ID   CPF1_COPC7              Reviewed;        2410 AA.
AC   A8NF97;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Coprinoferrin synthetase {ECO:0000303|PubMed:31496254};
DE            EC=6.3.2.- {ECO:0000269|PubMed:31496254};
DE   AltName: Full=Coprinoferrin biosynthesis cluster protein cpf1 {ECO:0000303|PubMed:31496254};
DE   AltName: Full=Nonribosomal peptide synthetase cpf1 {ECO:0000303|PubMed:31496254};
DE            Short=NRPS cpf1 {ECO:0000303|PubMed:31496254};
DE   AltName: Full=Siderophore biosynthesis protein cpf1 {ECO:0000303|PubMed:31496254};
GN   Name=cpf1 {ECO:0000303|PubMed:31496254}; ORFNames=CC1G_04210;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DOMAIN.
RX   PubMed=31496254; DOI=10.1021/acs.orglett.9b02861;
RA   Tsunematsu Y., Takanishi J., Asai S., Masuya T., Nakazawa T., Watanabe K.;
RT   "Genomic mushroom hunting decrypts coprinoferrin, a siderophore secondary
RT   metabolite vital to fungal cell development.";
RL   Org. Lett. 21:7582-7586(2019).
CC   -!- FUNCTION: Nonribosomal peptide synthase; part of the gene cluster that
CC       mediates the biosynthesis of coprinoferrin, an acylated tripeptide
CC       hydroxamate siderophore (PubMed:31496254). The biosynthesis of
CC       coprinoferrin depends on the hydroxylation of ornithine to N(5)-
CC       hydroxyornithine, catalyzed by the monooxygenase cpf2
CC       (PubMed:31496254). The second step, the acylation of N(5)-hydroxy-L-
CC       ornithine to yield N(5)-hexanoyl-N(5)-hydroxyl-L-ornithine is catalyzed
CC       by a not yet identified acyltransferase (Probable). Finally, assembly
CC       of coprinoferrin is catalyzed by the nonribosomal peptide synthase
CC       (NRPS) cpf1 via amide bond formation between three N(5)-hexanoyl-N(5)-
CC       hydroxyl-L-ornithine molecules to release the linear trimer
CC       (PubMed:31496254). Interestingly, proteins seemingly not directly
CC       related to biosynthesis, such as transcription factors, replication
CC       factors, and autophagy-related proteins, are conserved among the
CC       clusters homologous to the coprinoferrin cluster, suggesting that the
CC       cluster may also play developmental and cell biological functions
CC       (Probable). {ECO:0000269|PubMed:31496254, ECO:0000305|PubMed:31496254}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:31496254}.
CC   -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC       (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC       (C) domains) which when grouped together are referred to as a single
CC       module. Each module is responsible for the recognition (via the A
CC       domain) and incorporation of a single amino acid into the growing
CC       peptide product. Thus, an NRP synthetase is generally composed of one
CC       or more modules and can terminate in a thioesterase domain (TE) that
CC       releases the newly synthesized peptide from the enzyme. Occasionally,
CC       methyltransferase domains (responsible for amino acid methylation) are
CC       present within the NRP synthetase. Cpf1 has the following architecture:
CC       A-T-C-T-C-T-C. {ECO:0000305|PubMed:31496254}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of coprinoferrin and
CC       fails to form fruiting bodies. {ECO:0000269|PubMed:31496254}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AACS02000002; EAU88504.2; -; Genomic_DNA.
DR   RefSeq; XP_001833231.2; XM_001833179.2.
DR   AlphaFoldDB; A8NF97; -.
DR   SMR; A8NF97; -.
DR   STRING; 5346.XP_001833231.2; -.
DR   EnsemblFungi; EAU88504; EAU88504; CC1G_04210.
DR   GeneID; 6009726; -.
DR   KEGG; cci:CC1G_04210; -.
DR   VEuPathDB; FungiDB:CC1G_04210; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000092_0_0_1; -.
DR   InParanoid; A8NF97; -.
DR   OMA; WQYVPVR; -.
