ID A0A2P6VJ49_9CHLO Unreviewed; 1585 AA.
AC A0A2P6VJ49;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030268};
GN ORFNames=C2E20_2613 {ECO:0000313|EMBL:PSC74125.1};
OS Micractinium conductrix.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Micractinium.
OX NCBI_TaxID=554055 {ECO:0000313|EMBL:PSC74125.1, ECO:0000313|Proteomes:UP000239649};
RN [1] {ECO:0000313|EMBL:PSC74125.1, ECO:0000313|Proteomes:UP000239649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 241.80 {ECO:0000313|EMBL:PSC74125.1,
RC ECO:0000313|Proteomes:UP000239649};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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:PSC74125.1}.
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DR EMBL; LHPF02000005; PSC74125.1; -; Genomic_DNA.
DR STRING; 554055.A0A2P6VJ49; -.
DR Proteomes; UP000239649; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000239649}.
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 757..784
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 517..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1585 AA; 167148 MW; 7A6B41FD02125E37 CRC64;
MEDSGMTSSP EGGPGPGAAP QPPPDGAADA WALDVSGAAA SSPKHANPTP AEAEPPVAAP
AAHGNTSVPD ADADAARVAA AERPVVPLPA QPLARAACAH DPPAPAGAAH AGERDGLANG
ATHPPAAPPA PLERPDAAAA AAEAEAALGV AAVPPPQLAD ADAKAEASRR AQLVADWARA
AVNNPGEVWQ AQHATSVAAA AAAGASQQQQ PAQADQKALR AEDIVRPAQQ HAEAGAAHQA
QQQQQQQQQQ VHLNIATGVR VHQRAATVEE AAAELAAAAA AAYDAPHQHP SFLQQQQQQQ
AGYYQQQQEA YYLQQQQRQV LGGGGRGQWH RAVVQEAGPE ADFMLSGLPY AQDGERRHHL
LKHELPDEAK GVNALRFFGV DNVRQAVRRI NKMAQRELQE MFQRVYGVRS SSNNNLWLRK
KLIEAVNTRP KNGSSPLPVS GHDAATAPRA GGDGGAGSDA ATLRRRRKKS SAPVRASDGV
QADPENAAEA LLTMLGGGPD GSDDGDDSLS SGNGEPRFAA PPPPAAPPPA KKPKLEAVVR
PRTQRAAAVN AVAAAAKAVL FDTPMEIDTA PGFSSGVRGT YGGRGGGRAA GSGAAAGARG
RGGRGRKEQE EDHQPSWSMQ QPYGYGADPA CQAQQQGGFG APPAADPNQP PHVQLLRMLL
QQQGAAPAAT AWGQQPHQQQ QQQQGYGAPQ QAQQGYGYHP PAAQHQQQAP APGGNVFAEL
LSTLLQRQQA AAAPAPAQPA ADPVMAAALR MLPPEAAAAA QAALAQAQHN AAAQQAAASA
QQQQQQQPAA ATMLAAAAKD LLASLLQHQQ GQAAAAAAPP AAPTNGGAQQ GMDSLLQDPM
LARLRQQFME HQQQAQQQGP EQQQQLLLQR HQQHVERQQQ QAQQHALAQQ QQQPGEVQRS
EREGSQEASA AVRSPHAGSQ PPAGAHGTAQ LEGKVAAAAG GSAAAVKEEL ASDGQLLDAG
AGAEQPANGG GPLHKEAAEA AQDAAARQSP VAPDALQASP EEEAPGGEAA AARAQQQEQQ
ARQEQQAQQH QAMLQAMLPQ LLAQNPLLSR LREQMQQQAA QQQQAAQQQQ AAQQQQQAAQ
QQQAAPAPPP VSAGRAPDAA TPASGNLHAQ LLAGLMQQQR LAAVVGAPQQ QAQQQQPGEG
AAPGATGNEL LARLLLRAAS GQHSSGSGSS MAALEGQSLT TGEQQPANGQ QQQDGEQVIT
PWDVTGGADG KIDYNKLVAQ FGCQSIDEEL VARIERLTGR PAHPFLKRGI FFAHRDLKEL
LDAHERGEPF YLYTGRGPSS EALHLGHLVP FMFTKWLQDA FKVPLVIQLT DDEKFLWRGL
AVEEARRLAR ENAKDIIACG FDVRRTFIFS DFEYVGGAFY RNIARIQRCV PMNQVRGIFG
FTMDDHIGKI AFPAVQAAPA FPDTFPHMFG ERKDVRCLIP CAIDQDPYFR MTRDVAPRLG
HKKTALIESR FFPALQGESG KMSASDETSA IFVSDTPKQI KAKVTKYAFS GGGATVEEHR
AKGGNLDVDV PWKWLNFFLE DDARLAQIGE EYSSGRMLTG EIKGELVGVL TEMVERHKAA
RAKVTDDIVD AFMSVRPMPW DQMYG
//