ID A0A162T573_PHYB8 Unreviewed; 672 AA.
AC A0A162T573;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=AMP-dependent synthetase/ligase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYBLDRAFT_128652 {ECO:0000313|EMBL:OAD66342.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD66342.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441004; OAD66342.1; -; Genomic_DNA.
DR RefSeq; XP_018284382.1; XM_018429230.1.
DR AlphaFoldDB; A0A162T573; -.
DR STRING; 763407.A0A162T573; -.
DR GeneID; 28990136; -.
DR VEuPathDB; FungiDB:PHYBL_128652; -.
DR InParanoid; A0A162T573; -.
DR OrthoDB; 45466at2759; -.
DR Proteomes; UP000077315; Unassembled WGS sequence.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd05943; AACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
DR InterPro; IPR032387; ACAS_N.
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 NCBIfam; TIGR01217; ac_ac_CoA_syn; 1.
DR PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077315}.
FT DOMAIN 48..105
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 110..426
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 672 AA; 75084 MW; CD3A7E20196872AC CRC64;
MTFSTTNKTD ALSTTPKCLW TPSNVSQTEM DKFRKHVNSK YNLKLADYTE LWKWSVTKID
AFWSTVWEYT GIISSQPATQ VIDLSVRMDA IPEWFKGARL NFAENLLWCR DPKKIAIIAA
GEGHPPEPMS YEKLYENVLQ CAEAMKSFGV KTGDRVAAYI PNCPEAIIAM LAATSLGAIW
SSTSPDFGTT GVLDRFSQIK PKILFSVNAV YYNGKTLDHT VKLNTVVKDL PSVETVVVIP
FIKDFVGQPV QKSQSWDQFL SKVPKSALPK KISFAQLPFN HPAFILFSSG TTGLPKCIVH
SGPGLLLQLK KEHVLHGNMH ADDVFFYYTT TGWMMWNWLV GALGIGATIV LWDGSPFKPA
PISLWKLVDQ LKITHFGTSA KYIQSLQEAK ISPKTECKLD SLKVVYSTGS PLKPESFDYV
YEHIKKDIML GSITGGTDIS SLFAGHNSAL PVYRGEIQCI CLGMKIEAWA DTNKPVYAQS
ADLVCTEPFP CMPVYMYQDP ERTKYRNAYF DVYDNVWYHG DFVWINPKTG GVVMLGRSDG
TLNPAGVRFG SAEIYNVADH FANHGIEDTL CVGQKIKDQD DERVVLFLKM KTGVVLTETL
VKDIKTKIRF ELSPRHVPAF ILPIEDIPYT INGKKVEVAV KKILSGQTIT PTGTLVNPKS
LELYYNIPAL KQ
//
