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Database: UniProt
Entry: A0A2L2U367_9HYPO
LinkDB: A0A2L2U367_9HYPO
Original site: A0A2L2U367_9HYPO 
ID   A0A2L2U367_9HYPO        Unreviewed;      3960 AA.
AC   A0A2L2U367;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Fusarium venenatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI70300.1, ECO:0000313|Proteomes:UP000245910};
RN   [1] {ECO:0000313|Proteomes:UP000245910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA   King R.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000256|ARBA:ARBA00004685}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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DR   EMBL; LN649231; CEI70300.1; -; Genomic_DNA.
DR   STRING; 56646.A0A2L2U367; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000245910; Chromosome iii.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd19532; C_PKS-NRPS; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245910};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..440
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2397..2474
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3518..3594
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2509..2567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3960 AA;  432934 MW;  161CB99B97FF53B3 CRC64;
     MAQDSQYREP IAIIGSSCRF PGSSSSPSKL WDLLHQPRDV IKTFDAERLN LARFYHENGD
     THGSTDVAAK SYLLEEDNRL FDTSFFGISP MEAAGMDPQQ RILLETVYEA FEAAGLTLEQ
     LRGSLTSVHV GVMTSDWANI QARDTETISK YNATGSANSI MSNRISYVFD LKGPSETIDT
     ACSSSLVAVH NAALGLLNGD SDTAVVAGVN LILDPAPYIN ESKLHMLSPD SRSRMWDKAA
     NGYARGEGAG AVLLKTLSQA LKDGDDIEGV IRATGVNSDG QSPGITMPFA PTQTALIRKT
     YARAGLDPKK DRPQYFECHG TGTPAGDPVE ARAISDAFTG GDMSVENPLY VGSIKTVIGH
     LEGGAGLAGV LKVLLALKHR VIPPNLLFNE LNPSVAPFYG PLQIPTTAIP WPELPDGVPA
     RASVNSFGFG GTNAHVIIES YEDTPDEPSL HENEGILGPL VLSAKSGASL LRTVETYRNH
     TQSNPTLDIA ALSAVLQERR STHRVRAHFS GSSREAIMSD MEEFLSKYGK ATGDNIGHVP
     KLVNPRERSG ILGVFTGQGA QWPAMGRELI HSSPIFRRTI EECEDVLADL PEKNRPQWSL
     IKELTADAST SRVAEAAISQ PLCTAVQLAL LSLLTVSGIK FDAVVGHSSG EIGATYAAGI
     ISLKGAMQIS YYRGLHAKLA SGTDGKRGGM MAAGLSPMQA REFIARPDFK GRIGIAACNA
     PRTVTLSGDL DAIAEAKLVL DKDNVFAREL KVDTAYHSHH MLPCAEPYLQ DLLACDIEVK
     QPQQGQCVWN SSVRGDTQLL RGDLTSLKGQ YWVDNMVRTV LFSQAIESSI WHGGPYDLIV
     EVGPHPALKG PAEQVMKASY GSVPVYTGVL DRKKTAIDSF SAAIGLTWAQ LGPGFVDFTN
     YRNAFYKSNT SPPVRMIKDL PTYSWDHDKV YWREGRMSRR FRLGKDTSHE LLGRRTLDDN
     EFELRWRNVL KLNEMPWLRG HTVLDEVLLP GASYVSIAVE AGRYLAADAD KNLGVVEVEN
     IEILRPVVVP DNNAGVETLF TARLVEKSKD VIKARFSYYV CPDETVGSML QTCMGDLIVH
     IKSETISNGS ALPPRDQTPP NLANISNEQV YSLFNSIGLS YTGAFKSITD INRCLNYAST
     TSTWEADTLG DKYMLHPAVL DVAFQTLFVA KAHPASRQIT SALLPSHIDR VRVDPSVQIV
     RPGVSKAEIE TWAISQTATS LRGDLNIYDS ASGATFLQVE GLAVNMVGAV EGASDRSMFS
     KTIWGNDASL GLLDPKRNEA QDEKGMKMAD AVERVAMFYV KRIVDQIPPS EREEFIWYHQ
     RMFEAFEEHI RVVAAGEHPI IKADWLNDDV SILKTIDAQY SEEIDIKLLH AVGGHLAEVV
     RGNEQLLEVM TKDDMLNRFY MEGYASITTN KFVGDIMKQL TFKFPRAKVL EIGAGTGGTS
