ID L2GE93_COLFN Unreviewed; 943 AA.
AC L2GE93;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Nrps-like protein {ECO:0000313|EMBL:ELA36937.1};
GN ORFNames=CGGC5_3625 {ECO:0000313|EMBL:ELA36937.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA36937.1};
RN [1] {ECO:0000313|EMBL:ELA36937.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA36937.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KB020498; ELA36937.1; -; Genomic_DNA.
DR RefSeq; XP_007273993.1; XM_007273931.1.
DR STRING; 1213859.L2GE93; -.
DR EnsemblFungi; ELA36937; ELA36937; CGGC5_3625.
DR HOGENOM; CLU_002220_2_1_1; -.
DR OrthoDB; 2230730at2759; -.
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; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF35; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
FT DOMAIN 43..357
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 597..836
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT REGION 498..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..553
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 104383 MW; 64DB683B0C35AE53 CRC64;
MAIHTEGVAA RSLLTSEKPT LEIVETVKPV EQPRTVTDLL LRRVEEAPDV DVLAYPATAR
GRDDYVNYTA KDLDRFADEA ARKYAQAGLL PENPNSAQAE VIALLANSDI NYVVTMFALS
RMGFAVLYLS TRLSPEAYVN LLKKTNCNRI VISDRYSSIA SEITEQYPIS SFSILDRVDY
DLPTPSGERF PIFSHPNASQ RISFIVHSSG STGLPKPIFQ THAACVSNYS SGIPYRAFLT
LPLFHNHGIS TLFRAIVAGH RIAIYNANLP LSGTTLVKAM AATEPGSLHC VPYALKLLAE
TEGGIEALKK LKLVLYGGSS CPDDLGDRLV EEGVYLVGHY GATEMGQLMT SFREPGDKYW
NYMRPLASAK PWLRMIPIAA PWRSLGRLDD RVTLVNGEKV LPIPYENHIR EHELVQEVVV
FGVGKSIPGL IIIPSENAKD LSKEEILKNL SPMIEVVDIG TEYPRTDKGT VIRAAFYKQF
ADLIEDVYRR FQAPTDQARR XXXXXSRLAP AGGPPPRPLP QQARLRGPAE RDRLLRGRRR
QPASKHGTRP HPARRQPRRQ DPVVFESPTV VALAKHVHSL RTGEAAEAED EIETVVLTGA
TGSLGAHLLA QVVRQPYVKT VYCLARASSP SEAESRVLAS LTPKGLVLSD AKKAKVKYLP
TNLGQADLGL APEAAAELRK TLTTVIHSAW AVNFNLGVAS FEAQHIRGVH NLLNFCLGTE
TVDPARFYFC SSISAAAGTP IPARVKETYV ENLEHAQNMG YARSKVVTEH VVKAAATKTG
MTARVLRLGQ IVGDSEGGVW NQTEAIPLMI RSAKVIKALP ALDETPSWMP ADKMALAVQN
PTLFHWTFDF LRALRAAGLE FQIVSQREWV RRLRDSDPDP ETNPTYKLLR FFEEKYDNDR
PGREGLVFET QRTGERSPAV GEGWDVVGSR LVEKMVRWME TQW
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