ID S7WAD5_SPRLO Unreviewed; 597 AA.
AC S7WAD5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:EPR79846.1};
DE Flags: Fragment;
GN ORFNames=SLOPH_98 {ECO:0000313|EMBL:EPR79846.1};
OS Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC Spraguea.
OX NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR79846.1, ECO:0000313|Proteomes:UP000014978};
RN [1] {ECO:0000313|Proteomes:UP000014978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA Williams B.A.P.;
RT "The genome of Spraguea lophii and the basis of host-microsporidian
RT interactions.";
RL PLoS Genet. 9:E1003676-E1003676(2013).
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:EPR79846.1}.
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DR EMBL; ATCN01000090; EPR79846.1; -; Genomic_DNA.
DR AlphaFoldDB; S7WAD5; -.
DR STRING; 1358809.S7WAD5; -.
DR VEuPathDB; MicrosporidiaDB:SLOPH_98; -.
DR HOGENOM; CLU_457214_0_0_1; -.
DR InParanoid; S7WAD5; -.
DR OMA; HASENYK; -.
DR OrthoDB; 911at2759; -.
DR Proteomes; UP000014978; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000014978}.
FT DOMAIN 1..565
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 159..395
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 300..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 597
FT /evidence="ECO:0000313|EMBL:EPR79846.1"
SQ SEQUENCE 597 AA; 69447 MW; 142204996199BD7E CRC64;
MQHRILIANN GLSALKFILS IKKIDHNKKY NKCEKLNKKN NYDNKKDLID KKFCGASFDK
NEFVLIGMAT SEDIDGNYLY INYLDEIIHV ESGPSEKNFG NIELIAKIAI EKNIDMVYPG
WGHASENYKL PEKLSELGIK FIGPSKDAME MVGDKIGSLK LCEKLKIPTV PWQSITFTNK
HKQEKNNCIK DVLSNFIDKY KYPIMLKTSS SGGGEGITTI RNQHDLEMIE KTPANIDELF
VCKLIEEARH IEMQVIADNH KNVIILGGRD CTLQRRYQKL IEESPPVIVS KRNKHKINNS
KNEEEFHRTD KSMKEKNKSK HDNTRVYHLM KKYSKKLILS SNYIGVATVE FLYLPKSNEF
YFLEINSRVQ VEHPCTEIRY DIEIPVIQLL IALDYKIIKE TIKKKDKKNK CNTAKINDRD
NNKKEKTKDD TKTVNNYSNT IIIKKNKTKQ HVIGIRIIAE DNNFNPVTGN PSIETNIYKN
NNIYAYFSLL NGKLNKYADS QYGHIFITGK NRRAAINNCI KFLESNTNLK IRYIDTHLEF
IKYVLQSKIF RENEYYTDTA EKIKKEFINK KRYDNIDNYK NDKDLKIIND IDRKSGS
//
