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Database: UniProt
Entry: A0A010RMQ1_9PEZI
LinkDB: A0A010RMQ1_9PEZI
Original site: A0A010RMQ1_9PEZI 
ID   A0A010RMQ1_9PEZI        Unreviewed;      2780 AA.
AC   A0A010RMQ1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:EXF79254.1};
GN   ORFNames=CFIO01_05042 {ECO:0000313|EMBL:EXF79254.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF79254.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF79254.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF79254.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXF79254.1}.
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DR   EMBL; JARH01000561; EXF79254.1; -; Genomic_DNA.
DR   RefSeq; XP_007597146.1; XM_007597084.1.
DR   STRING; 1445577.A0A010RMQ1; -.
DR   KEGG; cfj:CFIO01_05042; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_60_8_1; -.
DR   OrthoDB; 2209130at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05918; A_NRPS_SidN3_like; 2.
DR   CDD; cd19545; FUM14_C_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.90.1590.10; glutathione-dependent formaldehyde- activating enzyme (gfa); 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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_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; IPR011057; Mss4-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   PANTHER; PTHR45527:SF3; SIDEROPHORE SYNTHETASE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 3.
DR   SUPFAM; SSF51316; Mss4-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467}.
FT   DOMAIN          918..994
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2006..2090
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          72..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2780 AA;  305529 MW;  643DB3239A751A07 CRC64;
     MLSTDGKWKL TPRLHSVKFV FDAPIPADAK TPDEIFFDNP FPAEIPGVPK RFVFKTPTTH
     DFDQEVIGLQ TSTKHDEDGL DANVPYDAQA SDVPESKETL TPSTDSRTKI TSGESQPGSV
     THLRGPTCDA PDDMESIVCS AWALILSSFI DSEVVNFDVC VSSSDSPQPT SSATPVIVSI
     DTQVSVSAFL QQIKDNGPVF KSVSQGLGAF RETGGEPLFK TLINFSTTSL QHQQQPANSH
     SFAFQLHCLV QGQDLQLSAT FNERSICKAT VRLLLSDLEH VMWQLANSTG EHSTLADVQI
     MSPASQRHLV KLNRPLPTRE EYLVQELIAK HAKSNAQAHA ICAWDGILSY SELQRSSEIL
     AAHLASLGVG PEVVVPIIFE KSAYSIISIL GVVMAGGAVV VLDPSLPAAR ISMIIKDVDA
     KIVVSSSVSE NKIPSQIQQE NRVLVNRSFL DRLPLVRQFP LKHISPSPSN ALYVVYTSGS
     TGKPKGVIIT HETFCSSAKG FTKAIHLDSP NCRVLQYSSF SFDISMLEVF ATLMTGSCLC
     IPSEEDRMNN LASCINSMKV NWTMLTPSVA SLIVPEEVPS LEVLCLVGEA LPQAIADTWA
     DHVKTINAYG PAECSAITIV SEPRTKGVKS ISLGRPPNCA AWIVRGDGQL ASFGAVGEIV
