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Database: UniProt
Entry: F0VEL6_NEOCL
LinkDB: F0VEL6_NEOCL
Original site: F0VEL6_NEOCL 
ID   F0VEL6_NEOCL            Unreviewed;      1257 AA.
AC   F0VEL6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Lysine decarboxylase, putative {ECO:0000313|EMBL:CEL66124.1};
DE   SubName: Full=Putative lysine decarboxylase {ECO:0000313|EMBL:CBZ52160.1};
GN   ORFNames=BN1204_019490 {ECO:0000313|EMBL:CEL66124.1}, NCLIV_019490
GN   {ECO:0000313|EMBL:CBZ52160.1};
OS   Neospora caninum (strain Liverpool).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX   NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ52160.1, ECO:0000313|Proteomes:UP000007494};
RN   [1] {ECO:0000313|EMBL:CBZ52160.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CBZ52160.1};
RA   Aslett M.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBZ52160.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CBZ52160.1};
RA   Reid A.J., Sohal A., Harris D., Quail M., Sanders M., Berriman M.,
RA   Wastling J.M., Pain A.;
RT   "Comparative genomics and transcriptomics of Neospora caninum and
RT   Toxoplasma gondii.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {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).
RN   [4] {ECO:0000313|EMBL:CEL66124.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CEL66124.1};
RX   PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA   Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA   Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT   "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT   Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT   Transcript Features.";
RL   PLoS ONE 10:e0124473-e0124473(2015).
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DR   EMBL; FR823388; CBZ52160.1; -; Genomic_DNA.
DR   EMBL; LN714481; CEL66124.1; -; Genomic_DNA.
DR   RefSeq; XP_003882192.1; XM_003882143.1.
DR   AlphaFoldDB; F0VEL6; -.
DR   GeneID; 13443925; -.
DR   VEuPathDB; ToxoDB:NCLIV_019490; -.
DR   eggNOG; ENOG502QWPE; Eukaryota.
DR   InParanoid; F0VEL6; -.
DR   OrthoDB; 246721at2759; -.
DR   Proteomes; UP000007494; Chromosome VIIa.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR011193; Orn/lys/arg_de-COase.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 2.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT   DOMAIN          472..700
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          747..938
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   REGION          49..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1157..1257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1039
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1169..1247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1257 AA;  138963 MW;  D5AB780FCDD4DB10 CRC64;
     MLERRGTLRY GAARRLRQFG SRDSILLTPG ASFSMQSSSG LFLPQLGAAE PRSLSRDSDS
     PRDFDVDSAM RTNPRHMRGG YPGQGDRDRG ERERSRSYLG HAPLGRGLSP ANGGDGREDS
     GGYGGRGQLA GRGGRDRDDA SEGDSALGRG LYWAGEKSRG ERGDARLADM TSALSITTED
     DFAAGGPNAE HAWLRKADTF TQADEDLVSS ETTYVAMLRE ELWQALSAHV AMWRKEKIEA
     GLNCLEQIEW FWGAEGMQKV HEVRALVKDN KMDSAGVVIS SVTASMSSVT GSMQGRHHCF
     YVLVVVPPCT FRNRDHRVNL AAELRRIASK EQSQDSSLVY RIVEVDSIRR ALLATIVNPD
     ILAVVLQDNV PIEHSHSSHA LVGFEAFVRG IDVFVETPVT KMRAGAPVLA TVIQSIAQCR
     SNIDVFCVCT AMGLATLEPV SHLVKRAFFP NDDHSDLHEA ILAGVRSKMR CPFFEALRRY
     AERPIGVFHA LAISRGNSVR RSKWIQGLIE FYGVNLFKAE SSATCGGLDS LLDPHGSLLD
     AQNLAARAYD ANYAFFVTNG TSTSNKIVLQ AVLRPGDVVL VDRDCHKSHH YGFVLAGSSP
     CYLDAYPLHR FSMYGGVPLE AIKRTLLAYR SAGRVAEVKL LVLTNCTFDG IVYNVKRVVE
     ECLAIAPHLV FLFDEAWFSY AMFHPILKRR TAMHAANEIR RCLMEGRYHR RFQELLETLG
     TDDLTSVDAE TLVKTRLYPD PRRMRVRVYA THSIHKSLTA LRQGSMILVN DDLFESHVHT
     PFKEAYYTHM STSPNYQILA TIDVGRSQME LEGYGLVERQ IEAAFFIRRL LTRDLLVRKY
     FTVLSPRDMI PAAMRKHSKA LLGEEALQCE MNLQTLEQVW LTDDEFVLDP TRITLFTGLS
     GLDGDTFKVK WLMDKYGIQI NKTSRNSVLF MTNIGTTRSS CVFLKACIRS CAQELEMHRL
     MSSTRELEEV NDAIRALVED CPDLPNFSAF HPAFKKTLFP HDVCEPPNEP SPAAEGGASE
     GSGDGAKPAR ERERGDGDQK GATAGSTPGE DALSLVRDGD LRAAFYLAYD EDVVRYLSLR
     ETKEAILRGE QLVATTFVIP YPPGFPVAVP GQVLTLALVD FLLKLDVKEI HGFDHKLGFR
     LFTEGILNDQ LRQRRAAERE KTDLQGMRLL PSAPQNVNVT VSPPCGATVE SEASPPSVSA
     GRETPDNAAK SSSSANGNEL DSNHAKTGST STNDTRRSDT SSSPPPSGRE GKREPNP
//
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