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Database: UniProt
Entry: C5FCP3_ARTOC
LinkDB: C5FCP3_ARTOC
Original site: C5FCP3_ARTOC 
ID   C5FCP3_ARTOC            Unreviewed;      3918 AA.
AC   C5FCP3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 97.
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=MCYG_00465 {ECO:0000313|EMBL:EEQ27577.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ27577.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
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).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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DR   EMBL; DS995701; EEQ27577.1; -; Genomic_DNA.
DR   RefSeq; XP_002850361.1; XM_002850315.1.
DR   STRING; 554155.C5FCP3; -.
DR   GeneID; 9225582; -.
DR   VEuPathDB; FungiDB:MCYG_00465; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_37_5_1; -.
DR   OMA; GGWLINM; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000002035; 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:0043604; P:amide biosynthetic process; IEA:UniProt.
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:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd19532; C_PKS-NRPS; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR010071; AA_adenyl_domain.
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; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
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; 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; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-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; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
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:UP000002035};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..438
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2354..2429
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3508..3584
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2434..2489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2437..2451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2464..2489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3918 AA;  432142 MW;  A94AAB78E1B8A120 CRC64;
     MPQRKEPIAI IGSACNFPGN STTPSKLWEL LKEPRDLSKP IPDNRFNADV WHHKDNSHHG
     TSNVTKSYFL EADPAVFDAN FFNIPPNECE AIDPQQRMLL ETVYESLCAA GVTMEGLRGS
     STACYVGLMC DDWAGMLAKD WDCLPQYAAT GISRAIMANR ISYFFDWHGP SMTIDTACSS
     SLVAVHEAVQ VLRSGDCNVA VACGANLILT PGMYIAESKL KMLSPDGKSR MWDQGANGYA
     RGEGLAAVVL KTLSQAIKDG DNIECVIRET AFNQDGRTTG ITMPSNLAQT ALIRETYKKA
     GLDPLNPNDQ PQYFHAHGTG TPAGDPQEAE AISRAFFNDG QVAEKKLWVG SIKTIIGHTE
     GTAGLASLIG TSLALQNKTI PPNLHLNQIA EKVKPFYTNL EVPTTSHEWP SPPAGQPMRA
     SVNSFGFGGA NAHAILESYD PIENQASCKE TERSLFTPLT FSANSEKSLR GMLETFSQYL
     SAENAPDISD VAWTLQNHRS ALVYKIAISG RMTTDLVAGI DAARNQKDSI GVRSSGPEKL
     TVLGVFTGQG AQWPTMGREL IKTSGHVRNI VAGLDRSLQE LPERDRPNWS IQGELEADNK
     SSRLSEAALS QPLCTAVQIV LVDLLKAAGT NLEFNAVIGH SSGEIAAAYA SGFISARDAI
     RVAYYRGLYA KFARSPSGKK GAMMAVGTTL EDAEEFCQLD EFEGRITVAA SNAATSVTLS
     GDGDAIDKAQ VVFKDESKFV RKLRVDTAYH SFHMNSCSEM YLKAMHTCGI EYKEGYSSVS
     WYSSVIPDKK MASSDLNGQY WADNMNNTVL FSQAGITAVK ESGPFDLVIE IGPHPALKGP
     CLENLEQATG VGGTPYTGLL SRGVDDVKAF SAALGYIWEC FGSAAVDFGG YDKLMSANSQ
     RRNLSAELPE YSWDHTRSYW LDSRVATSYT TREAPHPMLG VNAVEGSTGT QIQWRNILFP
     KEISWIPGHR LQGQNVFPAS GYVCMAIEAI MTLSNNREVQ LIELEDVDIA RAISFLDDTA
     GIEIIFTLNV LSSEPELISA NFQISSCPKG DNTLTLNGKG KISIRFGESI VDALSVSQVP
