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Database: UniProt
Entry: A0A1A8VN60_9APIC
LinkDB: A0A1A8VN60_9APIC
Original site: A0A1A8VN60_9APIC 
ID   A0A1A8VN60_9APIC        Unreviewed;      2249 AA.
AC   A0A1A8VN60;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Lysine decarboxylase, putative {ECO:0000313|EMBL:SBS80202.1};
GN   ORFNames=POVCU2_0003980 {ECO:0000313|EMBL:SBS80202.1};
OS   Plasmodium ovale curtisi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=864141 {ECO:0000313|EMBL:SBS80202.1, ECO:0000313|Proteomes:UP000078560};
RN   [1] {ECO:0000313|Proteomes:UP000078560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Naeem Raeece;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FLQU01000052; SBS80202.1; -; Genomic_DNA.
DR   Proteomes; UP000078560; Unassembled WGS sequence.
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; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 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:UP000078560}.
FT   DOMAIN          543..768
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          820..906
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   REGION          1046..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1480..1500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1721..1747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1961..1981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1087
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1480..1499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2249 AA;  255468 MW;  01EB735E6C51EE98 CRC64;
     MNTANDAMFY SANNFVYAVN FSENNPEKET KSMNEGNDCI PSSNALSEEL GSVAERDEVA
     SNDSICRNRN VSRNGNANSN IITNLSKNQS AIQSSINSAI HSAIHSSIQN SIQSSIQNVI
     PSTSRHHYKD AKDLSQKWKK EESYQIGSRR REKNRLKSSK YEKINVLERY INISNATNVC
     SLRIKLWEAL MLYVNKLHLE FVYFILNCLE EIEVYWGEEA TNNLQDILNL VNDKKYKDVL
     YKIGEILSSL SVTTSKSTEE NPFFYTLIVS AKRDENNNNN NYNSDLSCEL SKIIQYEHNR
     LSNQNNNKKL EYKIIEVSNA KEALLACLIN SQILSVVLVD NLVIDEEFTK EKDYFPYIDD
     NALNNNCVNN SYLLNCNTTN STQIKTPLSH NIGNNGGSPG NKDTVRGSLS SCRHNISNGQ
     MCNHGQMCNH EHSRSSGSES KRQSSFLLKR DYKFEIGDFV LGYDQLVAAP LEKMKKGYNS
     LVILIKSIAY IRSSVDIFCV CTSITLDKLQ SVNNKIIRIF TTHDDHSDLH ESILDGVKKK
     IKTPFFNALK SYAERPIGVF HALAISKGNS VRRSRWIQSL LDFYGVNLFK AESSATCGGL
     DSLLDPHGSL KEAQIMAARA YGSKYCFFVT NGTSSSNKIV MQALVKPGDI ILVDRACHKS
     HHYGFVLCQA LPCYLDPYPV SRYGIYGAVP IYVIKKTLLE YRNSNKLHLV KLLILTNCTF
     DGIVYNVKRV VEECLAIKPD LIFLFDEAWF AYACFHPILK FRTAMAVADK MRSKEQKKVY
     YKIHKRLLKK FGNVNSLHDV PVDYLLKTRL YPNPSEYKVR VYATQSIHKS LTSLRQGSII
     LISDDNFESH AYTPFKEAYY THMSTSPNYQ ILATLDAGRA QMELEGYGLV EKQVEAAFLI
     RKELSEDPMI SRYFRILNAE DLIPDSLRQC AVSYMKRKNK IYSKEGSPSL SKCSDNVTYS
     CISNNIAKRA TDQSENTKYR ICHKKPNFSS CEGVHEVVES ATGLGVTFSN DSHISNGFVS
     SGSGRYESCN PARGNRLREG HLREGRFQEN HFSGNDPQMS RVTDGKKKKK KRNDISSVTH
     DDDNSNDSTN SENECFSIEE SRENKNGNCS CNSSNYLNNF LEYFECSWLS EDEFVLDPTR
     ITLFTGYSGI DGDTFKVKWL MDKYGIQINK TSINSVLFQT NIGTTGSSCL FLKSCLSLIS
     QELDQKKTLF NERDLNQFNE SVYNLVSNYI ELSQFSGFHP LFKKRYSTSS IFNREGDLRK
     AFYLAYEEDY VVYILLLDLK ERIKKKEMIV SASFIIPYPP GFPVLVPGQI ISEEIVDYLS
     GLSVKEIHGY DENIGFRCFY NFILNYFYHI VTSDPYAYYQ KMDKKTYDKL KLSSLNKKKN
     TDDIYHLYIY DKDRNKLKKI YLRNGRNAST DNNTTVSDSY EEVTSCSIPH IGPVRRCVPA
     ISSVSAVSGG SAIGRIDAQK QCSEKEDNFC DVNGENGLSN DISSLNNSEN TSPQKKSSTE
     SIIKKGHYNE STMKGKKNLR KYISVPNNIR TDEYNVFLSK IKEGEFEIIG TPKNDNRNFL
     VNSANCYYNK KAKDLIRQTN GFKKIYKDHT HLCTEDNLIV DRDICNSSGS NGQNHFERKK
     NMIKNDLPLS NREEVGMEVE NWEEARIGTA NWEKVPNGEH LSNVVFKKHR GDVIFEEDRL
     SVRRTCNVGI SHRLSGRRRG NVSTANPENA ILQAGQVNAV RSKPGKGTGR GVGKNRNGII
     TERGNIPNGS ITNKQNMLYS FSDVYSIRQV GKMNNKDGEK YDHILTDVVP KIKQSNIILY
     NKINNNSMLV QRKRLSNVND YTCNLNEKNN HKEYRGKDFV CYSDSNKKNK NVMYVKHEEE
     YVKEESDQDI NENIFEYNNK LFRVNRVIGK KEDDNGIGST GVIRGHNIEM SRCLEFTQGQ
     PTREEKKGRD MHSNVNSVSN VRNLTNGSSS MGNRIRAGII GNRSRGRTRV KKQSNRSSMQ
     EPLAHVSYLP EQNIKRNVEE MYIEGEPIRE RDTEQNVFIS KVPSERDGLN GKGLSHTHCP
     NEAKSHNYAN ENMCTDMNYV TKEGDMEGVV NGNAHEYPNE GSNGLVNVLA NDNSSFKSSQ
     KSSDSSNCRD EWGQMGDVHL NFVGNDQGHG KLNTQEKIET EICRSSFPFN EKELNKDPVL
     LENAGDRNSP RKLNTLNNNS YINNLITNVD DDTFVHKEGN FFLECAMTNS EINCSSFEMD
     MSLNNIYSHD GDGIGQHMHR GGDKKGEFK
//
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