ID A0A099JRQ8_9MICO Unreviewed; 446 AA.
AC A0A099JRQ8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN ORFNames=BJ997_000292 {ECO:0000313|EMBL:MBB5639744.1}, GY21_02415
GN {ECO:0000313|EMBL:KGJ80840.1};
OS Cryobacterium roopkundense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ80840.1, ECO:0000313|Proteomes:UP000029864};
RN [1] {ECO:0000313|EMBL:KGJ80840.1, ECO:0000313|Proteomes:UP000029864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuG17 {ECO:0000313|EMBL:KGJ80840.1,
RC ECO:0000313|Proteomes:UP000029864};
RA Sisinthy S.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5639744.1, ECO:0000313|Proteomes:UP000561726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21065 {ECO:0000313|EMBL:MBB5639744.1,
RC ECO:0000313|Proteomes:UP000561726};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|PIRNR:PIRNR037226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGJ80840.1}.
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DR EMBL; JPXF01000005; KGJ80840.1; -; Genomic_DNA.
DR EMBL; JACHBQ010000001; MBB5639744.1; -; Genomic_DNA.
DR RefSeq; WP_035834966.1; NZ_JPXF01000005.1.
DR AlphaFoldDB; A0A099JRQ8; -.
DR STRING; 1001240.GY21_02415; -.
DR eggNOG; COG1473; Bacteria.
DR OrthoDB; 9781032at2; -.
DR Proteomes; UP000029864; Unassembled WGS sequence.
DR Proteomes; UP000561726; Unassembled WGS sequence.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR CDD; cd05672; M20_ACY1L2-like; 1.
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;
KW Hydrolase {ECO:0000313|EMBL:MBB5639744.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029864}.
FT DOMAIN 215..303
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 446 AA; 46823 MW; 8889A282186904EA CRC64;
MSFSNAPSTT YLQKLEAETA RKMQTYESVP SRFAGAPAPL ATAVEAEVNA LAADLHDIVH
TLHADPETAF AEHRSAAFLV QVLASHGIDA QLGVHGLDTA IRAEIGSDAR SQSGPAIGIL
SEYDALPDVG HGCGHNVIAA TGLGAFLALA NTLKHNPDAF DGRVVFLGTP AEEGSSGKEV
MARNGAFDGL DAAIMVHPYG YDLADQVWLG RRVLTVTFRG VAAHASAQPF MGRNALDAAT
LAYQAIGLLR QQLPPVDRVH AVIAEGGTRP SIIPERAVLK IYARSKFAET LKDLSARLND
IADGAALMTG TSVEIDWDEH APSLPVRTNN ALTGRWVAAQ QRRGRSPLPL GVVSETIAAS
TDFGNVSHRI PGIHPLIKIA ASDVALHTHE FAAAAATDAA ELGALDGASG LALTALDFLC
DAELRRSVAD EFAAQGGPVD VPHFFD
//
