ID   A0A452I109_9SAUR        Unreviewed;       452 AA.
AC   A0A452I109;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Selenocysteine lyase {ECO:0000256|ARBA:ARBA00040554};
DE            EC=4.4.1.16 {ECO:0000256|ARBA:ARBA00039054};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000021151.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000021151.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the decomposition of L-selenocysteine to L-alanine
CC       and elemental selenium. {ECO:0000256|ARBA:ARBA00037407}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
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DR   AlphaFoldDB; A0A452I109; -.
DR   Ensembl; ENSGAGT00000024088.1; ENSGAGP00000021151.1; ENSGAGG00000015537.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.10.260.50; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11601:SF62; SELENOCYSTEINE LYASE; 1.
DR   Pfam; PF00266; Aminotran_5; 2.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT   DOMAIN          36..121
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          139..434
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  49522 MW;  A993EFC218F78F47 CRC64;
     MEGDQVEKMV LTKDGRKSAV DKECDGEENK SVESKVYMDY NATTPMAPEV IQTVTEAMHE
     AWGNPSSSYT AGKKAKEIIN KARESLARMV GGRPQDIIFT SGGTEANNLV IHTALRHFRE
     SRVLGQDGPG EDHKRAAGAT PHFITSNVEH DSVRLPLEHL VKEHMAEATF VPVSKITGQV
     EVDDAIAAIR PTTCLVSIML ANNETGVIMP ISELSQQIQI LNQNRMALGL PRILMHTDAA
     QMIGKGRVDG QDLGVDYLTI VGHKFYAPRI GALYVRGPGV TTPLHPMLFG GGQERNFRPG
     TENTPMIAGL GKAAELVNKN CEDYEAHMKE VRDYLEERLE ASFGKQRLHF NSRFLGAKRL
     CNTCNFSIWG PGLQGRMVLS HCKNLLASVG AACHSEKGDQ PSSILLSCGI PCEVARNALR
     LSVGRDTTKE DVDIIVEDLK QSVAQLEQNR VT
//