ID M7X3H7_RHOT1 Unreviewed; 716 AA.
AC M7X3H7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=RHTO_05056 {ECO:0000313|EMBL:EMS24876.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS24876.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS24876.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS24876.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6; Evidence={ECO:0000256|ARBA:ARBA00001003};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000256|ARBA:ARBA00004393}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB722644; EMS24876.1; -; Genomic_DNA.
DR RefSeq; XP_016275995.1; XM_016418719.1.
DR AlphaFoldDB; M7X3H7; -.
DR MEROPS; S10.007; -.
DR GeneID; 27369069; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_1_1; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361156};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 566..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 77106 MW; A65BBE772E7710E5 CRC64;
MTAGGARYSW SARDPRTRRG FPVDTPQFER RVRDLSTRQS NPDEEMSAAN FFIPSLPGQP
ADSSLTMYGG HIPSAPPKNG VPDTESDAHL YFFMVRNKHI ADTERTLLWF NGGPGCSSFD
GGMMEIGPHR LVPNGDGKLV EAEGAWNEYA NVIFIDQPVG TGYSYMSTNE YVHDLPEASA
HVVEFLSKFY NVFPEFKNHD TYIGGESYAG QYIPYFAQAI LASPRLPTRL KGLLIGNGWI
DPYNQYPAYL DFALQAGVIK EGSDAEKAVR KEVKTCQEHM DVKVSGGMDK MPIHLGICER
ILGAITDSTI QSVNGQNMCV NNYDVRLTDT HPACGMNWPP DLHDMYPYLG RDDVKSAFHA
TRHPGPWVEC NGQVGAQFYT PNSRPSVQLL PELLEKVPIM MFAGAEDLIC NHVGIERMIE
NLEWNGEKGF GNATAEEWVV NGKSAGTWTS ARNMTYVKIT GASHMAPYDE PLATHDMFLR
FIGVSLLSAA GPAAQVPSRI GNEIPAVLGS TLPNGTAIDS SSSGGLSAEK QLDGVSSGSS
GDSSSLGLNS GGGKLGYGGD AALEGLVHAS SALVLVALMA AAFALFLWFR RRTQRLSRGG
EGGGWGALGG RPGGLSKHAR AKSLGRGGGL GLGGVEHEED DSEDVEGRPG VGGDSHELDE
LMSSRRAGGA GDAYRDADEK RRLAGGRRDE EEEVFGLGDD EDDEDEAAGG RKGRLD
//
