ID A0A0A0AD81_CHAVO Unreviewed; 453 AA.
AC A0A0A0AD81;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:KGL91443.1};
GN ORFNames=N301_15268 {ECO:0000313|EMBL:KGL91443.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL91443.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL91443.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL91443.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|RuleBase:RU003737}.
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DR EMBL; KL871239; KGL91443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AD81; -.
DR STRING; 50402.A0A0A0AD81; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00622; PLPDE_III_ODC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR002433; Orn_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR11482:SF4; ANTIZYME INHIBITOR 2; 1.
DR PANTHER; PTHR11482; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01179; ODADCRBXLASE.
DR PRINTS; PR01182; ORNDCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
PE 3: Inferred from homology;
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858}.
FT DOMAIN 44..278
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 280..380
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
SQ SEQUENCE 453 AA; 48873 MW; 7F1ED816C4B1C309 CRC64;
MNGYLDESNF MMVEEGFTTR DLLENLLVEL CQASDQQAFF VADLGDIVKK HLRFLKALPR
VKPYFPVKCN DSEGVIRLLA ELGAGFACTS KAEIARVQSI RVPADKIFYS SPCKQVAHIK
YAASHGVQLM TFDNEVELSK VARSHPQARV LLGVAADSGP PALPGMMFGT TLKSCRHLLE
TAKEQAVEVV GISFHLGSRG LEPQTFAQAV AVAQLAFEMG TELGYQMHLL DIGGGFPGTE
DTRARFEEIA AVINSALDLY FPDGCGVDII ARPGRYYVTS AFTFAASITA MDEVPAEQPG
SDGGWDGGMV GWADPCARAP LSPLPAPLQR KNLAARGASY HPLHSSSLRG PPGHGEDCIA
DGLELPQLQV GDWLIFKDMG AYTIATSSLL GERPQPQITY AMSHVAWKAV QLFQGKPPQT
EDDHETVCAP LSCGWEMAET LCATPVFAPA SII
//