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Database: UniProt
Entry: A0A0N7G7K4_CEV01
LinkDB: A0A0N7G7K4_CEV01
Original site: A0A0N7G7K4_CEV01 
ID   A0A0N7G7K4_CEV01        Unreviewed;       376 AA.
AC   A0A0N7G7K4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE            EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN   ORFNames=ceV_127 {ECO:0000313|EMBL:ALH23033.1};
OS   Chrysochromulina ericina virus (CeV01).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae.
OX   NCBI_TaxID=455364 {ECO:0000313|EMBL:ALH23033.1, ECO:0000313|Proteomes:UP000203826};
OH   NCBI_TaxID=156174; Haptolina ericina.
RN   [1] {ECO:0000313|EMBL:ALH23033.1, ECO:0000313|Proteomes:UP000203826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CeV-01B {ECO:0000313|EMBL:ALH23033.1};
RX   PubMed=26634761;
RA   Gallot-Lavallee L., Pagarete A., Legendre M., Santini S., Sandaa R.A.,
RA   Himmelbauer H., Ogata H., Bratbak G., Claverie J.M.;
RT   "The 474-Kilobase-Pair Complete Genome Sequence of CeV-01B, a Virus
RT   Infecting Haptolina (Chrysochromulina) ericina (Prymnesiophyceae).";
RL   Genome Announc. 3:e01413-e01415(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC         diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC         Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC         ChEBI:CHEBI:456215; EC=6.3.4.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00000047};
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DR   EMBL; KT820662; ALH23033.1; -; Genomic_DNA.
DR   RefSeq; YP_009173382.1; NC_028094.1.
DR   GeneID; 26048994; -.
DR   KEGG; vg:26048994; -.
DR   OrthoDB; 21892at10239; -.
DR   Proteomes; UP000203826; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR   CDD; cd01992; PP-ATPase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012094; tRNA_Ile_lys_synt.
DR   InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR   NCBIfam; TIGR02432; lysidine_TilS_N; 1.
DR   PANTHER; PTHR43033; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43033:SF3; TRNA(ILE)-LYSIDINE SYNTHETASE; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000203826}.
FT   DOMAIN          68..234
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
SQ   SEQUENCE   376 AA;  44602 MW;  3C75B6DE6D3C6BA9 CRC64;
     MNAMYGFVKT TLYNLIYNDK LYNIDFDKYK NILEYVPNVQ LKIQEQNIAD EEIMKKISEF
     CKLLDNKKVL VSLSGGVDSM VLITILHWLD FDIVAGHINY NNRNETTIEE EFLQQWCLFN
     NIKLYIKNIN NIKRSTIKRS EYELITKNMR LDFYKEIIAT ENIDYVLLAH HKDDIIENVF
     ANICRGRNYL DLAVIREHTT ISEIKIGRPM INYYKTAIYE FAHKYQVPYF LDTTPKWSIR
     GKYRDVISPA IEDAFQKNVK ENLISISDQA DQWNSLIEKQ IIQPFIEKIK INLIDNKTSI
     EFNIEKYINY PIAFWSVVFM NLFNQFGSKA PSKKSIQTFI NTIKYRVRQN HSHKYNITLC
     NNNKCTIKNY NVTIEF
//
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