ID A0A0V0RRE3_9BILA Unreviewed; 1750 AA.
AC A0A0V0RRE3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=serine--tRNA ligase {ECO:0000256|ARBA:ARBA00012840};
DE EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
DE Flags: Fragment;
GN Name=Sars {ECO:0000313|EMBL:KRX17035.1};
GN ORFNames=T07_10315 {ECO:0000313|EMBL:KRX17035.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX17035.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX17035.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX17035.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001706};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily.
CC {ECO:0000256|ARBA:ARBA00010728}.
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:KRX17035.1}.
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DR EMBL; JYDL01000095; KRX17035.1; -; Genomic_DNA.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR021629; Mediator_Med23.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR033729; SerRS_core.
DR InterPro; IPR010978; tRNA-bd_arm.
DR NCBIfam; TIGR00414; serS; 1.
DR PANTHER; PTHR11778:SF7; SERINE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11778; SERYL-TRNA SYNTHETASE; 1.
DR Pfam; PF11573; Med23; 4.
DR Pfam; PF01569; PAP2; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRX17035.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1048..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1082..1101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1108..1126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1199..1215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1453..1693
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 1750
FT /evidence="ECO:0000313|EMBL:KRX17035.1"
SQ SEQUENCE 1750 AA; 201737 MW; C270C4357EEF6D00 CRC64;
MSVSLSDFEA KVKNLFKEHA KTGIAHFFFR PYLITSSEEC EKKILISTAN ELMEIFTSLP
QNLQESAFSI VISHRVLSNS ANRIVDFFVR NVTQRQMLSI KCICEKLLTC AELNINSCGW
NDTFAFFMEN ISLLDYKDLL NPQMRLLTHV FMHYTYRDAI AVLLGTAKPE KSRIPYFEEV
ITEIILELMF TAECDHSQLN PQAWRIISTQ IIYLTLQQSI CFTRLVKILH TKLTHYPYRY
ARNQLMWCLF NFLSGGMQKY SGKSAWPSPA LVETYCRMLT YPDLEILGLK QFTSHIVLTA
ARHQCCEMMY ICCEILNYRL FNIPSTYRVH AIVTLQQTLA FAKFQTNASL YWMYRYYYYY
YFAPFARLLN SFVAVAADGT KQSIAENEEL MRIIILTLAR STVISSKVLG PRKVLVHLKS
LADFLVYETN SADVNRCVDV LNRLIFKYAV VPLERFMLTM LLRDYEGNDA FYALLIVMLL
VQRSEELRSA VADCVAMLPS DYWHCQDWND KYQAYQTKHA ERTWSQVHVE LSRASLTPND
CPLPVYFGTR CLQMLPVVDL LLQKLVESPA ACLKFLDSTL SILGPLYRFH PYPVSFLYST
FRFYEKRLVE SPAIKQKLAL AVHGACVPAR DDHWLLSAEF VGWVSQATDR GPWVPDLNYY
AALVRRLIDT FSEPRQQWSR KTDLRFVEFN NFQTHALYSI CIELMSLPVG VVDVGNALVT
LVTHWHSLVD KNTVMYWVNA IGLIFSALPI SYMEPFYQTI LTTLCSDHMN SINTDVSNKL
DFEKRSKLME DCYPARILAL CHAVWLHSAP GYLQLLPQAL RSTWIPHVRS EGQFLYVCHL
VAPFLQRFYQ ERTKFTMDIT TDLYQMLYNV DCEVGDWKYE DLICDFFYHV KYMYVGDSVR
QDTDRIIPML RPSLQQKLRY ISFAQGEQSA GTPFSEMINP IKLLGIQMVV WLQRLPIFGE
TAQHFWLAVT KLGDPLCFHF LAPLRWIWIL LDDRPYWWVH TAGVSGHLSH PLKQFQWTCE
TGPGSPSGHA MVSASVWFNL LYNLQSDLVL GDLSGICWLL YVVFLIAVSI SRTYISAHFP
DQVILGIVVG ICIALVTRSL VGHRRRRWSN LIAFMIALLL IALSVHEAHR FFGVDTHRSI
ELAAKYCHRA EWIHQSTTPL ASFFRDVGVL ISVAILLANK SMFTNKNNKI TSKFFSTKFA
QALLGVGLNQ LVALIPIGRL PTVLFYELFV PENYIFWYDC HQALIVLLLT MVLDLDNFRV
EKGGNVQAVR VSQQKRFQSV DLVDQVVETD QEWRRSRYLS DEWNRLKNLC SKEIGEKIKR
KEPVDGNSTL PDSLTDKLQK LTVDQIRALS VSQIKQLRLL IDHEMEKSYK LVENLEAVRF
KALSQIGNLV HNSVPVSENE DDNEIVRTWG ELEVRKKYSQ VDLGIMVDGY DSERGCSVAG
SRGYFLKGPL VFLEQALIQL AMHMLFKKKY TPLYTPFFMR KEVMQEVAQL SDFDDQLYKV
IGKSSEVKEE IAEEEKYLIA TSEQPIAAYH RDEWISKESL PLRYVGFSTC FRQEVGSHGR
DTSGIFRVHQ FEKVEQFCIT SPHDDASWEM LEEMISNAEM FYQTLNIPYR VVSIVSGELN
NAAAKKYDLE AWFPGSGAFR ELVSCSNCTD YQSRRLRIRY EFVHMLNGTM CATTRTICAI
LENFQEENGI AVPEALRQYM PDDYKDFIPF VKPAPKVEQA AKRGNKSATA EKSTQYVGTC
IILAVDRSTV
//
