ID A0A8U0ATW2_PESTX Unreviewed; 2694 AA. AC A0A8U0ATW2; DT 12-OCT-2022, integrated into UniProtKB/TrEMBL. DT 12-OCT-2022, sequence version 1. DT 02-OCT-2024, entry version 12. DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM}; OS Pestalotiopsis sp. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis. OX NCBI_TaxID=36460 {ECO:0000313|EMBL:UPN67564.1}; RN [1] {ECO:0000313|EMBL:UPN67564.1} RP NUCLEOTIDE SEQUENCE. RA Li J., Zhen H., Chen Y., Liu L.; RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MW373492; UPN67564.1; -; mRNA. DR SMR; A0A8U0ATW2; -. DR GO; GO:0004312; F:fatty acid synthase activity; IEA:TreeGrafter. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:TreeGrafter. DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt. DR CDD; cd05274; KR_FAS_SDR_x; 1. DR CDD; cd00833; PKS; 1. DR Gene3D; 3.40.47.10; -; 1. DR Gene3D; 1.10.1200.10; ACP-like; 1. DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1. DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1. DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR023213; CAT-like_dom_sf. DR InterPro; IPR039551; Cho/carn_acyl_trans. DR InterPro; IPR042231; Cho/carn_acyl_trans_2. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd. 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; IPR049900; PKS_mFAS_DH. DR InterPro; IPR050091; PKS_NRPS_Biosynth_Enz. DR InterPro; IPR020806; PKS_PP-bd. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR006162; Ppantetheine_attach_site. DR InterPro; IPR016039; Thiolase-like. DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1. DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1. DR Pfam; PF00698; Acyl_transf_1; 1. DR Pfam; PF00755; Carn_acyltransf; 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; PF21089; PKS_DH_N; 1. DR Pfam; PF00550; PP-binding; 1. 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; 1. DR SUPFAM; SSF47336; ACP-like; 1. DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1. DR SUPFAM; SSF53901; Thiolase-like; 1. DR PROSITE; PS50075; CARRIER; 1. DR PROSITE; PS52004; KS3_2; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. DR PROSITE; PS52019; PKS_MFAS_DH; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 2: Evidence at transcript level; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 9..435 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" FT DOMAIN 926..1233 FT /note="PKS/mFAS DH" FT /evidence="ECO:0000259|PROSITE:PS52019" FT DOMAIN 1989..2064 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT REGION 926..1058 FT /note="N-terminal hotdog fold" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT REGION 1078..1233 FT /note="C-terminal hotdog fold" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT ACT_SITE 958 FT /note="Proton acceptor; for dehydratase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT ACT_SITE 1146 FT /note="Proton donor; for dehydratase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" SQ SEQUENCE 2694 AA; 295619 MW; 1D4D2496E0DCFAE7 