_263290; -.
DR   VEuPathDB; ToxoDB:TGFOU_263290; -.
DR   VEuPathDB; ToxoDB:TGGT1_263290; -.
DR   VEuPathDB; ToxoDB:TGMAS_263290; -.
DR   VEuPathDB; ToxoDB:TGME49_263290; -.
DR   VEuPathDB; ToxoDB:TGP89_263290; -.
DR   VEuPathDB; ToxoDB:TGPRC2_263290; -.
DR   VEuPathDB; ToxoDB:TGRH88_067720; -.
DR   VEuPathDB; ToxoDB:TGRUB_263290A; -.
DR   VEuPathDB; ToxoDB:TGVAND_263290; -.
DR   VEuPathDB; ToxoDB:TGVEG_263290; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1540.10; -; 1.
DR   InterPro; IPR002610; Peptidase_S54_rhomboid.
DR   InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR   InterPro; IPR035952; Rhomboid-like_sf.
DR   PANTHER; PTHR22936; PTHR22936; 1.
DR   Pfam; PF01694; Rhomboid; 1.
DR   SUPFAM; SSF144091; SSF144091; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Protease; Serine protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..283
FT                   /note="Rhomboid-like protease 2"
FT                   /id="PRO_0000239075"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        178
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000250"
FT   CONFLICT        172
FT                   /note="Q -> QQ (in Ref. 2; AAU11321)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   283 AA;  30663 MW;  53BE9B772B5B682B CRC64;
     MANIRTLSDY ASSPPRGSSA LEGEVGQGGS PLPLFFPSGT QSGENVSWIQ WLCPGIHLKS
     PIIIISFVQI AVYIASLAAG LAPNEILAPT PQTLVMFGAN IPELIRVGEI WRLICPLFLH
     LNLFHILMNL WVQIRIGLTM EEKYGWKMLL AVYFGVGVLA NMISAAVLFC GQMKAGASTA
     VFALIGVQLA ELALIWHAIQ DRNSAIISVC ICLFFVFVSS FGSHMDSVGH IGGLVMGFAA
     GIWLNENSDI KPTWYDRARL TSQVALAAAP ILSCIFIFLV PRC