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Database: UniProt
Entry: A0A3N2NUJ2_9ACTN
LinkDB: A0A3N2NUJ2_9ACTN
Original site: A0A3N2NUJ2_9ACTN 
ID   A0A3N2NUJ2_9ACTN        Unreviewed;       520 AA.
AC   A0A3N2NUJ2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Alpha/beta fold hydrolase {ECO:0000313|EMBL:ROT26071.1};
GN   ORFNames=EF879_25955 {ECO:0000313|EMBL:ROT26071.1};
OS   Micromonospora sp. HM5-17.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2487710 {ECO:0000313|EMBL:ROT26071.1, ECO:0000313|Proteomes:UP000281230};
RN   [1] {ECO:0000313|EMBL:ROT26071.1, ECO:0000313|Proteomes:UP000281230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM5-17 {ECO:0000313|EMBL:ROT26071.1,
RC   ECO:0000313|Proteomes:UP000281230};
RA   Thawai C.;
RT   "Micromonospora sp. HM5-17, a new actinomycetes isolated from a hot spring
RT   soil.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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:ROT26071.1}.
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DR   EMBL; RJWA01000016; ROT26071.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2NUJ2; -.
DR   OrthoDB; 4006962at2; -.
DR   Proteomes; UP000281230; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ROT26071.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281230};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..520
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039629606"
FT   DOMAIN          105..268
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          421..500
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          348..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  56435 MW;  FFF185964DD44393 CRC64;
     MVTTLVVSVA GLATMVVGAP TAAAPPSPVP TVRWQPCPEY SDDEIRARGV RADRIPEFRA
     LLARTECGTV TVPLDYRRPT GRTISIALTR LKATDQKRRL GSIALNPGGP GGPGYLMPID
     IVMTHAEHAR LNERYDLIGF DPRGVGYSTN VECPPPEAAG SPQAGPLTEE AARQRYDAQV
     RHNVSCAGSD PEFLGQLTSA NVAHDLDRLR KALGERRLSF LGVSWGTRLG MVYRSLYPGK
     VDRMFLDSVA MPHYQFDMFD DRRTAAAERN FGRMAEWMAD HDDVLHFGTS ADEVRAAVVA
     LRQSYDDEPR SFTDLPMPVD GSIIAKLASQ DSRGWPTAAR ALAELRDATG PTAPPTVRQI
     FGGQSSPSEP GVSRPDRFSP TMQQAVMCNE DSSRPDFATA WAAYQRRLAE NPVTGRATDF
     SVRCAGWPLP VQEVRLHRAA GSLVLSGHRY EMISPYEWTV EVQKLIGGTV FTVEDDVHGS
     VLFEPSCGAE LVRYFETGRI GTGCPGAGGP PPLASGGENA
//
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