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RBD2_YARLI
ID   RBD2_YARLI              Reviewed;         297 AA.
AC   Q6CDV6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Rhomboid protein 2;
DE            EC=3.4.21.-;
GN   Name=RBD2; OrderedLocusNames=YALI0B20878g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382128; CAG83409.1; -; Genomic_DNA.
DR   RefSeq; XP_501156.1; XM_501156.1.
DR   AlphaFoldDB; Q6CDV6; -.
DR   SMR; Q6CDV6; -.
DR   STRING; 4952.CAG83409; -.
DR   EnsemblFungi; CAG83409; CAG83409; YALI0_B20878g.
DR   GeneID; 2907094; -.
DR   KEGG; yli:YALI0B20878g; -.
DR   VEuPathDB; FungiDB:YALI0_B20878g; -.
DR   HOGENOM; CLU_071084_0_0_1; -.
DR   InParanoid; Q6CDV6; -.
DR   OMA; NTFPFIH; -.
DR   Proteomes; UP000001300; Chromosome B.
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; 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..297
FT                   /note="Rhomboid protein 2"
FT                   /id="PRO_0000206192"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          268..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   297 AA;  32725 MW;  D456B178892079A4 CRC64;
     MAQFPLFQKF QKAIQHPPAL SLGLPIFLTV IFLLSQRYVW IEDDLELRST ALTNFELNRI
     SFYPLVHATW FHLLLNLVAL QPIVSQFERV NGTVRTGIVL NILAVVTAIP WCLLSIGFFP
     DEAVLGSSAW IFSFMGYWAI RESSKQPTTQ LAPNLVVPTW LLPIIYLVVI AIVIPSSSFI
     GHLLGLIAGW MMALGYLDVL IEPSSKVVLW IENKISRVID LIPSSIVTFY REEGALDTRA
     AARADTNRSL SVSGGNFLGF QANSSQADLE AGTRSRGNSS VDPTTSFPGT GQTLGTQ
 
 
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