ID A0A0V0V466_9BILA Unreviewed; 2219 AA.
AC A0A0V0V466;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=T09_13866 {ECO:0000313|EMBL:KRX58326.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX58326.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX58326.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX58326.1};
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 -!- 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:KRX58326.1}.
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DR EMBL; JYDN01000087; KRX58326.1; -; Genomic_DNA.
DR Proteomes; UP000054681; 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; SSF81995; beta-sandwich domain of Sec23/24; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1441..1463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1533..1555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1567..1586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1593..1611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1645..1663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1707..1726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1926..2176
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 784..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2219 AA; 254814 MW; 310715C4055165BA CRC64;
MSVSLSDFEA KVKNLFKEHA KSGIAHFFFR PYLITSSEEC EKEIVISTAN ELMEIFTSLP
QNLQESAFSI VISHRVLSNS ANKIVDFFVR NVIQRQMLSI KCICEKLLTC AELNINSCGW
NDTFAFFMEN ISLLDYKGVR DTLKRLLDIP IPVHLQVDQR KSVEAVEKLI KTICDRKNNL
LPAYFVITEI IKNLPEQRCF SHWRMADCFT EIIESFRPLA QLNSVCGRTF MTPIPGHVGF
YFNAFWKLEA LSLRFPLKGL LPYSQDLLNP QMRLLTHVFM HYTYRDAIAV LLGTAKPEKS
RIPYFEEVIT EIILELMFTA ECDHSQLNPQ AWRIISTQII YLTLQQSICF TRLVKILHTK
LTHYPYRYAR NQLMWCLFNF LSGGMQKYSV EEFAVILDLY RLLYTGRDIF TVSGSDSSCV
LMLAPTCIWI HILKKSPSME VELPPTVNTQ RKFLQEALKN KTQFNTDNYM VAVLCNAYSS
TSEIFQQDLL PILLENLDNT RGHNSTQASG NFASNTTSSM PYPNGAVSEV KLRPLKLEFL
DSVSVHVRMN IANSLIGTFG RFMQGKSAWP SPALVETYCR MLTYPDLEIL GLKQFTSHIV
LTAARHQCCE MMYICCEILN YRLFNIPSTY RVHAIVTLQQ TLAFAKFQTN ASLYWMLERT
LLLQFQWYPH YEIFQAPFAR LLNSFVAVAA DGTKQSIAEN EELMRIIILT LARSTVISSN
SDSCFIEGVY RELLNKLPSY SWPQSTLSVF PQVFCSHYTQ QQQQQQQQQQ QQQQQQQQQQ
PQQPQQQQQQ QQPQPQQSNV VVGSSQQPQQ QQQSRFLLKQ QVDEEYIKHR TFGSELSLID
YFTNTSTSTV YLCLLWRLVY DTGELPAVSM KILEVLGPRK VLVHLKSLAD FLVYETNSAD
VNRCVDVLNR LIFKYAVVPL ERFMLTMLLR DYEGNDAFYA LLIVMLLVQR SEELRSAVAD
CVAMLPSDYW HCQDWNDKYQ AYQIKHAERT WSQVYVELSR ASLTPNDCPL PVYFGTRCLQ
MLPVVDLLLQ KLVESPAACL KFLDSTLSIL GPLYRFHPYP VSFLYSTFRF YEKRLVESPA
IKQKLALAVH GACVPSRDDH WLLSAEFVGW VGQATDRGPW VPDLNYYGAL VRRLIDTFSE
PRQQWSRKTD LRFVEFNNFQ THALYSICIE LMSLPVGVVD VGNALVTLVT HWHSLVDKNT
LMYWVNAIGL IFSALPISYM EPFYQTILTT LCSDNMNSIN TDVSNKLDFE KRSKLMEDCY
PARILALCHA VWLHSTSGYL QLLPQALRST WIPHVRSEGQ FLYVCHLVAP FLQRFYQERT
KFTMDMLYNV DCEVGNWKYE DLICDFFYHV KYMYVGDSVR QDTDRIIPML RPSLQQKLRY
ISFAQGEQSA GTPFSEMINP IKLLGIQMVV WLQRLPIFGE TAQHFWLAVT KLGDPVMTFS
LYFPALFPFF GTAALDMVIV GAFSEISNCI LKWILLDDRP YWWVHTAGVS GQLSHPLKQF
QWTCETGPGS PSGHAMVSAS VWFNLLYNLQ SDLVLGDLCG ICWLLYVVFL IAVSISRTYI
SAHFPDQVIL GIVVGICIAL VTRSLVGHRR RRWSNLIAFM IALLLIALSV HEVHRFFGVD
THRSIELAAK YCHRAEWIHL STTPLASFFR DVGVLISVAI LLANKSMFTN NNKIASKFFS
TKFAQALLGV SLNQLVAFIP IGRLPTALFY AVLLPALIVL LLTMVLDLDN FRVEKGGNVQ
AVRVSQQKRF QSVDLVDQVV ETDQEWRRSR YLSDEWNRLK NLCSKEIGEK IKRKEPVDGN
STLPDSLTDK LQKLTVDQIR ALSVGQIKQL RLLIDHEMEK SYKLVENLEA VRFKALSQIG
NLVHNSVPVS ENEDDNEIVR TWGELEVRKK YSQVDLGIMV DGYDSERGCS VAGSRGYFLK
GPLVFLEQAL IQLAMHMLFK KKYTPLYTPF FMRKEVMQEV AQLSDFDDQL YKVIGKSSEV
KEEIAEEEKY LIATSEQPIA AYHRDEWISK ESLPLRYVGF STCFRQEVGS HGRDTSGIFR
VHQFEKVEQF CITSPHDDAS WEMLEEMISN AEMFYQTLNI PYRVVSIVSG ELNNAAAKKY
DLEAWFPGSG AFRELVSCSN CTDYQSRRLR IRYGQTKKMM AKAEFVHMLN GTMCATTRTI
CAILENFQEE NGIAVPEALR QYMPDDYKDF IPFVKPAPKV EQAAKRGGNK SATAEKSTQ
//
