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Database: UniProt
Entry: M7XKT1_RHOT1
LinkDB: M7XKT1_RHOT1
Original site: M7XKT1_RHOT1 
ID   M7XKT1_RHOT1            Unreviewed;       454 AA.
AC   M7XKT1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=RHTO_02357 {ECO:0000313|EMBL:EMS20743.1};
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:EMS20743.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS20743.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS20743.1,
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   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247, ECO:0000256|PIRNR:PIRNR037226}.
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DR   EMBL; KB722659; EMS20743.1; -; Genomic_DNA.
DR   RefSeq; XP_016271862.1; XM_016416034.1.
DR   AlphaFoldDB; M7XKT1; -.
DR   GeneID; 27366370; -.
DR   eggNOG; ENOG502QQPD; Eukaryota.
DR   HOGENOM; CLU_031812_1_1_1; -.
DR   OrthoDB; 1074531at2759; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          192..274
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   454 AA;  48075 MW;  5FD7D9F93A7BEE01 CRC64;
     MPHAKLPTPS QDDLNAAIRE AIDTVDAELR EVSLSIHSHP ELAWNEHHAH DVLTEYMSRQ
     RGFVVTKHAY DLPTAWTAVF TSSAPSNDDK LPVVGFNSEM DALKGIGHAC GHNLIAIAGC
     AAAIGVARTL ERFQLPGKVV LLGTPAEEAG GGKAVFIQRG AYDEFDACLM VHPGPGGGGK
     HGAGIMTSSC VAGLTVTYHG ASAHAGGAPE KGRNALDAAV LAYQNVSALR QQLPKDAKLH
     GIISGCENWS ANVIPGEAKL LYGIRSPSAS DLAPLIPRVL RCFAGAALAA NCTYTLTSEI
     LYLDVRPSPG LAQAFKDFAE KEYGEEGYEV PEDCPTGGST DFGNVSYRCP SLHPMFYLPD
     AAGDEHPPAV ATPSAHTATL RAASALASSG LRVLTSPSFR AQIRRDWEED MHLAQGEKAV
     SVIERLVPSV EVGPAGKEVR EGRFCDYCVC GCEK
//
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