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Database: UniProt
Entry: A0A261EV92_9BIFI
LinkDB: A0A261EV92_9BIFI
Original site: A0A261EV92_9BIFI 
ID   A0A261EV92_9BIFI        Unreviewed;      1172 AA.
AC   A0A261EV92;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Hydrolase {ECO:0000313|EMBL:OZG50790.1};
GN   ORFNames=PSRA_1357 {ECO:0000313|EMBL:OZG50790.1};
OS   Pseudoscardovia radai.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Pseudoscardovia.
OX   NCBI_TaxID=987066 {ECO:0000313|EMBL:OZG50790.1, ECO:0000313|Proteomes:UP000216725};
RN   [1] {ECO:0000313|EMBL:OZG50790.1, ECO:0000313|Proteomes:UP000216725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24742 {ECO:0000313|EMBL:OZG50790.1,
RC   ECO:0000313|Proteomes:UP000216725};
RX   PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA   Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA   Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA   van Sinderen D., Ventura M.;
RT   "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT   family.";
RL   BMC Genomics 18:568-568(2017).
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:OZG50790.1}.
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DR   EMBL; MWWR01000013; OZG50790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261EV92; -.
DR   OrthoDB; 3252468at2; -.
DR   Proteomes; UP000216725; 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; IPR043708; DUF5648.
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   Pfam; PF18885; DUF5648; 3.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OZG50790.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1172
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038988939"
FT   DOMAIN          289..463
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          759..817
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          68..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1172 AA;  121634 MW;  0FF537D1CDB18F7A CRC64;
     MTMRRILSIA TCVVATMAMS LPLTATAYAE DAAAQSQLEE VSAQLLAATS AASTIPTTST
     ISAVASGGAT TSASDASTDQ DAAALASSDS PSATDDVAEG LAAANASHAS MMLAASAQDA
     HNDSSDDALQ IDAPSSDPAL AESDQADAAV EQVASQAAQN ETAGESSTTP DPTDFASLAA
     DDPLRDLPQA AYDYSFVSNG TVTLTGPRPG GTATGSVPAG LESYYSQGID WNLTTCAAFG
     LTTPYDTATR ASRCAYVSVP LDYSDLDGRS VQIGVYMYPH DPSVECYGVL FVNPGGPGSS
     GMSIATHLPG MLSNAVGNAT AWSHYDIVGF DPRGVGNSLP QIRCQSDAAQ DAQREGGDGL
     TNEQYDAIDQ YNAQQCYANT ATSYEGITGD DFIPTVSTDT VARDMDVLRS ALGCEKASYL
     GYSYGTRIGY YYAMQFPRSV HAMVLDGNMN VFEFESAWNS SLDKGRYSGY YTNLRSVTST
     SAASAEGASD AAAGAASSPA AAGADDASAA GTDAVATSGP ELQLTAPSYA GAENAQMASF
     EATFRQFLSW CLTSSNLTGG SACAVGDHVD GTPADAQIDA AEAAYQQIAR QYWGGKDAGL
     SDGRALSFQD FTTATCEAMY SSTRWKAFNI GLRNAKNGNG SWMMYLADTY NERSSGIAHY
     DPATGAWGTR SGYANRNAAL YVIQTQDGKQ VSQGESSSAY TSAQRARRMK AYYAAAPFAD
     PGADESGVAR GLSTGIGMQF FFTSGGNLLS NPGYEMSTLP NVLVISTTYD PATPYVNGVV
     NARALRGTLL IVAAARHCEY GYNRAATGIA NEYLAGPDAF QSKVDAGTFG SGTVYAGSSN
     VTTKDVFSNV ITGSECQLVS FRHTESVATS YDSLTDGTSG NKRNVELGGT SADGKTDATA
     EGTYITVKRP DATADSAETD RVTGGSAVRV FLNDIDVDCT AANAGCTYRA YLYSASGGAS
     GASDGAGAAG GAGAGAAVQL GEAVAATSGG GGYYLDLTIP ADAALGAAKI AVYRENDWLY
     GWQAITIVDA TTGGDADAGK TMYRLYNPNT GEHFYTADLT ERANLAAVGW RDEGRAWVAP
     VSGDAVYRLY NPVAGGHHYT MSRHEADTLV SQGWRKEGVG WYSAPASTGT AVWRVYNPNG
     GAHHYTTDAA ERSELIRIGW NDEGVAWYAL AS
//
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