ID A0A0M8P6L6_9EURO Unreviewed; 2709 AA.
AC A0A0M8P6L6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KOS44607.1};
GN ORFNames=ACN38_g4509 {ECO:0000313|EMBL:KOS44607.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS44607.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS44607.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS44607.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KOS44607.1}.
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DR EMBL; LHQQ01000058; KOS44607.1; -; Genomic_DNA.
DR STRING; 229535.A0A0M8P6L6; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000037696; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1901336; P:lactone 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; 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; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR008160; Collagen.
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; 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; 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:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF21089; PKS_DH_N; 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 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; PS00059; ADH_ZINC; 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 Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037696};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 24..447
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2628..2706
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2709 AA; 295868 MW; 5A538F006B7E1C0A CRC64;
MPSFMNELEG NSTQDPGDLN VAGAEPIAII GLAIRAADEA TEAEAFYDFL LRARQATRPI
PEDRLSSKGF YHPDPDHGGT FYAKGASLLG ESPNGFDSAF FKMSKTEVQS LDPQQRILTE
NVYHALENAG LPMEEVISSN TSVFVSGFNR HHADRINSDL ELSFKHKPTG AENSMISGRV
SWFYDLQGAS LTIDTACSSS LVALHLARQD LAARESKMAI VSGVSVMGFL PHLMSMTYSG
LFGAEGKSMA FDQRADGYGF GEGVGTVILK PLSAAVRDGD TIRAVIRSTG INHDGHTPGL
TYPSPTAQES LIRKTYKSAG LDLKDTTYAE SHGTGTQAGD LIECTAIAAA FDTQNRDSPF
YIGAVKPNIG HLEGAAGIAG VIKSVLLLES GIIPPNATLK DVNPKIPEAW NVHFPKKCIS
WPTSGVRRSS ISAYGISGTN AHCILDDAFH FLKERDIYAP HRTRQTVPTR EEIEILLAQV
SQKYKAEGEY HNQQNSLTNG HESTTNGIHG TGNINGMNGI NGTHVVNGTN GKNGTLGASG
PNGVNGVNGV NGVNGVNGVN GVNGVNGVNG VNGVNGVNGA NGVNGCKHEN QSSNDLVLQN
RQVPKILLLS AFDETALKKV VAGVREHVAG WPLQSDNLAT QALDDLAFTL SEKRSRLAWK
SYGLCGSVQE VQDKFSEFPS KPIKSRTPLK IGFVLTGQGA QYAKMGEQLL VYPVFRQSME
AAEAYFRSLG SEWSLIEELR RESKDSRVST SALAHPMSCA VQIALLDLFI SWNLIPHRVT
GHSSGEIGAA YLAGKISREA AWKVSYYRGS VHLRGKSHAA GGMIAVGLEE EPLLLLLKKV
HAKLPGGTLS IACFNSPRNH TVSGDDAMVV ALKELLDEQG IFARKLKVGH AAHSAHMEAL
SEDYENLMGI LLSKRLLRFG HTIHMFSTLT GRLLDDTCVP EKGSHWCDSI VGPVRFTEAL
KSMCFDTTEG DGVSTRGTCV DVILEVGPHP AMQSAAKDII GSSVEIPYFA TLTRKDTGLK
TLLHTIGQLA ALGADVDLDK VNRATNPLID PNMIVNLPSY PFNHEEQGLY ESRLIKNTRL
RKFPRHDLFG APVADWNPNS PRWRHFLRVS ENPWLKEHVV GADYVFPGAG YVVMALEAMK
QIADPAELIG INLRDIVFKS MLVVPDTTQG VEVCLSFYPE ADSKTTISNS WKRFEVASYD
QTTEEWVEHC TGKISPDYKD PVNPIDTSRQ EGLEKAKWLE FVEAREGDCK DPIDFAPLHA
HLRDIDINHG ESFRNMFNST ISGRNSGLMT GDIIVPDIKR WMPKQYAHDH LIHPTTLDNA
FQAAFAAIFD LKGKKMLSRG CIPSSVREMW LSTTDLSSKA NTTLRCTCEA SPGLHDSFEI
DIHSWDPSNV SAKLFSLAGA KMAPFKPARS DENPSDDKAS YSIDWHPDLD LLSNDDLRKL
VPSSSNSTVS YQAQLESLSR LQLASTLLAT DGLLAIRGLD DSALEPHHKK YQHLLRDIAA
NISIDSVPYV PLEKWLKYSR NPGLKKQLYR EVEARTLDGQ LLIRMGSQIS AILRKDVTAE
HLLFGKDNLF YDWDETTLLQ GNILPVLDQY LNILRRSYRS LRILDVSGRT GNLAEHVLKT
LCQANDLSPI EKYVVGSVFD GACPPTKERL AAWNSIVTYK TLDLGTDIVE QGFELDSFDF
IIANNVVHTE PNMKEVFQRL NSLIAPGGRL LVFDETRPES LNSNVSFGSL AVWWQATESF
RSNGPFAPKD EYNRLLRETG FSGTDFDASS SAYTEFADYT MMASTAIKQP SQTAAPVWEV
LLILQSESEM SRLFMKRLMN AGVKYSVCEL DELDTVSVAG KTCISFLEAN RPILNNVDGS
TFSKIRDLLI ACSSLLWVMG DPLTQPEFQM APGLLRTIRW EQDRENLNLV SLSLDGEVTA
TVESNSDAIF RVFKHQFLAG PKNTNAEYRV RNQVIETNHL VKNTNANTAI DAKLLRPKPT
LFQWDQIGRP VRLTSPQPGV DSLVWNTDDN YVEQPLAENE IEVDVRAVGL NFKDLLVAMG
EIAQPGFGHE AAGVVRNVGS SVGGLKPGDR VMCLGDPSPG RMGTLRTYSR IHSDLAIKIP
ERLSFEIAAG LPVIYGTVIY SLGHIARIRA GDKILIHAAA GGIGQAAIQY AKVKGAEIFV
TLSSITKKNF IMETFGIPES HIFSSRDLSF SRGIKHISPG GVDIVLNSLS GEALRESWAC
VAPFGRFIEI GKLDLQAGSK LDMTPFLNNV TFAGVDLNAL AEERPGICQD ILKELMELWS
AESVREARPT QSLGYGQLKD GMRLLQTGKG MGKITLVPDS HPVLAMPAPL SPLTLDPNAS
FILAGGLGGI GRSIAVRLAT MGAKHLVFFS RSATVSEEGQ KTISHLKSLG CTSHVFQCDI
SDSTRLAEVF TEIKNKLPPV KGCIQCSFVL RDGAFHAMTH QDWQTALAPK VSGSWNLHNL
LPDVDFFLML SSITGIVGNR SQANYNAGNN FQDALARYRV SKGMNGTSVN LGAVVGIGFI
AENSEYAGKH TFKVANQQNE EEVLTTVEYL IDGRYHTNMT ERTAQLVCGL RTPASFSIGD
EEAPTHLTYP MFSQLPPANP KSGLAAGAEV QSVTRVRDLL QAAPTQSDAA QIIIKAIRHK
MADLLNISDD SFDDSLNART NGVDSLIEME FRTWLGKELG ATVSLKDLAK DLTQLSARIA
SLSSLTNFG
//
