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Database: UniProt
Entry: C8V691_EMENI
LinkDB: C8V691_EMENI
Original site: C8V691_EMENI 
ID   C8V691_EMENI            Unreviewed;      1052 AA.
AC   C8V691;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=NRPS-like enzyme, putative (JCVI) {ECO:0000313|EMBL:CBF75107.1};
GN   ORFNames=ANIA_10486 {ECO:0000313|EMBL:CBF75107.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF75107.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA   Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA   Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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DR   EMBL; BN001302; CBF75107.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8V691; -.
DR   STRING; 227321.C8V691; -.
DR   EnsemblFungi; CBF75107; CBF75107; ANIA_10486.
DR   VEuPathDB; FungiDB:AN10486; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_002220_2_1_1; -.
DR   InParanoid; C8V691; -.
DR   OMA; QNMGYAQ; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR   GO; GO:0044550; P:secondary metabolite 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.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560}.
FT   DOMAIN          553..634
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1052 AA;  116760 MW;  2EE8D8A682CEF37A CRC64;
     MLSTIRPQAP THIDKLAHDT EDVASPQAEP LTVDELVRHR ASLGPSQPVV YYPRAGIEYS
     EFPLQNLDVF AYRVAKILAE KIPPRKSSSE CPAVVALLGP SNLDYLVLLL AVTKLGHAGL
     LLSTRISVEA HVSLIERTNA QHMFVHGSFR DIAAKVSERI PLVQVHSIPS EENYDYHIPD
     EPIDTNLLSH LDPEVETKHL AWIIHSSGST GLPKPIFQSQ RAAVKNYAGN MNMRGFITLP
     LYHNHGICCL FRTIYSNKTL HLYNPQLPLT SQYLVEIMRS YNFEIFYGVP YALKLLAESE
     EGIEALAKLK AVMFGGSPCP DSLGNLLVEN GVNLIAHYGS TETGQLMTSM RPPGDKRWDW
     LRPSETVKKY LRMEERYPGI YESVVLDGWP SKVMSNRPDG AYATKDLFLK HPEMEAYKYY
     SRLDDTITLV NGEKVIPLDL EGRVRQLSVV ADALAFGIGK SNIGLAVIRA PEAASMTDEQ
     VIDAIWPAVE DAHQTLPAYG LLPKNMVRVL PADAPYARTD KGTVIRQAFY RDFADLIEAS
     YEAGDDMTGT MLLSEEELKA FLHKELSAIV PARTTNGFTD EEDFFSLGMD SLQASQLRSV
     LVKSLDTKGY KLGLNVVFEH PSIASLARYL FSLTSKTLET MASIEEQMEA LISKYSDFEH
     HVPRPNELSG RYIVVTGATG SLGCHVVAKL STLPDVQKIY CFVRANSTLD AYGRLLGSLR
     TRRVYDTLST SAKNKLIALP SNLALATLGL DTMTYNTLTS TITDIIHCAW SVNFTLHLSS
     FEKDNIAGIQ HLANLCLRAQ RPAPATLNFC SSISAVVRSP EPSIPESLPL SLAHAQAMGY
     AQSKLVAEHL CVKAYQQTGL CTRVLRIGQV VADTENGIWN TTEAIPLMIQ SATTIGALPK
     LDEFHRWLPV NTVAGVVVDI ALSESDVDGP KDAQAIYNII SPYPFHWTNE LLPCLRDAGL
     VFEELDTRTW LKRLRESNPD PQANPPIKLV DFWTGKYDHD FPPRVVGWET GKTKAVSRTF
     GQAKKLQRDI VQKMMSYFFG VDGWGKGKVK LT
//
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