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Database: UniProt
Entry: F0V879_NEOCL
LinkDB: F0V879_NEOCL
Original site: F0V879_NEOCL 
ID   F0V879_NEOCL            Unreviewed;       512 AA.
AC   F0V879;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Radical SAM enzyme, Cfr family, related {ECO:0000313|EMBL:CBZ49920.1};
GN   ORFNames=NCLIV_004040 {ECO:0000313|EMBL:CBZ49920.1};
OS   Neospora caninum (strain Liverpool).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX   NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ49920.1, ECO:0000313|Proteomes:UP000007494};
RN   [1] {ECO:0000313|Proteomes:UP000007494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX   PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA   Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA   Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA   Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA   Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA   Wastling J.M.;
RT   "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT   Neospora caninum: Coccidia differing in host range and transmission
RT   strategy.";
RL   PLoS Pathog. 8:e1002567-e1002567(2012).
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DR   EMBL; FR823381; CBZ49920.1; -; Genomic_DNA.
DR   RefSeq; XP_003879955.1; XM_003879906.1.
DR   AlphaFoldDB; F0V879; -.
DR   GeneID; 13445969; -.
DR   VEuPathDB; ToxoDB:NCLIV_004040; -.
DR   eggNOG; ENOG502QQ98; Eukaryota.
DR   InParanoid; F0V879; -.
DR   OrthoDB; 276083at2759; -.
DR   Proteomes; UP000007494; Chromosome Ib.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040072; Methyltransferase_A.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30544; 23S RRNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR30544:SF8; RADICAL SAM SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007494};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        486..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          86..328
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          16..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..66
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  56748 MW;  5FD6F24CB206A2E4 CRC64;
     MRYGAVAYAL FPEAKKKPRD ACVETSEAQP REEKGTAAEE EDEKEEDEEK EEDEEKEEDE
     EKEEDEERGE SVKLGKTSDV ARPFKSNRRA TVCLSAQVGC QMGCTFCATG TMGKKRNLAE
     WEILEQLYHA SRVEKIRNIV FMGMGEPLDN YNNVVASVRF MTQPNKFAIG GHHVCISTVG
     LPHRIRQLAS DLPTCRLALS LHAPDQPTRL KLMPRAAAGW KLDRVLDATD EFVKQQKRVN
     STAMKNIGLL VEYIMIQDVN DTIDQAHALG RILQPRADAV IVNLIPYNPT EVPYDYKPST
     PERVDEFLRI LRQDYSIKVL VRQTLGQDID SACGQLVVRA GKDKSGEKVP ERVARASHGA
     ARTRDARDAT PVESSAGSQW PFSSRDRESA CASKAPSGAA QISTRQKCSR SRSDERETDS
     DDASDDGRDK HSAVPLSSWW QDVKALPALM QSCKGMCADS LWTLATDAER EDEEEAVAAT
     HGKRTLLAAS VALLAGVVAA GVANWFLRRA RV
//
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