     IEGPPVARGY LGDEEKTRAV FLDDPDFLRG VVRKPMRCYR TGDLGKMNHD GTIDFLGRKD
     TQVKINGQRV ELGEIEHQLR QQLNSENLPS SSGMNWELIV ELLRPVGGEQ NILTAFIAPK
     TISGTHFHGE GQLIIEESHS LWTTIHRKFL KATGDLASAL PGYMIPRAAV PCSTLPLSPS
     GKVDRKTLRT YGNALTSKQL LRSPSDMEEH TTSVTFPGAR STDFPDSEEE SSIGQHTLIS
     DTYPSTEASI SLCESPQSNL TPTEKSLRLA WSEVLGLPED SILLEDDFFK LGGDSIGAIR
     IVAACRKQSL QINVANIFKN SVLGKMALVC KSTTSEKQTV SPVQFIPFQF LRQEDIPELQ
     EEAAFQCDVA VNRIEDLYPC THMQEGLMAV NLTRPGSYTG RWIHPLPRDV DLSRFRKCWE
     DIHAASPILR TRFATTSTAG SLQTVISENV QWLLHDDLEV FLEQDDANPM FPGDSLNRFA
     LVTSKSGDVT FVWTIHHMLY DGWSLAMLCD RVNDSYHGRS IKPATDYRNF IEYTQNITSE
     TYATYWKTEL QAVSLSNFPA APKPGHQSIA RAVIRDELCI NVDQSSGITM STIVRAAWSL
     MISHFSQSND VLFGATVSGR NAPLDNIESV EGPTIATVPV RVRLDKGSDI LDFLRKIQDH
     ATSMIPYEQS GVQQIKLLNE DTRRACEFQN LLVIQAGGGW DETGPGPLGK PIYREEFTTF
     PVTCEAWLHC GRIEFTTHVD EDVTSRLFVA QAIETVKVVM SQLAWATSQS YRPSQIADLA
     FESTSTSVQQ RASQTLEAKE VSATLHQLIT KTSLAQPQRD AVVSTAASLS YEELEDISTA
     LAVQLIDKGV LKGDSIPLCF EKSIWTVVAM LGVLKAGASF VPLDPSQPVS RLRKVVTQIK
     AKTVLMSAFQ HKATDLGAVA SLIVNRDTLG GISKLQHQRQ PPAQVTPDST AYIIFTSGST
     GDPKGIIVSH AAFASSAMAH GSVFGMSHEH RVLQFSAYSF DASLFEILTT LIHGGTVCVA
     TEKERFENLG DFASRTRVNL ALLTPSVARI IRPTEMPFLK TLVLGGEAPD EALIKKWLDA
     GLTLFNAYGP SECSVIAACH SCTYDTDPKT IGKPVGCSAW VIAADDDTVL VPNGQVGELL
     IGGPTLADGY LNDSEKTIAT FLSRVPWISR EKHTSTYRLY KTGDLVKRAT DGTLVYVGRK
     DLQVKLNGQR IELGDIESHI AGCCSVKRGI VVFPSSGPFS HQLVAVLELE EEEEEGERLS
     SLHQIMTRFN IVAEEIRHEL NVKLPSIMLP AHFIDVATLS QERFPLSTSG KVDRNKVTAW
     VQYLSVRESA ILDTSAPIPS TVATIQSHEL LAYELAQEIT NLVSQRTLSP GPRLDGFNDL
     LLHTSGLDSL NMMSLMHFVR LKYNVRVSMQ LLMDEQTSIR KLAAFISRAA SNDLVPLTSS
     TINSETWRID LMAEIDRLDA GLQKLPGILF QDVQDNFTKK TGNLRVFLTG ASGYLGTQIL
     RQLLERRDVA LVTTLVRGAT PEAAKDRVVE AAQKALWWTE FHEDKLDVWM GDLAKSMLGL
     GQNQWDLLSD GHTFDIIIHN GAIVHWNKSY AALEAVNIRS TVQLLGIAVQ NPAMRFAYVS
     GGRQWRSTEE RDEDIARELS DSMGYSQTKF VAEVLVKRAA ERCPVSQRNI RVFRPGLIIG
     TPAEGVANLD DYIWRLTAAN IEMGIYNADE EQAWLHLSDA ATTSVAAIRT AFNPDSSASP
     VTQHEEGITW GAFWTLVRGL GYKIRPARAA QWLSTVRNDI LRRKEEHPLW PLAHLLEDGS
     MEWEEAAKIQ DMCPLQLKVA LKKNVEALVR LFARGHNASI APYVTTGALE NVPGLVKYDN
     HMFISDTIDG GFAPWLPKEE NGDPVQRWKG HRNSEEVPFD WPVSKSIPTS RLNASPSPSS
     TQFHCHCKGV QLSLRSAADL KADPAKESTS TCVDPKTLKF KACSDSCNSC RQHFGSDIIA
     WTFAPLTHIN FSTEPASAPS QFPQTIAELK EAVLSKTKDP RLGTLAVYNS SPEVERYSCS
     VCSASIFYAV YDRGDMVDIA IGLLDHPDGA RAEGLLAWNY SLLGWTADAA GGWRERLVAR
     TKDSMKEWAR SLNEDQSTKD
//
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