DR   OrthoDB; 9183at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 3.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.559.10; -; 3.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 3.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF47336; SSF47336; 3.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..2410
FT                   /note="Coprinoferrin synthetase"
FT                   /id="PRO_0000452734"
FT   DOMAIN          783..860
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1324..1400
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1858..1932
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          237..646
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A248AFK6, ECO:0000255"
FT   REGION          891..1260
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A248AFK6, ECO:0000255"
FT   REGION          1298..1317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1436..1839
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A248AFK6, ECO:0000255"
FT   REGION          1992..2315
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000250|UniProtKB:A0A248AFK6, ECO:0000255"
FT   MOD_RES         820
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1361
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1893
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2410 AA;  267726 MW;  EBCA5161FD168D6E CRC64;
     MALRDTAGVP PLLQGYSIVE WPDLTCDRHP SPTPYTSTQP LSSFNVQSRG SLLLAAISRM
     LGAYCGASDI LLAVQVPNKR DYVFVRVNWS DNETWQEVAA RTASQTRKTK SKLLVGDIRR
     AFELPDKQNP CPVLVRFTPS EEPSYFSDFP AVFIFDAKKS SLTLSAPKSL LHPSINDQLL
     SQIISLYHHA GANPKTPVSS NPTFPSHLTS VYDRLPEEDI SNAYPHIPLV KFATEYLERR
     AKTNPHDIAV RWFPELSIDD SNLPSETSTY EELDRKASQL GRWLVTRGLA PEDRVAVCLS
     RDLIFHAAFF GIMRAGGCYV PIDPELPDER KAYIARDSGA KFVLTTSELS SQDLFGSSTI
     YVDEPEVANA IDEQDGGTFN IATPEGLGYM LYTSGTTGNP KGCLLTNHGL AQAIIALSST
     AADVRMKDIR EGRYLAVASI AFDVHLAETI VPMALGMPLL SAPRSQLLEN LPQYVKLLGI
     THLGIVPSLI EATLNASKDN EGGLALRYIA SGGEKMSDSI LDKWANHPQV RLANFYGPSE
     VTIGCCARYM DSNTPRANIG RPLANVSGYV VDADLNILPR GGVGELVVEG PLVGRGYHGR
     PDLTEKVFLE WPEKGRWAYR TGDLVRMMPD STLEILGRID TQIKVRGVRI ESEGISAIVR
     KAEVPSADMV LDATTVLAKH PALGSEQLVS FVTWDSTVPV STRKSLRPSL SIPPRGFLKS
     IRSICNKELA SYMRPNHVIP LNWLPLSSNG KTDTKILVEL FKNLDIAQLA SLISSEDDVS
     VSRDCTPLEA EVFEIVQRHA PSYAQRPHPE LNIFECGLDS MGVIRFAADL KLTFGKAIPA
     TEIMKKPALQ DIAQLVHVST MNHSLVGTPL PTIDAATHKH LSSIYSNDIE DILPPFPVQE
     GVLARSVEDT SLYVQHVILH LDSGTSMSQL QRSWESVIAA HPILRTVFYV DRSVWQVVFK
     SFNLPNSWSD RSLSVKTVEE FRARFYSRFA GEITKDINRN LSSIPPFRLA YFRCTGFNVL
     VLSIHHALYD GTSLPVLLRD VENSYLGLER VQKASLRAIL AEISKHDLAL AQQFWRDSFR
     EFEWPRPAFR QGSNALASSV KYLSVHFTQK LSVIREVANK KQVTLQALLS FTFAYLIGSR
     LYDSNDVAFG VIRSGRMLPV DNVDVALCPT ITVLPMRVRL GDANSTLVNI QNGISTMTEH
     EHVPLGKVQN WLRPGEPLFE VLFSVSVQQQ EESKIWRPCD YEPPAADYAL SVEAVVNVHD
     DTLIVRAAWL DGLITQDHVA DLLHGFEKVT LTLDKGEELP LPSRRSPEPV RKVNDDEDPS
     AQVLLDPVVV ADLQQTICDF LEIPTAILTN RVSFISLGLD SIKAVGLAKR IRALGYDVSS
     TEILRASTLK RLARVVSNNK QKKEEPYEHY AQLVRQVEGY ISKSEVQLSP EDEVKIIPST
     ALQSGMLSQT VGSDGRLYVH AFPLTLSPGV DVQRLKSAWE AAAEKIDILR TSFHFIPDNG
     TWVQVIHSFN ELKWSIQNLE GFVNVTSAVK SFVESIECTD EFAFSTPPFW LRVFTPLKGP
     SVLALVMHHA LYDGGSVNSL LDVVQRIYRG ESISYPVQFA DLLPDFFRQE LQNLERTLLP
     LHSLPSSDPY HISIRQVEVK DVDLKRLLTE TEVTLQCLLQ GALAQSLAIL TRSADVVFGN
     VVSGRVGRGT EEVVGPILNT IPCRVHISDH DSVDALLQSI HRFNMEAASW QQASLRSIQK
     ALMVDRIWDC LFTFQPLAPP PQAAIWSLDI EEHEDIHIQY PLHVEIEQNK DGFSVRCACQ
     SNVLDKAGLL NFMDTLSNTV QQFVANPKER IGRTFSVPSP SNTDPTPTTV VAPAPATVQA
     GIIHPVLLSA IRDFAPDAEV TFDTPLPALG IDSITAIQIS GKCRRSGLRL TATQILNSST
     VKDLVLQATE IKATAKSTQV SDGVFKPLSS EEKDSIARRF ADDAKYIENI SVTTAGMKWA
     IGGWQRTNGS LFQYLFTFKL PDDVDHARFK NAWHMFIRRH ELMRSTFATA PGGTEPRIVT
     FSKDFKFDHW AEIVVDDAVF YRRLLGKMKE MVSDPVPISR PPVRAALFRS DKQSYFIFHI
     HHFQYDAWSM QVLLNDLSSI YYDQEPWAVT DLRAFTSLFD PNEERLSVQR RFWEKALSPS
     FKPSLLPSLL NEVQGPLATP TGQPQLIMVP GALTNVSRYE EQARKLGVTL QTVLLAAWAQ
     VQANRSRTSA STFGVWQVSR SGHIDGIERL AVPCVNVLPI HVKVGGSLVE VTKRIQVDLS
     ERLSQPVIEH SDLVNISKWT GMSGETPIFN VNVNVVKLPV TLKRDGLVEP VKAPYYIPRI
     AVPTVTPTLD RLAVSPLCQN DVVVDIIVYE ESDSILMSIE AVDNIMTEGQ AKDIIQEWAS
     VVSTTLSYKD