ID A0A1Y2V2N9_9PEZI Unreviewed; 2178 AA.
AC A0A1Y2V2N9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTA90737.1};
GN ORFNames=M434DRAFT_397722 {ECO:0000313|EMBL:OTA90737.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA90737.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA90737.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA90737.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112511; OTA90737.1; -; Genomic_DNA.
DR STRING; 1001938.A0A1Y2V2N9; -.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
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; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 385..803
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1663..1737
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1638..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1743..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2178 AA; 238409 MW; DFF5186139EFCD89 CRC64;
MGERLRGPLP GPTILLFGPL ALSFDETAFS QVRKIVVENE DSRWALDTIA EFPQIWKSLT
ASIPSLKTSS GLKQLEDLSD AFRTGRPLET PFPLPNKLLI PLVIVSHLTQ YAAYLRNSTE
EQQVDPFSTS KLDRETLGLC TGLLSAFAVS SSENSEQFKK YAAVAVRLAM LIGTVVDAQD
EATEPSKSLS AAWNSVEGGE ELKRIVKSFP ETYVSVNYDE NRATVTTKAS TILKLQQQLR
GAGLIASEVS LYGRFHADVN LEKLGLLLDF VDAHTEFQFP NASSGLAVPT RSNRGGDLIV
QGPLHHHALQ SILAEPPQWF QTVCVVRDET LKNKDSAILS FGPERAVPPS LLRGLNPQVF
HVADLDGMTS RFETFSQKEL RTFSDNDVAI VGMSIKVAGA ETLDDFWDLL VSAKSQHKEV
PKERFSFETA FRDVDPKRKW FGNFIENYDK FDHKFFKKSP RESSTMDPQQ RHFLQCAYQA
VEQSGYFQSA EPESRVGCFV GVCSRDYDCN IACHAPNAFS ATGNLQSFIS GKVSHYFGWT
GPGLTIDTAC SSSAVAIHQA CRAIITGECT AALAGGTNVV TTPLWFQNLA GASFLSTTGQ
CKPFDAKADG YCRGEGVAAV FLKKLSAAVA DGDQILGVVA ATGVQQNENC TPIFVPNAPS
LSDLFRSVTK QARLKPAQIS VVEAHGTGTG VGDPAEYDGI RRVLGGPASG RDKNLLLGSV
KGLVGHTEAT SGIVSMVKVM LMIQKGMIPP QPSHTAINPA IGATPADKMT IPSSLQIWDA
DFRAALINNY GASGSNASMI LTQSPFANTK AIKDTLECPT GAKYPFWLAG LDDQSLRRYA
KVFRKFLGNK SYSSADLSLS NVSFNLARQS NRSLEKAVLF SVRSLEELDQ KLASLERGEA
SVAPIAHPES KPVVLCFGGQ VSTFIGLDQG LYQRVAALRK HLNNVDAVAR SLGAGSIFPG
IFETTPGKDT VQLQTMLFAI QYASARSWIE SGIKPVAVVG HSFGELTALA ISQVLSLEDA
VKLVVNRATL VRDAWGSEKG AMMAVEADLA DVEKILAESN QKVPEEKPAS IACYNGPRSF
TLAGSTTAID AVAATIPSSL RSKRLNVTNS FHCALVDPLV EALEQVGKTL TFRKPTIPVE
RASEFPTQER HAAKFVADHM RYPVYFNHAV QRLAKQYPSA VFLEAGSNST ITSMASRALG
NPSGSLFQAI NITNSDKAWD NLVDATLNLW KAGTPVQHWA HQASQTREHS PLLLPPYQFE
QASHWIDFKV PPKVSALPIT QKTEHEEKVP EGLLTFIGYQ DSKKRVAKFR INTMIPKYER
LIVGHVIAQT ASICPATVQL DLVIEAVRSF RPDLAAAKLE PQVHVMENQS PICVNPSRGV
WIEVEEDTSG RSPSWNFQVF STDMPQGTAK TLHTTGKVVF CSTEDLTLKL EFARLERLIG
HARCVELLQS GDVDEILSNR NIYKIFSDVV DYGEDYRSLR KLVGCGNQSA GLVVKQYNSE
TWLDAHLADS FCQVGGIYVN CMTDRAPTDM YIANGIEQWI RSPKLRPGDA RPDSFHVLAT
HHPADKQYLT DVFVFHPKTG ALLEAILGIS YVKIPKASMS RLLSRLTVGG ATVASPSSPA
KVALFEAAPT EIVPPRSIQI KEPKASKAAK TPKPPKTKKQ PKSDVASKVK EILVELSGLE
LDEIKDDSQL ADLGIDSLMG MEMAHEIEAA FRITLPESEL MEIIDMPGLM KCVQKAVGGD
AVGADEVSEQ SDDDVSSDSD AQSYSDSGSS SGHPTGLTTP AADYDKDPYD DALSTCGEDL
KLPFTTVMEA FKETKALTDD KIAEYGQTNY FDTVMPLQTN MCVALTLEAF DKLGHRFREA
KPGDKFPRIP HPKEHSRLVD YLYKMLEKES HIINVNGDTI TRTSVAAPTR SSKEILQDLL
ARFPDQTTAD KLTFYTGSNL AEVLKGETDG IKLIFGTPEG RELVSGLYAE WPMNRLFYKQ
MEDFLARLCS KLDMSEGPLK ILEMGAGTGG TTKWLVPLLA SLNVPVEYTF TDLAPSFVAA
ARKKFKPYPF MKFRTHDIEK APADDLIGTQ HIVVASNAVH ATHSLRVSGS NIRKALRPDG
FLMMLEMTGT LYWVDMIFGL FEGWWFFDDG RTHAVTHELR WEKELQAVGY GHVDWTDGAR
PENKCEKLII AMASGESR
//
