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Database: UniProt
Entry: A0A368VQT1_9ACTN
LinkDB: A0A368VQT1_9ACTN
Original site: A0A368VQT1_9ACTN 
ID   A0A368VQT1_9ACTN        Unreviewed;       522 AA.
AC   A0A368VQT1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=TAP-like protein {ECO:0000313|EMBL:RCW43964.1};
GN   ORFNames=DFQ14_105109 {ECO:0000313|EMBL:RCW43964.1};
OS   Halopolyspora algeriensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC   Halopolyspora.
OX   NCBI_TaxID=1500506 {ECO:0000313|EMBL:RCW43964.1, ECO:0000313|Proteomes:UP000253495};
RN   [1] {ECO:0000313|EMBL:RCW43964.1, ECO:0000313|Proteomes:UP000253495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8575 {ECO:0000313|EMBL:RCW43964.1,
RC   ECO:0000313|Proteomes:UP000253495};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-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:RCW43964.1}.
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DR   EMBL; QPJC01000005; RCW43964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368VQT1; -.
DR   OrthoDB; 5166357at2; -.
DR   Proteomes; UP000253495; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253495};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..522
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038488862"
FT   DOMAIN          145..333
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          421..520
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          34..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  55146 MW;  F7293BDD5BDC621F CRC64;
     MPRITHRAGA LLLPLVLLIV AACSAGPSER PAVAYRGSQQ QVPPAPAPPE PAPLPPLGPP
     AQQALGWQDC TERTRLEIGV STLPEGMSFS CSRLLTSLSP PGAISSGTSR ISLLSVGSGS
     IPLVVVNDIR GVPGTAFTAR LALKLPPEML ETFRIIGMDR RGSGRSDPAT CFPPAARETI
     VGFDPRATER AALDRLLDSV RSASQECLLE LEKRAQAYDT WRTAADLEEL RIELGVPRLH
     AIGRGEGSRV LATYAQRYPR SVGRMVFDGA PDPTLDALGR TKKQAREAER TFDAFAAQCT
     AGNACPLGPD PRRTVEDLIE RTRATPLPGA GSPVTAGTIV RAILLGLTDP DRWHELVQAL
     DAADRGDGTM LGRMVAPLLH GDAAHPPGLD SRVITRCNDT TLRVPPQRGV GIATELVDRF
     PLFGGVLAQQ LVQCSLWPVP QRSLPVPSNP ALPPIPVITT ATDPLTPALG SEHMADRLAA
     GITVTWQGTG HGALGRSRCA TLNASGFLVH GALPAENTAC PA
//
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