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Database: UniProt
Entry: A0A1I4YVP0_9ACTN
LinkDB: A0A1I4YVP0_9ACTN
Original site: A0A1I4YVP0_9ACTN 
ID   A0A1I4YVP0_9ACTN        Unreviewed;       552 AA.
AC   A0A1I4YVP0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=TAP-like protein {ECO:0000313|EMBL:SFN41843.1};
GN   ORFNames=SAMN04487980_1019108 {ECO:0000313|EMBL:SFN41843.1};
OS   Streptomyces sp. cf124.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFN41843.1, ECO:0000313|Proteomes:UP000198530};
RN   [1] {ECO:0000313|EMBL:SFN41843.1, ECO:0000313|Proteomes:UP000198530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF124 {ECO:0000313|EMBL:SFN41843.1,
RC   ECO:0000313|Proteomes:UP000198530};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; FOUV01000019; SFN41843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4YVP0; -.
DR   Proteomes; UP000198530; 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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..552
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011613011"
FT   DOMAIN          104..273
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          421..514
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          512..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  59380 MW;  63A44FEFC3363B45 CRC64;
     MTMYRSPSRR HSRLRLVGAA VTALVLAATG TATQAMAAQS TGQKAGSGQT PPPPVPTLTW
     ADCQGGYECA NAEVPLDYRA PEGKKITLAV VRKKAADPAK RKGTLFMQPG GPGNSGVDFV
     RNNYAGLPAA LRESFDVFGY DVRGVGRSSA LTCFDDTRYT KAVTDAKGVP GPDAFGPALR
     EAAEFNQACL DNSGELLPYV GTEYVARDID LLRQALGEEQ LTYYGRSFGS YIGTVYAAMF
     PKRVRALTLD GAYDPYKYAY RPYAYDRAQY QALDGSMSRF LDWCASDPAI CGFGDGDPRA
     AFEQLKKDLD ANPVTTASGG KANGYTLVYR LMFNINEGKV IWPSLGAALK KAQARDNTSF
     LLRPPSPASF DFLGPNVVVE CVDKEYPKSL RKLERNVTAN AKDAPLLGPA MAFGPPTYDH
     QHATACVQWP AEKVSRYDGS FRARGSQPIL VLGTTGDPDT PYQDAVALSR QLDNASLVTF
     DAEGHTAFGR SRCATDAVID YLVDLKVPAS GTTCADETQP PSSTPKTAPP GTTLSELRNG
     VNERVERIDA VS
//
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