ID A0A072NZW3_9EURO Unreviewed; 3191 AA.
AC A0A072NZW3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEF52558.1};
GN ORFNames=A1O9_11401 {ECO:0000313|EMBL:KEF52558.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF52558.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF52558.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF52558.1,
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 -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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:KEF52558.1}.
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DR EMBL; AMGV01000017; KEF52558.1; -; Genomic_DNA.
DR RefSeq; XP_013255148.1; XM_013399694.1.
DR STRING; 1182545.A0A072NZW3; -.
DR GeneID; 25286299; -.
DR VEuPathDB; FungiDB:A1O9_11401; -.
DR HOGENOM; CLU_000022_31_2_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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; 3.30.70.3290; -; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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 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; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF22; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF00755; Carn_acyltransf; 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; SSF52777; CoA-dependent acyltransferases; 2.
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; PS00440; ACYLTRANSF_C_2; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 3: Inferred from homology;
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 4..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2527..2604
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 472..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2610..2629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2950
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 3191 AA; 350622 MW; 0562BBC635536779 CRC64;
MADLEPVAII GIGCRLPGGV GNAEDFWRLL SEGGSGWSVV PKDRWNVDSF YHPDGTSIQS
YNTKSGYFMS QDVTDFDSRF FGFAHHEADV TDPQQRILLE TTFEALENAG IPMESIKGSD
TAVYAALFAR DYDRIGYKNL EGLSQFHIPG TGEAIIANRV SHFFDLRGIS MTIDTGCSGS
LVALHEACTA LRTGQSRIAI VGGTEVLLHP DQNVIMSSGG MLNPDGKCYT FDSRGAGYGR
GEGVAVVIVK RLKDALADGD TVHAIVRNSG ANQDGKTNGV TLPNPDAQEA LIRRVYGDVH
LDPAETPYVE AHGTGTKAGD VAEVQSLGNV FTEKTRTRNL YVGSVKTNIG HTEATSGLAG
LIKSILVLKH QQIPPNLNFI EQKPGLNLDE RQISVPLDLV PLLPEGSKGA HRVSLNSFGY
GGTNCHVILE SLDQYLSDHI GYLTKGAVNG AVNGAVNGAV NGATNGIVNG ASGHSATNNS
EKNGVQLANG TNGVNGSHGS NGAEEKSTAA AEGMPLIFPL SATSEAALDE MPAQIQKWLS
GPDDSTSDLS DLSYTLACRR SLFKWRKAFV ASDVAELTAA LGEGKISKTR SAPSAKVAFV
FTGQGAQWAG MGVELIGSSQ VFKSSIESSS QLLKSLGCGW DLVQELSKSA AEKSRINESE
LAQPLTTIIQ MALVDLLSHY DVKPNFVAGH SSGEIAAAYA AGALAREAAV KASYLRGLQS
