ID A0A0V1PL10_9BILA Unreviewed; 716 AA.
AC A0A0V1PL10;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN Name=AcCoAS {ECO:0000313|EMBL:KRZ96869.1};
GN ORFNames=T08_6170 {ECO:0000313|EMBL:KRZ96869.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96869.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ96869.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96869.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ96869.1}.
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DR EMBL; JYDM01000006; KRZ96869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PL10; -.
DR STRING; 92180.A0A0V1PL10; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR CDD; cd05966; ACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
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 PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF244; ACETYL-COENZYME A SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..100
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 107..368
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 399..530
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 591..675
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 716 AA; 80100 MW; 82D5FBCFB4EB2FB3 CRC64;
MSDNVRMATF SIASEEDEQA ILPPPHLSEK AHCSSFSNYL EMYSQSVKDP EAFWTSFANE
LTFFKKWEKG CFLDYNFDRR KGPVYVRWMP NASLNVCYNC LDRNISRQLG DKVAFYWEGN
EPGVSMKLTY RELLKLVCKF ANVLKRKGVK KGDRVIIYMP MILELPIAML ACARIGAVHS
TVFGGYSAQA LAQRIVDAKA EVVITADGSY RGKKPILLKQ ITDQAISICE KRNVIVKHRI
IVRHLADNYT GFPSTQQDCK SKLQVQNCWF DEEMSAADEN CESEWMDSED PLFILYTSGS
TGVPKGVVHT QAGYLLYVYT TFRYVFDYQD DDVYFCTADI GWITGHSYVV YGPLANGSTV
VMVSGNLLAV ACALFNQNEQ QMINFIQTFQ FEGVPYYPEP SRYWDVVDKY GVSKFYTAPT
AIRHLMKFGS SYVERCRLDR LEVLGSVGEP INPEVWQWYY KVVGKSRCAI VDTYWQTETG
GHVLTPLPGC TNMKPGSASF PFFGVKPVLL NHDGQEIVGP GEGQLAFSAP WPGIARSLYG
NHDRYMDTYF AVPGYFSTGD GCTRDEDGYY WITGRIDDMM NVSGHLLSSA EIENAVVSHP
AVAEAAVVCA PDPVKGQIPY CFVTLKKVGG VVVDYAFTAE LVLDIKQTVR NQIGPVATPE
VFQQAESLPK TRSGKILRRV LRDVAGGNTT SFGDLSTLSE EHVIADLVNS RSSGIR
//
