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Database: UniProt
Entry: M7X586_RHOT1
LinkDB: M7X586_RHOT1
Original site: M7X586_RHOT1 
ID   M7X586_RHOT1            Unreviewed;       496 AA.
AC   M7X586;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   22-NOV-2017, entry version 20.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EMS18824.1};
GN   ORFNames=RHTO_05571 {ECO:0000313|EMBL:EMS18824.1};
OS   Rhodosporidium toruloides (strain NP11) (Yeast) (Rhodotorula
OS   gracilis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18824.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS18824.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS18824.1,
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
RT   toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KB722675; EMS18824.1; -; Genomic_DNA.
DR   RefSeq; XP_016269943.1; XM_016419232.1.
DR   EnsemblFungi; EMS18824; EMS18824; RHTO_05571.
DR   GeneID; 27369584; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EMS18824.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016926};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016926};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   496 AA;  54092 MW;  CF097A22917E5486 CRC64;
     MTMSTPASAL QPAQAFVDFV NKAVTPFHAV HECVQRLEKA GFTRLHERES WAGKLSPGGK
     HFVTRNQSSI IAFTIPPADA TKTGKPLGIS VVGAHTDSPR FVVKPVSKRE KAGYAQIGVE
     TYGGGLWATW MDRDLGVAGR VTLAGAAGKA KQEYSSHLVH VRNPIMRMPT IAIHLERTQN
     DKFHYNPETQ QVPIVALASK ELNRAFVEEN NSSAEVSFAD PLDISSHHHP ILLHTLAREL
     SEQIGEQITP AQIHDFELSL FDCQPATIGG ALNEFIFAPR VDNLFSSFAA VEALVLSASS
     SAPSDGRVSM IALFDNEEVG SVSAYGAESN FIESVFERVS VAFKAEGESE AEAYQRTMAS
     SYLLSTDVGH SVHPGFTDKH EENHKPLINS GIAIKTNSKQ RYATTSQTVF PLRRVAAEAQ
     VPLQEYLVRN DMACGSTIGP LVSKIGLRTV DIGAPILSMH SIREMAGVKD VKHLIDLFEK
     FFERFGVLDT LAETVD
//
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