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
//