ID A0A2J6QEC6_9HELO Unreviewed; 1036 AA.
AC A0A2J6QEC6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative NRPS-like enzyme {ECO:0000313|EMBL:PMD24619.1};
GN ORFNames=NA56DRAFT_620915 {ECO:0000313|EMBL:PMD24619.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD24619.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD24619.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD24619.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ613472; PMD24619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6QEC6; -.
DR STRING; 1745343.A0A2J6QEC6; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000235672; Unassembled WGS sequence.
DR Gene3D; 1.10.1200.10; ACP-like; 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; 1.
DR InterPro; IPR036736; ACP-like_sf.
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 InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT DOMAIN 40..343
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 660..910
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 1036 AA; 114759 MW; 0E3DC1E44871EB4A CRC64;
MGDVGVQTIY TYDEVIRSRA LDEDQVPLIA YPKSKLGITD YEFFTGKELD RLVDGAAKAL
INSGLRSLNG GEEETVGIYG ISDLDYIVTI FGLGRLGYTT FILSPRLPVS ACVSLLQDAS
AKTLLYAPQF HSLASQTSSS FSPSLALIPI LTREQYDLPN NPTPPFSRSG INLEKENFKK
LIMMHSSGST GLPRPIHYTH KRLLATMLTA QSLIAFQSVP LFHAHGFISF IQAIYTRKCI
YLFNGHVPQT HDTVTAAIRA ANPEIVWTVP YVLKLLCEKS DGVEVLRKCK VVSCSGSRCP
DELGDLLTKE GIHFGTVFGA TEVALILTSL NRPKEDKAWN YLRPPPHIAP FIRMKPIDGP
ICECVVLDGH KGKMMSNSND PPNSFHTKDL FIAHPTIPNA WKFVGRLDDR VTLTNGEKVL
PLPIEGRIQQ DPLVREAVVF GIDRPVPGLL LFKAENAREL NDEEFLDRVW PAIEDANSRA
EGFSQISREM VVVLGTDVEC PTTDKSSIKR AQVYREFKGL IDGVYERLES SQEGTLVLVG
EELEQWLMAA FEKLGVHLKD REDDFFSAGV DSLKAIQMRG LIIRNLDLGG NASKCPSMVV
YDSGNVKKLA EALLDIRNGR TSVNGADEIW EMENLIEEYS HFVKRQSDGG KAPESKVVLL
TGATGSLGSH ILSQLIKLPH VSKIYCLIRS ASAPQTAIER LNEAYQGRHS THIVSSAEIH
PLFSDISKPD LDLPPPILER VQAETTHIIH CAWEVNFALS VRSFTPQIAA LQNIINISLS
SPFSKPAHLL FCSSVGTAMA TPAPYPGADV FIDEIPINEV TDASPTGYAR SKLVAERMLE
KAVVHDGARA TILRIGQIIP SPKSGTMLWN PNEMIPLMVR SALSTGVLPE NPSVSDQCSW
IEVDSLSRAI LDIGGLTRGG LEKPESEESQ LVYNLVHPRP FSWRHDFLSA LKAAGLDFEA
VERRTWLEKL KNSEKDINKN PSRKLLAFWE AQNVDGGTII FETAEAEARS EAMRNMVRVV
DEEYVEKLLH AWRNVW
//