AIAKKLNELP GSMLATGYGE QAALQTIKAA NFDSEMGRVV VACVNSPAST TLSGDEPAMH
YVSEMLRTGG VFIRKLKVET AYHSHHMEKV ASSYLKSLEG LSSTETKSDV EFHSSVTGQM
KISDFGPTYW VENLVSQVRF NDAMTALLKS MAATGPPDAA NILIEIGPHS ALQGPINQIL
NSIPGFKSAY MAPLSRGKNS ISSFSAATAR LFELGAKVNF EKLFTKPRRV IDNLMPYPWD
HRVKHWAESR LSRDHRLRSF PYHDLLGVYD VMSPIEEPRW RHHLSIQRLP WLKDHVVDGM
TIFPGSGYSA MITEAMKQLV QLKKPDSEAK IANTIIRDVR ISRPIILPVE STDGPGDDIE
VQLILSPSKI SDANPWYSIR ILSLQSDGTW AEHVSGTVRA ELESASVTGK ERKATVDEAF
EAFERIQSRA QEKMNMETFY DERRAAGNDW GPNFALLYEA HIGPWVGFSK LRIPDMAQCM
PAGYFQPHLI HPTTLDASNH MVPAVFHREI KNAPLMPITT EEVLFTNNLS SKPGDEMIVA
MELKAEGKSQ ARGDVWVFQN DSVTGEVMFV SSMRGLVMRA VGEGASTDAS KPFQRKHNYQ
VYWNDDPDHL DKASFARLVE PHFPKNSSLL KQLSTIEKAT AIYLNRVKDM PVIQNPETAP
LFYLRDYSRW ISDYVNSDAC RKICESLSDS EQAEVLDRSD SSDIEGEMLG RVGRNLADIL
SNTADPLELL VADDLFERFH NQGPLTPLYQ QLVQYAGLLT NKNAQMDVLE VGAGTGSATL
PLFNSMGEDA SDLVKKYTYT DISSGFFETA KERLDRWKSI IEYRTLDVSR DPVDQGYEAN
AYDLVVASNV FHATKSIRET LTNVRKLLKP GGRLLFVEIN NSTAGASRSL GTIFGTLPGW
WDSVDGREGS PLLTPDQWHE QLLQTSFGGI EYSSQDCDGP LARASFIVSK AIEEQKPSDT
ASLIDSVTVI HNPVSPVGQS ASTTLTSAFQ QKGFSSSVNY SWEALAEVDA EACEGTMYVV
LDSANSSVLE HPTQEMFDRY QNLLVNCRNL IWISFQEEGG LKEGSIKGLA GGLARVVRRE
NGGVKLITID VRNVLGTEDD VSRFVQKVQD VALQLLAPDV NNRATVDEEF ALDGDKLLIP
RAYADKKFNN WTDLVNGRGD LSLQPFKNPA LPLRMEVGAP GLLSSIHFVH DTDASSPLGS
EQIQIDSKAF GVNFRDVLCA LGQLQNGSFM GECAGVVTAV GSGEFVQRTY KVGDRVVGMH
AQPFASYSRL NGYDAHVLPD DISFADAASM QVVFTTVYYS FVNIARLEAG QSVLVHYGSG
GVGQAAIQLA RHFGAEVFVT VGSEEKKQFI LDHFNVPESH VLSSRSSPRD LKRHLLRLTQ
NKGVNVVLNS ASGEMLAESW DCVASFGFHI ELGKTDIDKN THISMAPFKR NVTFSSVDLV
TIAKERPKVF YDVLDKTIAL FAKGVLKPVY PLNKFPIDQL ESAFRLISER KHIGKVVLDC
EHEEKVQAVL PAPALTKLQS EGTYIIAGGL GAIGRMLVTH LASRRAGNII TLSRGDLADE
ERIPWQAEIA KLGAKLHVLK CDITDESSVQ KVAEYCRQSL PPVRGIFHAG MVLRDRPLAK
MTGDEWNAVL GPKVRGTFNL DQAFSSPDLE FFVTLSSIAT TFGNPGQGNY SAANAFQDYF
VTHHDRTNPT RYVSVDLPVV DETQALAQIE LGTRSFILQV SMLFDVGELM QLMDYAMNRS
LELERPFLHA LMGFDRKSMS QGTGDDLFSA LFQTIPQMQT LSSQHPNGAD AKQDIESLLT
AANSFDEAVK VIMETAIEKF VRFLNLEADD VGPDQPLISY GLDSLVSIEL KNWMVRAFKA
TLQVSELTSS RNIAHLAELL ATRSKILPAG LSKQTQDQKP AKDESEGKTN FQEEQALLAQ
PDHAEIETLP CCPLPAKEAR QPVPNLVLGL QKHLENISHF AHSEEEVESL RSAMKEFLAP
GSVGEQVYQE IQKDARDPKV SNWISKFLSE GYYMPMRQAL QYCSFMVMNH PGPVQHTQAD
RAALLAETAF QFKHKIDNGT LEPLYILETP VCQAQLQWMF NTYRHPQIGI DEIRKTAGDY
CVVFRRGRLF QVPLRNGDAP VRFDALRATM AAILDHVQDE GTWAGILTSD TRDSWAKIRT
ELLAVSPANA HYFQVIEEAA FAINLDDSSP TNFTEIAKQC KMGSGFNRWH DKPMQFIVTA
NGQSGLLVEH SYLDGTTPAA LYDRMRDAIA AYKPTGQATP QVPSPEEIPL VLPSSLHKHI
SFLREQWLSN NALRDFISYE LPTLSGQILG QSKVPIKSGY DVLCQLAFFL YNGQRVVPNW
QPVMLSHFHD GRHDMVQMAS PKVRAFCEAV VATGEDEVPI LQKRNLMIEA ARDLSRRLSE
AKDGKGFFRL FVTIEQRWPK GQPRPRVFDD SLQKRTMEFP VSNINHNSVE SVTTPLDPHA
LRIRYTIHDD Q
//
