ID A0A1Y2UG44_9PEZI Unreviewed; 2414 AA.
AC A0A1Y2UG44;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTA81918.1};
GN ORFNames=M434DRAFT_85057 {ECO:0000313|EMBL:OTA81918.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA81918.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA81918.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA81918.1,
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).
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DR EMBL; KZ112631; OTA81918.1; -; Genomic_DNA.
DR STRING; 1001938.A0A1Y2UG44; -.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 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; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; SM00829; PKS_ER; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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.
PE 4: Predicted;
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:UP000194361};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..436
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2331..2407
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1409..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2414 AA; 263336 MW; DA9AB45341313340 CRC64;
MAQSKHHQQE PMAIVGFACR LPGGNNTPQK FWDFIERGQI APRNVPKTRF NFEGHYDGSL
KPKTMRQAGG MFLGDIDPAD FDAGFFEVGG AEAVAMDPNQ RQMLEVVFEG LENAGIPLEK
LDNQPVGCFV GSYAADYADM QNRDPEDRPP NNALGVGRAI LSNRLSHFLN IKGPSVTLDT
ACSGSLQGLD LACRYLQSRD VNAAIVATSN LYMSPEHLID TGNIGSAHSP TALCHTFDVA
ADGYVKAEAV SAIIVKRLED AVRDRDPIRA VVLGTATNSN GRTAGIASPS STAQAMAIKA
AYTHAGITDL NLTTYLECHG TGTQAGDPTE VNGVGSVFAA SRPADRPLII GSVKSNIGHS
EPAAGISGLL KAILSIENGF IPGMPTFINP NPKIDFLGNK VKAFRAGIPW PADAPRRASI
NSFGYGGSNA HAIVEQPKAA DRAHYVSSFA SADEEFTLLE EDAARPSVLV LSANDAASLR
ANIQSLGNHL INPRVKVSLS DLAYTLSERR TRLWHRAFIT TKNTELDEKP DSWFVAKKNS
HTPTFGFVFT GQGAQWPQMG KDLLQYFPWT RTILEELDGV LQSLHSPPSW SLISELTEPR
TAEHLRQPEF SQPLVTALQL CIIAVLESWG IKPRSVVGHS SGEIAAAYAA GLLDRAGAIT
AAFYRGRAAL NRKNEVDSDV GMLAVGLGAE AATEFIEKHG SGQAWIACFN SPNSVTVSGK
IAALETLREA ITAAGHFARR LQVDLAYHSQ LMDKIGEEYE DLLSTESQFR PTEKNLDGDV
ALFSSVTESK RTTPTDALYW KTNMVSAVRF HGALKAMLED EKAPNYLIEI GPSGALAGPV
SQVLKSLPTA VAGEITYTSS WSRGANAGKA LFDVAGRLWV AGAPIDMAVV NEYDGQERTI
VDLPNYNWNH STKHWHENAA SKDWRFRKYV VHDLLGSKIL GSSWRNPTWR HRLNVANVPF
LMDHRMGGDA IMPGAGFITM ALEALYQKHC ALLQPEEAAG IARNDLCYRF RNVRFSRALV
LEEGKDVIIT FTLTAVPGDK HWHEFRISTT EDDVVSEHCS GWVRIHDAID EPVEGEDALP
LKSPQAPKLW YKCQREIGME FGPAFQKLIE VEAVTGERKC RTLISLEPAE SKYNPQSYYP
IHPAALDGCL QTVVPSNASC DRTNVKHVMI PALIDDFIIN KVPARLYRGR SKATSVYGGR
GRLDIEKSWV ANTTVYDSET GQLIMQINGL NYTKLDVAPK PDPHTFHSVT WKPDITFLTQ
DQMMYLATDK DSNKLDTVID LIAHKKPALK VLEVNLDDED TSCFWFGVND FSARSAYAQY
AFGSSNAKTL VSTEAQYKDK GNVSFHSISP ENPAFGLPTD VAYDLAIVKA SEKVTSESVE
DSVKNLRPLL SEGAYTLLVR IDQEGVVTRA ESESSGSFEN LNRPSALGTP GTPSQSSDSL
VASSISSAAW DEEAAKKSLN VTHAHATSAV LEVAPTGNSP LAYLSKLNSS TGVVTNSPKH
LIVVRLSETT PASLPPSLQA TLEASGWAIT QQSYPFSKPT NGAVVLILDE LSKPVLKYVN
EKQWETIKGL VTSGTPLLWV TKGAQYPVTD PDNAMVHGLF RVARQEDPTV KLTTLDVQSS
TSAATSWAIE KVLGVLKDGT SLETEYMERN GILHVQRIMP DTLVNDFRHA EEEGLQPVTK
AFHGTEVQVQ LRAERLGTLQ SLMWCETETG EAPALDEGNV EVEVMAVGVN FKDVAITMGI
VPDNEYNIGF ECAGIVKRIG HGVTKFKVGD RVCMLKAGSY ANRVRVSVDR CHVIPDTMSF
EEAATIPSVY LCSLYAMYHL GNLKEGQSVL IHSATGGVGI ACIELAQYKK AEIFVTVGTE
EKRQFLESNY GIPRSHMFSS RNTKFAREIM KATGGRGVNV VINSLIGELL DASWRIMADG
GNMVEIGKRD IVDRNTLSME PFDRNCSFRA VDFSYTKDIK DSLVASLFDE LFVLIDGGHI
KPIHPITTFG FDEVQKALAY IRSGKHLGKI VISNGEREDI QVPIRPAIRG LQLRPDVSYL
IVGGLKGACG TLAIHLAQYG ARHLIISSRS GINDEASARI VASCNFYGCK VTEAKGDVGN
IESVRQLFKS ASPRIAGVIQ GAMVLRDKPF EMMTLDDYHT AIHAKVQGTW NIHRAAQEVQ
KQPLDFFTML SSTSGVVGNK GQANYAAANT FLDAFASYRQ TLGLHANTVD LGVIEDVGYV
AEQDTGLEAR FDKRQWTPID ETMLRKILTY SILQQDSTPL NADSATEMIT GVGFPLPQDG
SELAREPRFS YLFNSRGGSK IGLDDGDESD QTEQAIKQFR LMHKSGADVA ALKLTCVEVV
SAQFAKILRL ETEPEPGRPL VAYGLDSLSA VELRNWIRMK LGVELTTLDI TNASSLIALC
EKVVSKLPQP EATA
//
