ID   A0A0M3INI0_ASCLU        Unreviewed;      1637 AA.
AC   A0A0M3INI0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=oleoyl-[acyl-carrier-protein] hydrolase {ECO:0000256|ARBA:ARBA00012480};
DE            EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0002030801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0002030801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family.
CC       {ECO:0000256|ARBA:ARBA00029454}.
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DR   WBParaSite; ALUE_0002030801-mRNA-1; ALUE_0002030801-mRNA-1; ALUE_0002030801.
DR   Proteomes; UP000036681; Unplaced.
DR   GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0032787; P:monocarboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 2.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 3.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          657..733
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          805..880
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1637 AA;  187109 MW;  26F647A74226E4BE CRC64;
     MLEIIQQICN ALQQCIICIT GEPLRSDTII PIISTKSLRT MLICLSIVFI GAAYLPIDRT
     NPQNRIRQIL EESKVAYYIA EDDYNIKNII PILIEEVFEY LHNVSSTFKH RTLPDDLAYV
     IFTSGTTGKP KGVTIKQKAV INLAQQSAYN FSMSSTDCVY QFTNFIFDNS ILEMIMALSN
     TSALFIEERT FSTTIFLREI HSSHVTHALL FPGLVEMFSY EEVAQLVYLR YWIVGAEKLS
     ERLMSNALKN GVNIIQNYGP TETTAYALSK HMKILDNSNN LGKPIFNVIS MSRKCDGNKA
     PPLTSGELLI GGIGLMRGYL XTIKQKAVIN LAQQSAYNFS ISSTDCVYQF TNFIFDNSIL
     EMIMALSNTS ALFIEERTFS TTIFLREIHN SHITHALLFP GLVEMFSYEE VAQLVYLRYW
     IVGAEKLSER LMSNALKNGV NIIQNYGPTE TTAYALSKHM KILDNSNNLG KPIFNVISMS
     RKCDGNKAPP LTSGELLIGG IGLMRGYLNK EENFEQYWCK NHKKVQLYAS GDIVKQLRNG
     DVIFLGRQDE QVKIRGFRIE LPEIEATICA INSIKQCKVI VKEEPIPILI AYIVLKDGNS
     MLEENIVRQY CTQRLPYYMI PTYFLQIQQF PLTNNNKLDV SRLPSLDEIK KKRRRDEPKN
     ILEFQLWLLF KEVLNNEFIS TADDFFALGG NSLHAMRLAQ RIEENIGIEI DIEATIYAIN
     SIKQCKVIVK EEPIPILIAY IVLKDGNSML EENTVRQYCT QRLPYYMIPT YFLQIQQFPL
     TNNNKLDVSR LPSIDEIKKK RRRDKPKNIL EFQIWLLFKE VLNNEFISTA DDFFALGGNS
     LHAMRLAQRI EEDIGIEIDV RTIFQYRTIC RLAEKLDETR NETKRNTKSI RRTEQQLSII
     EYNYIPLSFQ QQQILFLSQT KQADYYSLLF VQNFDKSIDY RCLRMAFLRL ILRQPSLRTI
     FSEVNYETTQ AILSGTECYF HSDVQSAIPS DVPIIFRWPS SIGTDFISPI YCSISLTREA
     YTVMLVLSHI ISDAWSTRLI ETDLSQLYDR ITRGKFDDEK LAFTYAHYSV EQHARKDHLL
     KLANECALKL RNFLGDYQCI RRIFGKPSTT QTMTIKCVQV DFRLNEITSQ RVYQCCAKLS
     TTPFVIFVAS IGLSVHKLNG NRMLIIGAPI ANRSKSTEKI VGNFLNNLLI VSISPKIDET
     LRKYLRSINA TVEDARRYEC VPYCLINDIL VRGMDRNVEA LCQIYINCRY NLEDGKTNRL
     PPSKLHRVSE ISSMKNHLDQ VQVMGAQRGS PQQYAKCVHP IEVDIDLLNT NFECSIRIRA
     DIGSQEDAES LKKLMQHCLE EILRSAEEEM TSSNGAIQNT IAPYSSSPER FDLSPVEKNV
     DDRIETIGCH EERFLKKLLV LFHPLVGGVT LPYAALVRKL IPLLEDITIV GIQHPNTFAL
     ISNETKLTQS IEMLCTLYVD GIIDLVRKAD SCVFIGASLG AILAFECATQ LLQKGYIIEE
     IINIDGGGQP SAMPSITFEE HRKQMHNLLM RHTDGEHLNT HLQEAMIDNA WQLLRMVQNY
     RPKKRIEQRV HLLKVKGEES DDYGWSKIAN TYVTTIPGTH EDMLNEENSA TIANIIAKII
     CPSSMRHSPN VFKADGN
//