ID A0A2H3IIK3_9EURO Unreviewed; 2625 AA.
AC A0A2H3IIK3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Male sterility, NAD-binding {ECO:0000313|EMBL:PCH03970.1};
GN ORFNames=PENO1_029720 {ECO:0000313|EMBL:PCH03970.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH03970.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH03970.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH03970.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCH03970.1}.
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DR EMBL; NPFK01000060; PCH03970.1; -; Genomic_DNA.
DR STRING; 290292.A0A2H3IIK3; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0030639; P:polyketide 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; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; IPR013120; Far_NAD-bd.
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; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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; 2.
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:UP000218381};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 374..790
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1653..1727
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1764..1838
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1632..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1857..1872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2625 AA; 287561 MW; 0EAAA177A52A75CB CRC64;
MVSRIVNPCE GNTVLLFGPQ ALSFNQEAFL KLRATILGSP AYQWVLDVVD ELPTIWIALL
NSIPKLEVID GAKKLKNLSD WIRSGDIRGD SFPLPNILLS PLVVITQLTQ YANYIQEHPE
LRKSDKTETL GFCTGILSAL AVSSSAGEGQ FAKYGSVAVR LAMAIGAIVD AQDSERGPSK
SLATAWNTAN GEDELKRILA GFPDTYISVS YDHRRATVTT SSKTIAALQK ALRAAGIIAN
EVGLVGRFHS DSHWNEIDSV IEFTNTQPKF QFPKLSELLL PTRFTTRVED LASSKLHHAA
LRQILVDKSE WHRLFESVQE TRLGDETSLL LSFGPERPVP PSIMRVLSSQ VIHIADVSGK
SNQQPETNPY LIGDNDIAVV GMSLKVAGAD DVEEFWELLL RGESQHQEVP KERFSFETVF
RDIDPKRKWF GNFIRDHDAF DHKFFKKSPR EIGSTDPQQR HMLQCAYQAV EQSGYFRSKT
VDKKIGCYVG VCAADYENNI ACHAPNAFSA TGNLKSFIAG KISHYFGWTG PGLTIDTACS
SSAVAVHQAC RAILSGECSA ALAGGTNIMT NPLWFQNLAG ASFLSQTGQC KPFDAKADGY
CRGEGIAAVF LKKLSSAIED GDQILATIAG SAVYQNQNCT PIFVPNAPSL SDLFRDVVGQ
ARLEPKQITV VEAHGTGTPV GDPAEYESIH NVLGGTNRTT ALQLSSVKGL IGHTECTSGL
ISLIKTILMI QEARIPPQAS FSTINPHIHH SADHHIEIPT KALTWNENFR AALINNYGAS
GSNASMVVVQ APVTDKSVAV VEGSKSPFWF TGPDDRSLRA YASRFARFLQ SKSVSSKNLT
LGNVSFNVSR QSNRVHDKGL IFNAVSLQEL EQKLSSFASG KSEILSHSKV PTRPVILCFG
GQVSTFVGLD QQLYENVTIL RQHLDQCDAI VTKLGQSSIF PGVFQKAPVE DPVHLQTMLF
AVQYSSAKAW IESGVEPAAV VGHSFGELTA LCISGALGLE ITIKMVIGRA KIIREDWGSE
KGAMMAVEGD LEQVQRLLSV SVVEGEKAAT IACYNGPRSF TLAGSAKAIE EAAKTASTGA
FSSMRTKVLN VTNAFHSTLV EPLMDELDKV GSELTFCQPT IRLERATETG SNGSLTSKFV
AEHMRYPVYF NHAVQRLAQE FPSSIWLEAG SNSTITNMTS RALGSSGEYH FQAINITNTS
SGLTNLSDAT VSLWKNGLDI SFWGHNSKQT YSYTPLLLPP YQFEKARHWI EMKKPPNFSG
EPTVVEVVKT TVEELPKTLL TFVGYQDSHQ RQPRFRINTM IPKYEELVTG HIIANTAAIC
PATVEVDLAI EGLRTLYPGV TDTMQPQIHS VDNQAPICMD PSRSVWLEYE ALDDASHTWS
FKIYSTGTGK AATTTHVTGK IVFRGLDDPQ FQADFARYER FVSHDRCAAL LKADDADDVI
QGRNIYKTFD EIVDYGEQYR GLQKLVGKGT ESAGRVVMTP SGETWLDAHL SDAFSQVGGI
WVNCMTDRER TDMYIANGFE QWIRSPKVKP SAERPATWDV FALHQKHGDK AYVTDIFIFN
GVNGELAEVI LGINYAKVAK LSMSKLLSRL TATGSGAGCA SPSAAAKVQP GIAMTALTPA
ASSNGAAIPL ATKTRKAPKA PKAPKKKVSS GQPEITGKVR AMLAELSGLE PEEIKEDVEL
ANIGIDSLMG MELAREIENI FKCSLPEEQL VEVTTFQGLL QCIRSNLPAS AGEAEEVEDD
DEDDESLDDA RVFTPSDAAT SVSSTSKADV IEFLVEFLGI EESSVTRSTL LRDLGVDSLL
STELRGDISS KFGVDVPEEV MLEDLSVEEF DVQINGSSSL AGAAREPEAP KSAPSVSGPG
SAPSSSSASR ATGDNLNLPA ATLLEAFHET KVLTDKFIED YRCAGYIDTV LPRQDQLCIA
LAVEAFEQLG VSLKAAKPGQ KLEPIKHQPQ HNRLAEYLYM MLEKGARLID IDANGTITRT
AVATPTKSSN DICQQLVRDY PDHNFANRLT HFCGLRLADV LNGKMDGIKL IFGSPEGREL
VSGLYGDSLL NKLAYEQMKD FLRRLISKLP RNEGSLKILE MGAGTGGTTK WIVPMLDELN
FPIEYTYTDL APSFVAAARQ KFKAYPFMNF RVHDIEKQPA DDLLGTQHLI LASNAVHATH
SLTVSTQNIR KALRPDGFLM MLEMTETVYW IDVIFGLLEG WWLFEDGRRH AIAHQSRWEK
DLKSVGFGHV DYTDGHRPEV NIQRIFIALA SGQRYDRIPI PPKAVTNEAP ITDIVAREAA
VSKYLKKAVS GFTAVPISSP AYPVMSNQGV LVTGATGSVG SHIVAHLANL PSVKTVFCVN
RVSRSDALIR QQESLLSKGI SLTREALSKL VVIETDTHKP LLGLQRGEYD RLVRDVSHII
HNAWPMSGKR ALMGFEQQFV VMRNLINLAN EASASGPRKI TFQLISSIST VGYYPIWSGK
RNVPEIRVEM NSVLDNGYSD AKLVCERMLD ETLHKHPDRF RPMAVRLGQV AGSSTSGYWN
PMEHFSFLIK SSQTLRAFPA LEGELSWTPV DAVAGTLSDL ISGDHRPYPI YHIDNPVRQQ
WRDTIPVLAE AMGIPSSNVI PFKDWVGMVR RFPGSEVDNP AQLVQ
//
