RHBL6_TOXGO
ID RHBL6_TOXGO Reviewed; 531 AA.
AC Q2PP52;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Rhomboid-like protease 6;
DE EC=3.4.21.105;
GN Name=ROM6;
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;
RA Dowse T.J., Soldati D.;
RT "Rhomboid-like protease 6 from Toxoplasma gondii.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative serine protease involved in intramembrane
CC proteolysis and the subsequent release of polypeptides from their
CC membrane anchors. {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 -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; DQ314573; ABC40721.1; -; mRNA.
DR AlphaFoldDB; Q2PP52; -.
DR VEuPathDB; ToxoDB:TGARI_245590A; -.
DR VEuPathDB; ToxoDB:TGCAST_245590A; -.
DR VEuPathDB; ToxoDB:TGCOUG_245590; -.
DR VEuPathDB; ToxoDB:TGDOM2_245590; -.
DR VEuPathDB; ToxoDB:TGFOU_245590; -.
DR VEuPathDB; ToxoDB:TGGT1_245590A; -.
DR VEuPathDB; ToxoDB:TGMAS_245590; -.
DR VEuPathDB; ToxoDB:TGME49_245590; -.
DR VEuPathDB; ToxoDB:TGP89_245590A; -.
DR VEuPathDB; ToxoDB:TGPRC2_245590; -.
DR VEuPathDB; ToxoDB:TGRH88_060210; -.
DR VEuPathDB; ToxoDB:TGRUB_245590; -.
DR VEuPathDB; ToxoDB:TGVAND_245590A; -.
DR VEuPathDB; ToxoDB:TGVEG_245590; -.
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; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
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..531
FT /note="Rhomboid-like protease 6"
FT /id="PRO_0000239079"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 150..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 419
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 493
FT /evidence="ECO:0000250"
SQ SEQUENCE 531 AA; 58688 MW; D94F4FA78169D990 CRC64;
MKKSAGPFIA SWRPFVGLPV SLERGRTFSR VLGICTYTPA IRRQMLLSGV SVIPPPLSKN
FFRHAHLTGF SPFRSSCRRL FAQNGSDVAP LVSRIPNQSV APGDTQWSVS PMGVHCEHWL
KTRCLPGLPA AVFGSHQQVE AALLQRGLSP AKDASERVRS ATREDLVRRE RPTSEAGSHP
PLPSRSSVSA FQLRSRCDPA VSGPSDSAPC GLSQTSFSLR SSSSSGATTR FSVPAVCPVF
LCRSLPRLSG RFSRTRFGKQ RKRTEEQEDS KDFDTGPLSS GSIFTVLVGS LLFFDVLRSG
LYEHRKLLGA FLMTNAAVFT GWRLAATAGN GTWWTFLMRH FVLCRENLAR ARIYTFVTSS
LSHKSTGHLI FNLFVINQLF RLLSFDLSDR DFASLFGLAA LCGGLGHLLV SRQPVLGASA
FAYALLWTEA TRHSREMFRI LPIPFFPLTA LQLVQVAMCL EAAMAFLARP AFLARFPASR
LLRFAQGISW SGHLGGLAAG CLYSWYKRRV EGDRSWQSFS ELCRTYGTSD W