ID A0A072P434_9EURO Unreviewed; 2527 AA.
AC A0A072P434;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEF54616.1};
GN ORFNames=A1O9_09058 {ECO:0000313|EMBL:KEF54616.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF54616.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF54616.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF54616.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEF54616.1}.
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DR EMBL; AMGV01000009; KEF54616.1; -; Genomic_DNA.
DR RefSeq; XP_013257206.1; XM_013401752.1.
DR STRING; 1182545.A0A072P434; -.
DR GeneID; 25283968; -.
DR VEuPathDB; FungiDB:A1O9_09058; -.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; 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; 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; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF46; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 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; 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; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 55..477
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2442..2517
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2527 AA; 276810 MW; 0B5096332C121DB8 CRC64;
MGDIRNGHSN GHVNGDSSIG EGHVNGHANH GSGNRINCHA SSNGVPIPDA DGPIPEPIAI
VGMSMRLPGG ICTEDAFWDL LINKRTTRGP IPHSRYNYEG FYTDSGKPGS TCVRYGHFLD
DSDAIDVLDT SFFNVSKAEV EKLDPQQRML LEVVWECVEN AGQSNWRGSN TGVFVGAWGY
DWIDFLAKDP QQVGGMLNTL GSHDYTIANR VSYEYDLQGP SMTIKTACSS SLICLHQAVQ
SLRNAECDAA IVAGTNLILT PTTTMEQTES GVLSPTGECR TFDAAANGYA RGEAINALLI
KRLSKAREDN DVIRAVIRST AVNSDGRSAG LTTPSPKAHI RLIKGAYQSG RLSDPSETPY
VEVHGTGTKT GDPLELEAIS EVFGSTNDTY IGGVKANVGH SESASGVTSI IKAVLSLENR
IIPPQANFST PNPKIPFKEA RLVVPLEPTP WPEGRPERIS VNSFGITGAN AHAVIESAAS
YEGATGVTGS NGNDEGSDSE LLLVSATNTQ SLKERCGQIQ DYANEHPRLL SDLAYTLASR
RDHLSHRAYS IRTSPDSAEF ITADRSRQVP KLNFVFTGQG AQWPAMGKEL IESFPTFRED
IIQLGNVLKT LRDPPSWNLL EELIRDESKS RVNKAEFSQP LCTAIQVALV NLLRLLGIVP
SGVVGHSSGE IGAAYAAGAL SPEEAIAVAY YRGLITTQST RKGAMAAIGL NQPEARLYLE
NGVVIACDNS PQGVTMSGDE DALDRIIEHI NLDDPEVFTR RLKTDGMAYH SHHMADIGPI
YEECLRPIVK GRAPASGFFS TVTGKLTGSS ILGPQYWRQN LESPVQFYPA VRSMLANGTS
DQLFLEIGPH SALAGPLRQI FKASTSKARL IYTASLVRGK NGRQCVLDLC GQLFLQGLPL
TFQALTTGSS LLTDLPIYPW NHDTSYWSEN RAVKDWRLRK FPRHELLGSR ILEGNDVEPV
WRNLLRLKDT LWLGGHKVYG DVVFPFAGYI AMVGEAVRQL TEIDAFTIRN LSVKTAMVVQ
EGSVEIMTSL RRAKHSLESE KGWYEFTIVS HNGSMWAEHC DGEIRAGDFE SSVYAQEILT
APLPRKVPSP YDLFHSVGLH YDGSFRGLVD VSAMPGEKTA IGSLKTPATT DSPYSLHPAT
MDQCLQLLGM ASSEGLSRHL QRIPLPTFVQ RISIQPCKSR EVLRAKAVAT HISDQGDIQG
KMLAMQGPTA VLVVEGCHLS AFAEEEEAVL DDPVAAARAS WRPHIDFVPL ETLMISEEKD
VNEVKIIEEY GLLCSAEILE RIETTRDSNW HFTKFRKWMS DVVTGGRLGE NKIVSNSKEL
LELDRQERME LIHDLEEKLR TSPFIHVAEL TTRLLDNCVG IFDGTTEVLE VYRRDDTLTK
LYALTGARID SSEFFVTAGH SNPTLRVLEI GAGTGGTTLI SLTALTSINK EPMYSSYTFT
DISSGFFAAA KERFREFPGL EFKILDIGRD PADQGFELGT YDLVIASNVI HATEYIGATL
KNVHKLLNPR GRFFLQEVIP SSVKMKNLIM GPMPGWWLGE ADGRLNEPII TVERWSKELS
EAGFSGIECA VLDDPKNDSA FGANMIAKPA VNAQEYKSVT ILIRPDQVDT DILKLVQHVF
EKNEYYVDIC HLGNSIPPSQ DIISLVDTDK PFFDQLTAEN LAAFQKIVTE LTSARMLWVM
GSAQIKPSNS LFGIALGIIR CIRAEMSIPL GTLEIDQFDT GTSNTILTVF EKFLDTTPAI
GNADYEYVID DNVVKVGRYH WTTVSKELEA SQDLDNLPLK LGFEGSRASK LVKWTPQPLI
TLQPDEIVVH PMYVGIGPKV ILCCTVVRFS ANKVPQDFVT LDENTIRDYC GEVVEVGSDA
SGLNIGDRII GLGCCGVQTS FKTLATSVTK VPDDLEIEDA ASMPLAYATA FHCLRDLAGL
KKNQTVLITD ADSAVGLAAI RICQMIGADL YCSVHGYEQA DFLNEFGVRK VTVMATHNWS
ALIELAFENN KTGFDVILNV LSENLGQLCK CVAPRGKLIN LGCPTAESLD MKAFANNKTL
YNVNMGEMDD AYPRLLQEII SMVQQKQIVP IRPIRAIELE ELDAALRSSN KQDSIGKLIL
RLPKERTSLP IQPAPPTLKF RGDAAYLIAG GLGGLGRATS NCMAEHGARH FIYLSRSAES
SSLHQSFFRE LEAQGCSFQA ISCDITSYES VGKALQQATL PIAGVLQMAM VIQDRPFLSM
SHDDWVTAIK PKVDGTWNLH SALRDAKIDL DFFVMFGSSS GAFGIPGQGN YAAGNSFQDA
FVQYRHSLGL PASVLDIGVV SEVGYVSENK DILDYFRTAG FPILTEGQVF ETLHLSILQQ
YPLGEDKQTA AASAINPGFT SRSQLTLGVR ATKPMTDATN RVLFKRDRKA DIYRNIQAAR
MNSSMAGATR AGSGDEVASL MASLRDAADA ESVLIRPETL KLLRREIGAF IYESMLQSVD
EEEMEFGRSL MSLGVDSLVT IEVRSWIRRK LDVEVSTLEM LNGGTIENLG ELVLERMKGR
YAEKAKA
//