ID A0A1V4JF82_PATFA Unreviewed; 494 AA.
AC A0A1V4JF82;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Threonine synthase-like 2 {ECO:0000256|ARBA:ARBA00021942};
GN Name=THNSL2 {ECO:0000313|EMBL:OPJ70770.1};
GN ORFNames=AV530_017145 {ECO:0000313|EMBL:OPJ70770.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ70770.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ70770.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ70770.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ70770.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ70770.1}.
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DR EMBL; LSYS01007721; OPJ70770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JF82; -.
DR STRING; 372326.A0A1V4JF82; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR CDD; cd01560; Thr-synth_2; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648}.
FT DOMAIN 2..81
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 105..398
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 469..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 494 AA; 54829 MW; B2D63C930CF3D826 CRC64;
MEYISTQGGV GAVDFEGALF SGYAPDGGLF MPQSIPTLDW DTLQRWSCLS YRELVKELCS
LFITAKLVPR DTLNDLIDRA FSRFRHKDVV HLSRLKDGLN VLELWHGVTY AFKDLSLSCT
GQFLQYFLEK KQKHVTILVG TSGDTGSSAI ESVRGQKNMD IFVLLPKGLC TQIQELQMTT
VVEDNVHVFA AHGNSDEIDE PIKELFADVD FARKYNLMSL NSVNWSRIMV QIAHHFYAYF
QCAPSLDTTP LPVVEIVVPT GGGGNITAGC IAQKMGLPVR LVAVVNSNDI IHRTVQHGDL
SVSESVKATL ASAMDIQEPY NMERIFWLLS GSDSHLTKML MEQFSASKSL KLPEDLHRKL
SKTLQSCSAS DEDIVRAMQR CWEDNRYLLC PHSAVAAHYH YSQLDSTPRC CLAPASAAKF
QDAMLRAGLA PQLPPGIATL TSMETRSIPL EQGQDWAQAL RERIKAMAQR WETQGGQSAP
PGQGEITRQG VTQT
//
