ID A0A0V1L0G0_9BILA Unreviewed; 2071 AA.
AC A0A0V1L0G0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 23 {ECO:0000256|ARBA:ARBA00019696};
DE EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE AltName: Full=Mediator complex subunit 23 {ECO:0000256|ARBA:ARBA00031961};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
GN Name=Sars {ECO:0000313|EMBL:KRZ53019.1};
GN ORFNames=T02_3332 {ECO:0000313|EMBL:KRZ53019.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ53019.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ53019.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ53019.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 23 family.
CC {ECO:0000256|ARBA:ARBA00010222}.
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:KRZ53019.1}.
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DR EMBL; JYDW01000176; KRZ53019.1; -; Genomic_DNA.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; PTHR12691; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 23; 1.
DR PANTHER; PTHR12691:SF10; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 23; 1.
DR Pfam; PF11573; Med23; 2.
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:KRZ53019.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1386..1408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1420..1439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1446..1464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1498..1516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1536..1554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1560..1579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1779..2029
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 2071 AA; 237903 MW; 31256976999BF658 CRC64;
MLHILIKNTL LNHRISFWGF CAFVAMSVSL SDFEAKVKNL FKEHAKSGIA HFFFRPYLIT
SSEEYEKEIV ISTANELMEI FTSLPQNLQE SAFSIVISHR VLSNSANRIV DFFVRNVTQR
QMLSIKCICE KLLTCAELNI NSCGWNDTFA FFMENISLLD YKGVRDTLKR LLDIPIPVHL
QVDQRKSVEA VEKLIKTICD RKNNLLPAYF VITEIIKNLP EQRCFSHWRM ADCFTEIIES
FRPLAQLNSV CGRTFMTPIP GHVGFYFNAF WKLEALSLRF PLKGLLPYSQ DLLNPQMRLL
THVFMHYTYR DAIAVLLGTA KPEKSRIPYF EEVITEIILE LMFTAECDHS QLNPQAWRII
STQIIYLTLQ QSICFTRLVK ILHTKLTHYP YRYARNQLMW CLFNFLSGGM QKYSVEEFAV
ILDLYRLLYT GRDIFTVSGS DSSCVLMLAP TCIWIHILKK SPSMEVELPP TVNTQRKFLQ
EALKNKTQFN TDNYMVAVLC NAYSSTSEIF QQDLLPILLE NLDNTRGHNS TQASGNFASN
ATSSMPYPNG AVSEVKLRPL KLEFLDSVSV HVRMNIANSL IGTFGRFMQG KSAWPSPALV
ETYCRMLTYP DLEILGLKQF TSHIVLTAAR HQCCEMMYIC CEILNYRLFN IPSTYRVHAI
VTLQQTLAFA KFQTNASLYW MLERTLLLQF QWYPHYEIFQ APFARLLNSF VAVAADGTKQ
SIAENEELMR IIILTLARST VISSKVLGPR KVLVHLKSLA DFLVYETNSA DVNRCVDVLN
RLIFKYAVVP LERFMLTMLL RDYEGNDAFY ALLIVMLLVQ RSEELRSAVA DCVAMLPSDY
WHCQDWNDKY QAYQIKHAER TWSQVYVELS RASLTPNDCP LPVYFGTRCL QMLPVVDLLL
QKLVESPAAC LKFLDSTLSI LGPLYRFHPY PVSFLYSTFR FYEKRLVESP AIKQKLALAV
HGACVPSRDD HWLLSAEFVG WVGQATDRGP WVPDLNYYGA LVRRLIDTFS EPRQQWSRKT
DLRFVEFNNF QTHALYSICI ELMSLPVGVV DVGNALVTLV THWHSLVDKN TVMYWVNAIG
LIFSALPISY MEPFYQTILT TLCSDHMNSI NTDVSNKLDF EKRSKLMEDC YPARILALCH
AVWLHSTSGY LQLLPQALRS TWIPHVRSEG QFLYVCHLVA PFLQRFYQER TKFTMDITTD
LYQMLYNVDC EVGNWKYEDL ICDFFYHVKY MYVGDSVRQD TDRIIPMLRP SLQQKLRYIS
FAQGEQSAGT PFSEMINPIK LLGIQMVVWL QRLPIFGETA QHFWLAVTKL GDPLCFHFLA
PLRWIWILLD DRPYWWVHTA GVSGQLSHPL KQFQWTCETG PGSPSGHAMV SASVWFNLLY
NLQSDLVLGD LCGICWLLYV VFLIAVSVSR TYISAHFPDQ VILGIVVGIC IALVTRSLVG
HRRRRWSNLI AFMIALLLIA LSVHEVHRFF GVDTHRSIEL AAKYCHRAEW IHQSTTPLAS
FFRDVGVLIS VAILLANKSM FTNNNKIASK FFSTKFAQAL LGVGLNQLVA FIPIGRLPTA
LFYAVLLPAL IVLLLTMVLD LDNFRVEKGG NVQAVRVSQQ KRFQSVDLVD QVVETDQEWR
RSRYLSDEWN RLKNLCSKEI GEKIKRKEPV DGNSTLPDSL TDKLQKVTVD QIRALSVSQI
KQLRLLIDHE MEKSYKLVEN LEAVRFKALS QIGNLVHNSV PVSENEDDNE IVRTWGELEV
RKKYSQVDLG IMVDGYDSER GCSVAGSRGY FLKGPLVFLE QALIQLAMHM LFKKKYTPLY
TPFFMRKEVM QEVAQLSDFD DQLYKVIGKS SEVKEEIAEE EKYLIATSEQ PIAAYHRDEW
ISKESLPLRY VGFSTCFRQE VGSHGRDTSG IFRVHQFEKV EQFCITSPHD DASWEMLEEM
ISNAEMFYQT LNIPYRVVSI VSGELNNAAA KKYDLEAWFP GSGAFRELVS CSNCTDYQSR
RLRIRYGQTK KMMAKAEFVH MLNGTMCATT RTICAILENF QEENGIAVPE ALRQYMPDDY
KDFIPFVKPA PKVEQAAKRG NKSATAEKST Q
//
