ID A0A158R4S1_9BILA Unreviewed; 2167 AA.
AC A0A158R4S1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|WBParaSite:SMUV_0000424101-mRNA-1};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000424101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000424101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
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DR STRING; 451379.A0A158R4S1; -.
DR WBParaSite; SMUV_0000424101-mRNA-1; SMUV_0000424101-mRNA-1; SMUV_0000424101.
DR Proteomes; UP000046393; Unplaced.
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 GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 2.40.50.100; -; 1.
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 Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR049074; ACCA_BT.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013537; AcCoA_COase_cen.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF08326; ACC_central; 2.
DR Pfam; PF21385; ACCA_BT; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 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}.
FT DOMAIN 48..550
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 206..400
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1422..1754
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1767..2077
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2167 AA; 245957 MW; 2B4E90D378F1E907 CRC64;
MPTPSLLIHK NREFPDFEKS NEVDQRAETF STVEEFLGKY ADPKLARPIK TLLIANNGMA
AFKCVMSIRR WAQETFKDDR LFKFINLTTE QEISSNPEYL KMIDNFVFSQ SGGNESNYAN
VDEILKHATS NQVDAVWAGW GHASENPDLP NGLKQKNILF MGPPGTAMFT LGDKIASTIL
AQSAGVPTVP WSGSDIYLPK ELCDKGRSDI EVSNDLRMAA CVNDVNQAIS IIKEKNIPYP
VMIKASEGGG GKGIRKVRSE AEFEVNFRRV QAEIPGGHIF LMHCLEDARH IEVQLLGDMY
GQVISLRTRD CSVQRRCQKI IEEAPAIAAP TWVQRDMEAD AVRLAKMVGY VSAGTVEYLF
DPKTNKYYFL ELNPRLQVEH PLSEMLTNVN LPAAQLQIAM GVPLHCISEV RLYYGQSRYG
TDQIPFDQMH MKADKHIVSV RITSEDPDEN FRPASGEITN LNFRSTQFVW GYFSHVGAGS
LHEYADSQFG HLFATGSTRH LAISNMLNAL QELQLQSKFP VTVPYLISLF KDPEFENNAI
NTSWLDRRIA SKKHTVELPP LHMAVAYGSM LIAHSKITEA FSRFSNSISR GQILQPSELT
ETHQVELIYN NVKYSVTATR ISNFEYSVKL NGCSVSVEYR ELRNGTLLLK YNDRSHPCYM
DEEAEKYKVH IGRMQIVFEK ENDPTVLRSS CAGKLLTYEA EDGEILKPGQ LYASMESMKV
VLDMKVKKVG GRFKRIAQIG QVLHPGTLVG RLEEVVGTTS TKPHDFDGIF EEWKNSPTKV
LPINMRFNEI VQECRNVFDG YCKSEPTFSR HCELLVKDLF SVLFEPSLAF EQMRQILAVL
KTRIKPEVFE RLNGIIKHRI AEFPAKSVQN AVNEYLEMLD PQQYSVERLN FTPIIAICEK
FSSGTEGHTA LVLKELLEYY LQTEKYFQYY QYDKCVSNLL SEVKDAEKCV RTIYSHTRVN
EKNVLSMKML ERMGSDRRLV LSLSSVLEKL ASFVKNENLE LAHLARKMLI DAETPTFMEI
KRRGSSPSPS NIEKYDLLFE TFDSNFDSVL KYVTVCCGVP ESSILRLSDG GHPNDVQFPI
RVQKIAHGLG LPNDNVEERN VELRIIGDIY DVGGRLPKLA AKVTKPNSTL FLVSRIDAPK
RDITSKQKFS EIEEKLAAIL KEAVMRLDSP KIRELVAMVA PSDSYPLFFH FSMATREEVV
CQRNIDFAHL PKLGLHRLSE NYNIEKVRTH TPYSSGHLYR AQGKQDPTEQ RFFYRAVVRV
VDSYTASEVV KTVEKALRRA CLEIKVALYR SSTIDRNHVF LFIERTPSSN KIQMSPADWR
NVIYKGYRDC KESLWRSLVN QIEVDFVLYG ESRSYEQATK ILITDDTGYT PCIKSLRAEA
SNGNSSVSKW LHVDAGMEGF EHGLEIMVEG NRNSEWNPFV DPYLGRSEID KRRLKARTAK
TTYVYDYPLL FQRALVSAWT TSPSSSKKPS QMPQDLCQFH ELVYDETEKR LIERDDAGSL
STIGMVAWRV RLVVPEYPEG REIIVIANDI SHQIGSFSMR EHNLFYEASK LSRNEGLPRL
YIAANSGARI GLSNDLKKLF KVKWKDEKNP VQGFEFLYLN DEDLEVVKNL VTTERIGSFN
KITGIIGKER DLGVENLVGS GLIAGESSRG YDEVVTYCLV TGRTVGIGAY VARLLKRIIQ
VENADIILTG APALNSLLGR EVYTSNGQLG GTQIMTRNGV THASVANDYE GVCQLLRWLS
HTRNSKNVCI KLILVMSPLN ITKCVDPIDR PVAYLPPSLK DSDPRYMLTG HQDPTTLEYL
DGLFDRGSFE EIKPEWGKTI ITGRAKLGGI SVGVIAVETR SVVTEIPADP AAPDSQVKNM
QQAGQVWYPD SAYKTAEAIA DFNKESLPLI VLANWRGFSG GQKDMFEMVL KFGSYIVDEF
SRYMHPVIVY IPPYGEVRGG AWAVIEKKIN PECMHMYADP RSRAGVLEPE GTVQVKMRKV
RDLVPLICRM DPEMRELLER QKAGDDVKNA IDERVEYLMP TYRNIAICFA DLHDTPIRTK
AVGAIQGIIR WEESRHFFAW RLLRLCFERD IYRECFEAKT VEELEVAHAA LRRYMKERKN
EVREWDEVPD EEAYNILFAE RADIVEYLSK INKLNSLCNV ASKFGVSIDR LGDFVTKCDA
LIREFSE
//
