ID A0A371CTU0_9APHY Unreviewed; 1066 AA.
AC A0A371CTU0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Acetyl-CoA synthetase-like protein {ECO:0000313|EMBL:RDX43676.1};
GN ORFNames=OH76DRAFT_1487700 {ECO:0000313|EMBL:RDX43676.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX43676.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX43676.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX43676.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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DR EMBL; KZ857461; RDX43676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371CTU0; -.
DR STRING; 139420.A0A371CTU0; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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 Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT DOMAIN 583..658
FT /note="Polyketide synthase phosphopantetheine-binding"
FT /evidence="ECO:0000259|SMART:SM00823"
SQ SEQUENCE 1066 AA; 117887 MW; C12B49C91372543F CRC64;
MPLDPSRVPP HVSTDFREPA ELIARDDVAV SQYYAWQAKN NPNYPLFVYQ DGDHLEYITY
ARANRAMDRV ARYVASTVGA GTGGERPVVA LFANADTITY FCTAIGVMRT GCTLFLVSTR
NASAAIADMF QRTGTGHVIL SVDPFLRGTA REALATLANA GQHVAQLELP TFEDLFAEVL
DPQSPYEARV ELPTTFDMDA VGVIMHSSGS TGHPKTIGWT RKNLVAWGKY GLHDGFMTKC
VMGCHGTPMF HAMGAFLYAE APILGVIIAC FKPAVPPTVP TPDAVWEGIV ATGTDFSFSV
PSFIEEWARD PEKVLFMKNM KGLMFGGAAL NEEVGNSLAS KGVALVDCYG CTEAGLINNF
SRANPGMDWQ YWSVAPDVEC LFRPMGDETF EVVVLSPPDR PLPKTNTKIG DRDAYATSDL
VIRHPTKPDL WKIIGRIDEQ IVLSNGEKTN PIPLERMINE DPHVKSSLMF GRGKFQNGVL
IQPAEDFAFD PSDLKKLEEF RNLIWPTIER VNAYAPQHSR IFKEMILVTS PSKPFEFTVK
AQPRRHVILR AYNDEIEALY KEVENSAQSE FAPPAVWDEA STTSFIRSVV KKTLRRDIGD
DDDIFRNGGD SLQATYIRNT ILRALRETHK DAPKRLPANL VFAAPTISSL ARAVYGAVST
DEPSTSHTPA DLWKYVEKYS ANLPARPTNL VPRPTGKEVV IITGTTGGFG CDTLEHLLRD
ETVGKVYAFN RKGTQALERQ RAQFKARGLD ESLLDSPKFV MVEAVLHERD FGLEPAVLEE
IRTSVTHIML NAWKVNFNMS IASFEVDIQG ARNFVDLALS SPYTQAPSII FVSSIGVFAN
YNGPCPAPEA PLDDPKVPFG AGYGESKWVT EHVLQNVAAQ TDVHTVVMRL GQVAGDKLGY
WNESEWFPAL VKSALFQRCL PDIEGDISWF PAYEAAKAFA EMRHSPEPFL HLIHPRPVRW
HTVIAPIAEL FNVPLVPHEQ WVSALEKSVE AGSAAEVEAM RQNPALRLLP FFKAVKPAVD
GREALGLVSL STEKATRVSP SLAQMPMLDA ERARAWVAAW KRSGFL
//