CRC64; MRFDDESSTA PIALVGVSCR LPGGANSPEK LWTFLREGGE AWSPVPAERF NETSFYHPSA DDPNGTSHHR GGHFIDGDVR DFDHAFFRMS PQQAMAMDPQ QRILLEMTYE AIESAGWSRE SIASSETSVH AAMFTTDYDR NLYKDTLDLP VYYITGTEKA ILANRISHYF DLHGPSVTLD TGCSGGLVAL HQACQSLRDG ESSASIVASA NLTLNPDHHI GMSNLHLIGG SGRSFPFDDR GTGYGRGEGF VVLALKRLED ALRDRDPIRA VIRGTAVNQD GYTPSGITYP NGSAQADLIR SAYKRCGLQP KDVSYVEAHG TGTVAGDTEE LNALADVFCS STRSLPLYVG SIKGSIGHTE NTSGLASLVK AALVLDRQEI PPVAGFAHPK PGLPLDKLQI PTELIPLPIA TDITPTVSIN SFGFGGTNSH AILQPGPRSL PPCNDTAPCL FILSAHTEES LKSMIQTFTD WLENEPNVSL ADLSYTLCHR RTLLASRWGC VAEDRVSLLD QLKRRLGKAS SRMDRSEPYI VFVFTGQGAQ WATMGRELLI GSSKSSIFRD SFRTSQDIIK RLGAPWDLEQ ELLRDRAQSL LHTAQLAQPM TTVVQIALVD LLRAQGVRPR VVLGHSSGEI AAAYAADRIS HDAAIQIAFH RGSVADLYKS RDLRPGAMMS VGLSESDIGP FLQHLSRGKA SIACVNSPTN VTISGDAVAM DEVAARLEEK DAGIFHRSLN VDTAYHSHHM EAVADIYLDR LRPLATERDT RAGDNSIVFI SSVSGEIKTC DFGPAYWTSN LVSKVRFCDA VQTLARYRDL DGPGRSIFFV EVGPHPALAG PVRQSISAAG NSPIEFDYQP TLERKKGAAS TFLGLMACIF EHGAKLDVKS ISSLAPGLQT ASVLTNMPHY AWDHQTKHWH ESRVSHQYRT RRQPYHDLLG VRSAESTSIQ PRWRHMVCLA TLPWLAHHIV DGLVIFPGSG YLCMASEAMR QLTSENFPLK QLETLAFHDV SFLRALIIPD MPQRVETQLS LVPQPGLEYG FSFQIAAFTD GHWNEYCSGL VEAVLIDNNI LVGLAPVDSF LAQQSEFVGE AIDHEELYKG FSEVGNVYGP SFNGIRSFTV ASDASQALST VTIPDVASIM PERHQAPHLI HPSTLDILLH TALPLVERRP GRGSVMPTHV DELLVSGTDA MPRGPGSVLK ALTTLKSSGN RTSHADIFVE SELVPVLVAS GVEMRSLGDK NIASLDSTVT EGICYKLDWI PDVDFINKDA SPSPARLEDA VGNYCLKNTS TSVLELGTGR REFSLSFVTA AIAHRCRLAA FDFSDADMEH RLDIQELLQA RSVPSRVRNT GDILSEAVSE LYFYDIILVA NDESLKQAST LLKPGGRVFF QIGCLDTEKN IGSKMLQEAA SPLEVESICC DQDGFTTIIA TKPKNNNIKR LPERICMLRK SHEQSISSWA QNLQSLLHGL SPGFTSTTFD AGAVNAENEA ETCFLVIDDQ AEPFVSDPHY FEAVAELLKK GTRILWVSPA EPLSFHQIVG VARTAHAENE HLRMTTIHAD IEMLESQQLS NMIGSCLEHF TVQSDESVRE REYWMRKDGS VLIPRLLAND QLNLAVNNHQ GQFGIEDCYF AGSDHPLVLS SDSPAKKGLF VRDDTFSTPL AADMVQIETE AFTMSEAHLT RDFGDSMVRA MIAQDEISGQ WVNDHVSYVV AGGLGDLGRR LLTLMAQRGG KHLVTLSRKV PEDNDQNALQ ARLEAIQPGC RLYCLQCDLT SERSVQQAAA TLRDVGIPPV RGVINSAAIL QDRPLSTMTY DEFSLASMVK VQGTMALERA FKTASLEFFI MLSSAVNIVG ASVQANYNAG NAVQDALAQA RQKDTCCYVS LNIGWIEDAV HTAENDARLR GLGRSGLRAI QHDELLRFLD HALGCSEARH HVPQAIIGFD AESLSKAISH NGNIQSPMFS HVRRNFGATL PGTETLTPTS KVASFKEVVA SGDDEMVLDF ISAAICDRLV KLISVDVSRI DDRHGSLLEL GMDSLVAIEL RNWLMREFDA PIQSSEIMDD QTIRALGEKV ALRSRIVLAH RGSADQDVQE QVNMPQHGAI SQSDATATNS NGWCQDSNLP LLPIPALEDT LRRFQESRRA LDSPKEQDTT EKAVFAFLEG PGPSLQQKVE KSSPAEMSDN WEEELYLQRR EALQDYSEFS VGHPVDAPAQ TQSLRAAILT VAAARYAYEL ISGQVPPRSH HGQPVAGKAH DWLFWSTRLP GAYIDRMERH HPTSSVIILR RGHIFQLTLP GVGAHLDLSA VHAAFEQAIG LSDIPLPDVC TLTASDRRAW FQAREELEAN PENSSILAAI NSAMFVVCLD DESPTTSGER HTQFLIGSPE QPFTNRWLDK TVQFVVAANG LSAGVYEHTK LDLLDVRALH QRVNHEIFAH HDMESVTPSS VCPLRKHIWR PSPVMLKRIQ DLKFQLKSYH YVDHQYVTFE SLGTRSLRAL RASPHATAHL VALLAVYFVD GKIRPAWEVV SLGSFLHGRI DWVQTVSPAV RSFLEEASAA IADGKSGMVS HDKVSHLRPL FDAASTSHAR AVSDTSRGLG FVNHLYALRG ALKRDPSVTD EASPELFRTR IWNATRRGGA EQSLKIGFVP VQESDHPDAW DEGGFLMHGD RGIYIHSSVH GHCMKFAVSA HPDYAIAVCN TLQTASNLVL SILG //