ID F2SRZ1_TRIRC Unreviewed; 2208 AA.
AC F2SRZ1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Non-reducing polyketide synthase nscA {ECO:0000256|ARBA:ARBA00018393};
DE AltName: Full=Conidial yellow pigment biosynthesis polyketide synthase nscA {ECO:0000256|ARBA:ARBA00031359};
DE AltName: Full=Neosartoricin B biosynthesis protein A {ECO:0000256|ARBA:ARBA00033379};
GN ORFNames=TERG_05353 {ECO:0000313|EMBL:EGD89109.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD89109.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; GG700652; EGD89109.2; -; Genomic_DNA.
DR STRING; 559305.F2SRZ1; -.
DR VEuPathDB; FungiDB:TERG_05353; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR InParanoid; F2SRZ1; -.
DR OMA; LATNCVH; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
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; 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; 3.40.50.720; 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; 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; 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; IPR016039; Thiolase-like.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
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; 1.
DR SMART; SM00827; PKS_AT; 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; 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; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01184; UBIE_2; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 150..566
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1419..1493
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 43..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2208 AA; 245848 MW; E7BFA378EF967860 CRC64;
MRKEGLIVAE LSLQGYFHYQ GHQDSVELLI QLCDSNPELQ FSNHSSLDRS DHGHKSDSGF
TKDTKPHQLA LRSILVEQCD WYRTFAATYT SKSNGSQSQV VLFGHDNCVP PSMARNLGRN
LINATNLDEV LPSAEIQPHL EARHSHVRDD SDIAVVGMAC KVAGADDVEQ FWDILRAGKS
QHTEPPSDRF HFGTFWRELD PKRRWYGNFI TDFDAFDHKF FRKSPREMIS TDPQQRWMLQ
IAYQALQQSG YFLSPDRDKH IGCYIGLGCV DYEHNIACYP ANAFSATGNL RSFVAGKVSH
YFGWTGPSLT IDSACSSSAV AIHHACKAIL SGECTAAVAG GATILTSPIW FQNLAGASFL
SPTGNCKPFD ANADGYCRGE GVGAVVLKRL STALGDGDQI LGVISSSAVY QNQNCTPITV
PNADSLSTLF RDVTKQAGLD PSRISVVEAH GTGTPVGDPA EYESILRVFG GQNRPDTLSL
GSVKGLVGHA ETAAGIVSLI KVLLMIQERS IPPQASFNTI NPAIKRSPSD NMEIPTNLAK
WDTEFRAALI NNYGASGSNA SLIVTQPPEQ ALGTTIHSSS FPSGIKYPFW FCGNDDGSIQ
RYIARFRQFL ESSKCLGKTI TAFDLAFNLY RQSNRMLSRA LLLGSGSMAE LEATLKIFEN
DVSQIESMES VDIRSVIMCF GGQISTFVGL DREIYDTCKI FRKYMDECNS IIMSLGLDGL
FPDVFQKSPV KDIVKLQTML FATQYASAMA WIECGVKPVA LLGHSFGELT ALCVSGVLSL
PEAAKMIIGR ARLVRDLWGN DKGFMMAIEG DIQEVQHLLS EANKLQEGSQ KVTIACYNGP
RSFTIAGPVQ SAKIIGELLA NTPVLSSMKW KKLNVTNAYH SILVEPLVEC LQHLGRSLTF
DEGRIPVERC TEHPPSSGTF VTEFIAQHMR YPVYFNHAVQ RLSLRYPSSI WLEAGFSSTI
TTMAGRALNL PSDSHFQGIN FTSGRGLQNL ADATMNLWRN KLNVTFWPHH SLQTSEYNQL
LLPPYQFDKT KHWVTLKKPE EALFKLQDEP KPREEQPLRL WEFVDYNKDD KRSARFKINT
ASTEFHDYVA GHTIAHAAPL CPSTLQLDIV IEALLKLQPE YLSRNLQPQL QGLENHVPIC
LDLTLCVWLD VEAIDPDALI WEFRMISEPT GGKQTPTLHV SGKIRFKSNQ DIQLLNDFAR
YERLSGHERC LSLLNGDDSG DIIQGRNIYK VFAEVVDYGQ IYRGVQKLVG RGNESAGRVV
KKYTRQTWLD TPLADSFCQC AGIFVNCMTD ISENEMYIST KIEQWIRSPK LLPGDSRPDV
WNVLALHRCP SDKEFLSDVF IFDSQNGELL EIILGIGYKR VSKRSLGKML TNLTPGNQKA
EAKAMQPHVD AEIDIEASCS TPPPVRTTLT DSPGNGPPKD VSEDIRNLLA NVSGLETHEI
RSDTVLSDIG IDSLMGMELA REIETVFKCS LDTEVLNAVT DFKSLMKCIQ EALGYKIADN
VVSKPETNTS TIDMGITDAH TANGPPHVNG SLAEDEILNI PPDTIINAFQ ESKRLTDEFI
FKYKFADYAD YVLPKQTELC IAYITEAFEK LGCSLQKAKE GERLDRIPYL QKHHKFVNYL
YMMLEKVARL VDVDENAIIT RTAITPPFKH STILLHDLII NHPDHANDHK LTHLIGSKLA
ECLSGECDGV QLIFGSSDGR DLVSGLYGKS PINMVWLRQM EDFIHRLIQK LPTNKGPLKI
LEMGAGTGGT TAILVPLLSS LQMPVEYTFT DLSASLVAAA RKRFKDYTFV KFRVHDIEKE
PATELLQSQH IVIAANCVHA THNLVNSTKQ IHRVLRPDGF LMILEMTDTL YWVDVVFGVL
EGWWLYNDRR KHVVAHQSIW EKSMHLAGYG HVDWTTGARP ETSIQRLIIA LTSGPRYDRL
PMTPNNAPSQ ETDFVARQAI VDKYTREYST SFPAPGTATE PILPEALQGH SVLVTGATGS
LGSHLVAHFA RLPTVREVVC LNRRNSVDAL LRQVQSLEGK GIFLNEKSMS KLKVMATQGE
KEMLGLQDSE YQYLVHSVTH IVHGAWPMSI KRPIKGFESQ FQFMRNLIDL AVEISNLKSV
TPGFQFISSI ATVGYHPLKT NKVLVPEERV EVDSVLPSGY GDAKLVCEKI MEQTLHKLPG
RFRPMSVRIG QISGSRKSGY WNPVEHFSFL VKSSQTLRTL PDLKGVSY
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