     WSILNAIDDA YDSYTYTDIS SGFFPNAAEK FSSFSHKMIF KVLNVEDEPS GQGFEDGSYD
     IIVAALVLHA THDLKRTLHN TRKLLKPGGY LVLLELTGIA SVRATFIMGG LEGWWLGGDD
     GRRLTPLVTT VEWDNVLQDS GFSGADTVVY DLPDEAKHCT SVIVSQAIDD EFLRLREPLS
     CKSDFPSLTD PLVIIGGKKF WTSKVISEVQ KLLPRSWKRQ IKLVKSIDKI DASNLPSRMD
     VILLQDADES VFATTIAQPQ LNNLQAILMR SKNMLWVTTS GKSHAPRASL IQGITRVIPA
     ELPHLNAQLL GMPSEQTPTS AANHTVEAFL RLIQGEDVAR DGKILWAQES ELEISADGKT
     VIPRVIPDET LNETYNGSKR VISKNVDATE LAVCTEVVDG KVAMLSVDEQ DEGDGVRVDV
     HSTLHLPGFD DQSIYIIFGK TDSSWVVGLS HTNCSVLYLN SEILVAVKED TTHAQLASIA
     FTILARSIAV ISSTGSPVLF YNVDESFVRI IASEFGTRQL QAQFATSRAE APTDWIKIHP
     LASQRAIQRA IPQNTAVFID CSAGTASMAF TFTASIPANY QMCRLGSGLL SKALEMSKMT
     TATFLGQCIE AASNQKVPET EVIPASDIAG SNASVLGLRT FITDWTDKTA LPITVKPLQA
     QTLFKPDRTY LMAGMAGGLG LSICEWALRN GAKHMVITSR NPQLPKATLQ EAHRLGATVK
     VLPMDLTDKL SVKAAVAGIE ESMPKIAGVC NAAMVLKDGF FIDMDAEQLN NTLAAKVLGT
     EHLDSIFHDT DLDFFICLGS VASVIGNVGQ SNYHAANLFM DSLINQRRNR GLAASIIHIA
     YVTDVGYVTR EERDRQLDSH FRKVRLMPTS ETDVHHAFME AIRGGRPDSV SGSHDIIMGI
     EPLTEPVPLD QQPLWMKDPR FGHFAPPSSV HYQQESGAAG SAGNIRQCVE EADGDEQAVA
     AVIQAFCGKL ETMLQLASGS VNVSRPIIDL GIDSLVAVEI RTWFLKELGA DIPVVKILGG
     DTVEQVSTLA TKKLMARILE TKAAQPQEVK PKPEPEKAAP VPVPAIQTSL ESSAVPSASS
     QSVASSSRAS RDSSPSATSR SDTSATKQDM KSSTILTDDS SSDTGSLDLV REYPMSHAQS
     RMWFITQHSD DPSAYNMVFR YQVKGQVSTT RLRHAVSTTA HHHEVLRTCF FARVGDGHPM
     QGILASPRIK LKHVAIEQDA DVDTEMKRLS SQSWDLERGD TFELVLMSRD SENHELFVAY
     HHILMDVVGL GIMIRDLNVS YQMKLLNRNA ASYLDYSSTQ LSRNELYQRL SFWKSEFATF
     PEPLPLLPMA SVTTRPNNTS NNCHHQYREI RPDQFQVLAS TCQRLRISQF HFHLAIFQVL
     LARYTGTEDV CIGIVDANRS DPKFAETVGY FVNMLPIRAS ITQDANFSEI ARSISQKTLK
     ILSESALPFD VLLNELQVPR SASRTPLFQA ALNYRMGSIW EMPFGDAEMK LSDVKDADNP
     YDLSLGIAET PTGCVVELYA LASLYSEDAC ATILESYIRL LDAFSQTPDR TVDGVGVHEE
     TQVVRAIELG SGPVVEYEWA PTLSQRFRDI VQLYPDQLAI KDSCMELTYS KLNDRVQNVA
     NTLLHEGFTE GSCVAVLCEP SLDFVISMLA ILHIGGIYMP LDPALIIYHS ATEGRANILR
     SVGNTQFQEV PLDNIDHDSS VHVACTAKID APAVLLFTSG STGKPKGITL SQANFVNHLA
     LKNDLLRLEQ ETVLQQSSLG FDMSLIQTFC ALTNGGRLVI APSDLRRDPV ALSNLLSQEQ
     VTLTIATPSE YLAWFRYGYA SLVENQGWKH ACMGGEQVTR QLKNEFARLG HAGLQLTNCY
     GPTEITAAAT FQTILLSDSD NNDDLAVGKA LPNYSVRILD ASGQPQPLGH IGEICIGGAG
     VAIGYLDLPA ETSRKFVADS NGQRFYRTGD RGRLLPNGTL LYLGRLEGDT QIKLRGLRIE
     LEEVEAALVK ASDGLFAGAV VSRHGDVLVS HVTLVAGNEM IDQERVTQIL SSVKLPQYSI
     PASIAVLSTF PTTPNGKIDR KAIAATPASE SSSTMPMEKM TVREGELRLL WERVLVTSTR
     IAPSSDFFLL GGNSLLLMKL QAAIRETMMA PVSTRVLYQA STLRGMAQAI DKLRQERATG
     DIESEIDWDA ETAIPQWLVR QLDGATSSQK GRAPKTMGIE IMMTGTTGFL GGHLLQSLLA
     SEAVNKVHCI AVPADYEASL PHNEKIIHYS GSLLSPTLGL TSEQREELAK TIDVIIHAGS
     NGHCLNTYDS LRTPNVESTH FLASMAATKR IPLLFLSSNR VVLLSGNQAP PPSSVSEFYP
     STDGLEGHMM TRWASEAFLE KLAQHVQNTG SYWPVSIHRP AVVVSGQAPN SDALNAILRF
     SISMRCVPRL DRVEGYMDLA PLDKVVAELS EAAINLAQGQ SGNVATIQFK HHSSGVKVSA
     SKLREHLEGS YGVQFEELEL RQWMDRAAVA GMDPLITAYM EGILENDAPM VFPYMGELGQ
//
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