ID   A0A2W2EYU4_9ACTN        Unreviewed;       552 AA.
AC   A0A2W2EYU4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Transporter {ECO:0000313|EMBL:PZG29786.1};
GN   ORFNames=C1I98_31655 {ECO:0000313|EMBL:PZG29786.1};
OS   Spongiactinospora gelatinilytica.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Spongiactinospora.
OX   NCBI_TaxID=2666298 {ECO:0000313|EMBL:PZG29786.1, ECO:0000313|Proteomes:UP000248544};
RN   [1] {ECO:0000313|EMBL:PZG29786.1, ECO:0000313|Proteomes:UP000248544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7K107 {ECO:0000313|EMBL:PZG29786.1,
RC   ECO:0000313|Proteomes:UP000248544};
RA   Sahin N., Saygin H., Ay H.;
RT   "Draft genome sequence of Sphaerisporangium sp. 7K107.";
RL   Submitted (JAN-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:PZG29786.1}.
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DR   EMBL; POUA01000365; PZG29786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W2EYU4; -.
DR   Proteomes; UP000248544; 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}.
FT   DOMAIN          114..306
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          428..521
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..552
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  59314 MW;  8FC84E4F7674ABD0 CRC64;
     MAVGRRGPGE SGRRDQEPTP VIGDHVRRTV PLLAAALAAL VGLSPLAPAQ AAPAAPAAPS
     GGPAIAWQPC PEDPTADCGT LAVPVDWKNP GGPTIDLALA RRKATDPAAR VGSLLIDPGG
     PGGSGVDFAL AAGTYFSAEL NRRFDIVGFD PRGVARSRPI VCSAELAGQA PYPVIKSQTE
     FDAWRDFAKR LRADCRARTG PLFDHVDSGS VAHDMDAIRA ALGEEKLTYY GISYGTLMGQ
     MYAERFPGRV RALALDSNMD HSLGTGPFLY TEAHTAQDSF DEFVKWCGEE SRCALRGRDV
     RAFWASLLDR ADRGELRYPG EPDYRLTRLD VIGIAFSAFY GPAWYELAEL LVAIDAGAQR
     PPASAARLAA HAPERRHAGT APDEVEIPTQ VFCEDFRLPV RDYKEYAKHL RRSKAIAPDM
     ELSPAAVSVL AYCLSEPDPI PNPQHRLRVN GTPPLLLGNA LHDPATGYVW AVNAAAQIGK
     EARLVTYEGW GHGIYGRGEC TTGAIDDYLI SLKPPARGTR CAAVPPEPPA TAQNRSRPRP
     PASPLLPHVP LW
//