ID   RBD2_ASHGO              Reviewed;         261 AA.
AC   Q755H8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Rhomboid protein 2;
DE            EC=3.4.21.-;
GN   Name=RBD2; OrderedLocusNames=AFL155C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53219.1; -; Genomic_DNA.
DR   RefSeq; NP_985395.1; NM_210749.1.
DR   AlphaFoldDB; Q755H8; -.
DR   STRING; 33169.AAS53219; -.
DR   EnsemblFungi; AAS53219; AAS53219; AGOS_AFL155C.
DR   GeneID; 4621621; -.
DR   KEGG; ago:AGOS_AFL155C; -.
DR   eggNOG; KOG2632; Eukaryota.
DR   HOGENOM; CLU_071084_0_0_1; -.
DR   InParanoid; Q755H8; -.
DR   OMA; NTFPFIH; -.
DR   Proteomes; UP000000591; Chromosome VI.
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:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
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; Reference proteome;
KW   Serine protease; Transmembrane; Transmembrane helix.
FT   CHAIN           1..261
FT                   /note="Rhomboid protein 2"
FT                   /id="PRO_0000206182"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        124
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   261 AA;  29156 MW;  D3612EF702456EED CRC64;
     MDWKSMLRTG VHKPGALTAG LSVFLTLVYV LNWVFPINEK ILLDPGALRK LQLTRLSLYP
     LAHLSIFHLL LNLMSLFVPL SMFEASHGTV FTGITLNLLA IVTGVVYCLV GMLLYPNVYV
     GGASGWCFTL CGYFAVQEAG FRPHYELASL KMPTLYIPLV FLVLVTLLMP GSSFVGHLIG
     LGLGYLIGFR ERWLQMATPP GWLIVKIETW LDRWISMIPS VVKYHRESSV DRTAGYTPLY
     QESELPLHND NFPGQGRVLG P