ID   RBD2_PODAS              Reviewed;         289 AA.
AC   Q874X5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Rhomboid protein 2;
DE            EC=3.4.21.-;
GN   Name=RBD2; ORFNames=Pa5D0065;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=12892638; DOI=10.1016/s1087-1845(03)00025-2;
RA   Silar P., Barreau C., Debuchy R., Kicka S., Turcq B., Sainsard-Chanet A.,
RA   Sellem C.H., Billault A., Cattolico L., Duprat S., Weissenbach J.;
RT   "Characterization of the genomic organization of the region bordering the
RT   centromere of chromosome V of Podospora anserina by direct sequencing.";
RL   Fungal Genet. Biol. 39:250-263(2003).
CC   -!- FUNCTION: Probable serine protease. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR   EMBL; BX088700; CAD60752.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q874X5; -.
DR   PRIDE; Q874X5; -.
DR   VEuPathDB; FungiDB:PODANS_5_5980; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Golgi apparatus; Hydrolase; Membrane; Protease; Serine protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..289
FT                   /note="Rhomboid protein 2"
FT                   /id="PRO_0000206190"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        134
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  31604 MW;  4A81276AEC40F837 CRC64;
     MPPNITALNT TRARTYVFRL PLFTRVVIIA IVGFWLAGLQ SIVDIQQWGA LIPDEMGLAT
     LYRMNTFPFI HLNIFHAVMN ILALTPLMER FEAEYGTLNC LALFFGPLTT IPAFLYIGLE
     KFVFGNNVAV MGASMWVFLL LGVEAVKTYK VNPNFVIGTY SIPTWTTPIG VLFAMAVLVP
     SSSFWGHAAG LVIGYGGMFS STLNKKEKRQ CADVKGVAGL GYVKFLAPPE KILRWIEGKL
     NLLGRLPHYV SIDQKTYGRF GVLPSNNTPA AASPGVALGL VGSTQRLGP