     QFNMASVDID RFYKYLSDMG YNYSPPFKAI SSILRRKDAA VGEITDSRGG SWEDSFLMHP
     GFVDTSFQAV FAAFSSPGDD RLWSIHVPTK INRLSINPSL AVFPPGEEIV WPWQAVVTSE
     THDTPTADIE VFAPNKNGVL MEIEGIVLVP LAKASEENDV KLFSNLIYDL AQPDGVVAAP
     NRLSKPDAHI AKVSERFSFY WINKLLNSIT TKEEEETLSH FKYMLRWYRA DISILRAVGQ
     NIAHVIRTRG NIHEYTLKDN ILDRFYEEAI GLDITNQWEA NLAAQVAYRY PRMNIIEIGA
     GTGGSTRMIL PTLDKAFSTY TFTDISSGFF EAAEKRFSQY SDRMIFKTLD MEKDLSEQGF
     TEGHYDMVLA SNVLHVGPDI DLTLSNVRKL VKPGGWLINM EVATYFPSLR EGFSMSGFPG
     WWCGAETGRP WGPTIPVEEW DKVYKRTGWS GIDALTPNID SIDHLVVMAT QAVDPQIYTL
     RDPLALEHAH PQRENLVIIG GKTEEVANIV TECSSILRSH FSSIRNVTCI DNFSNSDTKA
     VATVLNLAEL DVPIMKELMD DQPQKLEGVK EVFSTPREIL WVTKGNRSES PYSRMLVGMA
     RTLRREYSGI NFQALDVDVL DSNSAKLFAE TLLRHLNLQA ANNQLVPDSI LWSDESEYHL
     EKNKIYIPRL ISADKINDRY NSYKRRITHE ASARDSNIEL ISKSNSYNLC EPSPLKPTTR
     SESDSEITVS QSLLQSVEVP LVGHFFLCYG TDDCGEHVIA LSDRSNSVVH VPRSWTIPYG
     GTPNPEQVIL SVAANLVAHL IIADISANST ILVHDPDQIV AAAISKQAAT KKIQVFFTTT
     QTSKKGPQWT YIHPKTPRRL LKKQLPKRIS TFINFSSISD KQTMVNLLDS LPLCCKQSDR
     SMFFGNSVAK RPGSNAELVS KILTTGFDIA KTTNFSVPYN RSTLPLDRVP GYSDRTKDLM
     VIDWVTDNKI SLTVEPIDPY ADLFSAEKTY LMIGLSGEMG QSLAEWMVNR GARYVVLTSR
     RPKVNTEWIE SMEDEYGATI KSMPLDITDA DALHSCYNKI CRTMPPIGGV AHGAMVLVDS
     LFQKMSYEDL MAALRPKVLG AINLDNLFSE NTLDFFILFS SITALIGNAG QSNYIGANSF
     MESLGLQRRR KGLSASVIAI SSLIGLGYFE RAENLDIDQF SRSGYRNVSE QDIHTLFAEA
     IVRGRPGTTE SHEVVSGVVP TYADGDIRAS YLKDMKFSHL ILERTSAKQD GSSSTQIPVR
     IQLLTATTED EVREVMQSGL TRRIKKMLRI PEEDVFNATD SLVEQGVDSL VAVEIRTWFI
     REIDIDMPVL KVLGGSSISD LLNDAIQKIS PELTPCLGSK GTKSNLNGHP TPPKEVPNPS
     FKPAAIDSSP SVTQDTQSQS KSPNTSLVHS TPLTITAITE TPAKPLGDEP RLAVENSNIQ
     QGLGRREKSE VTEKMSFGQS RFWFLNQALN DKTTFNMAIL VRLSGRIRVK DMERALELVV
     LRHDALRTRY FSTGEYMESP MQGVISTSAV KLVVKHCKDE SAAYRELDEL RSHVWDIGDW
     ETMKVSLLSS SDTMHYLVIG CHHIGMDGFS FNVFYSDLEK AYEGQKLPII PKSSQYGAFA
     RKQREDWENG NMNADLAYYR EIIPRNLNPI PLFPFAKTST RLPLDTYDTY SADVRIEPAL
     TKKIKAASRF LSSTTFHFYL AVLQTLIFRQ LDDCDEFFIG VADANRTDDK FINTLGFFLN
     LLPVRFERHA AKKFGEAVKQ VRDKVYTGLA HSKLPFDVLL DELKIPRSAT ATPIFQVFVD
     YRQGVQERQK YMGLDAVGEK WHLARTGYDM TLDIVENAAG DTRLELRLQK RLYTAQHTKL
     LLNGYVNLLT AFANNPTADW SVPDVWDSQT ISNALEVGRG RSLQYEWAPT VMHHIDNVVS
     QYGTNICLKD GTGKTMTYSQ MADRVNSICA ALIATKVIGG DKVAVFQQPT ADWVCSLLAI
     FRAGAVYVPL DLRSPLPRLA AIVDQARPCV IIAHSQTLRD VKHLEVPNAV VVNVSSLATS
     GQAMPNLAKP DELAVVLFTS GSTGIPKGIH INHSNIIKQL EGCSKQFEFK GTASYVLHQT
     AYSFDKSLEQ IFTALVHGGA LYVVPAEQRG DPISITNIMA SEGITHTATT PSEYLMWFRY
     ARDNLLKCKT WKCALLGGEV ASDAVIEEFR KLGMPIRLLD SYGPAEITMS CAKVELPYRS
     MITGHPAPVG FMLPNYSVSI VDSQMNPLPL GFVGEIVIGG VGVASGYLNN DELTKQKFIQ
     NSFGGDGMVY RTGDKGRLTE EGALFFEGRI DGDTQIKLRG VRIELEDIES TILQASAGAL
     THAVVTLRGK QDSTFLVAHV VFSATYAEPR DDLLTRLPIL LPLPQYMIPT IFIALDNLPF
     TTHFKVDRKA VLALPVPEVG NASTEQIIGL TETEAQLAIL WNHIIPATRV LIPGSDFFHA
     GGNSLMLVKL QAMIRQSFSV SLRLFDIMNA GTLRSMACLI EDALGAKELD WDAETALPTL
     PSRNPDISPP KHKDIVVMMT GATGVLGKNV LAHLVADDRI SKIYAVAVRP QNGISALTRI
     LDPKKKINIK HGDLDKARLG LSEKEAIILA SEADVILHLG ANRSFWDSYY HLRAINVFSV
     KEIVKIAHPR NVPIHFVSSG GVSAYSFNSP PTNGHDGYVA SKWAAEKVLA NAANEVGLKA
     VLHRPTKAPG GTSVAPTEIL DELLSLAKQL QKKPALDGLS GSLGIVPLEH IAEDIVRTIF
     GTEMIGLGQP EVITHSSTLN VNIKEFADRI LQDQDVSALE EMPALQWMGL AKKGGWSQFM
     VGHEIHMHNS NDRIVSTR
//
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