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Database: UniProt
Entry: A0A182XYR7_ANOST
LinkDB: A0A182XYR7_ANOST
Original site: A0A182XYR7_ANOST 
ID   A0A182XYR7_ANOST        Unreviewed;       356 AA.
AC   A0A182XYR7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA-directed RNA polymerase III subunit RPC10 {ECO:0000256|ARBA:ARBA00020093};
DE            EC=2.7.7.87 {ECO:0000256|ARBA:ARBA00012584};
DE   AltName: Full=RNA polymerase III subunit C11 {ECO:0000256|ARBA:ARBA00029985};
DE   AltName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000256|ARBA:ARBA00015492};
OS   Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI01353-PA, ECO:0000313|Proteomes:UP000076408};
RN   [1] {ECO:0000313|Proteomes:UP000076408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX   PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA   Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA   Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA   Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA   George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA   Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA   Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA   Sharakhov I.V., Tu Z.;
RT   "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT   stephensi.";
RL   Genome Biol. 15:459-459(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASTEI01353-PA}
RP   IDENTIFICATION.
RC   STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI01353-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC         threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC         Evidence={ECO:0000256|ARBA:ARBA00001803};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the SUA5 family.
CC       {ECO:0000256|ARBA:ARBA00007663}.
CC   -!- SIMILARITY: Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11
CC       RNA polymerase family. {ECO:0000256|RuleBase:RU003474}.
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DR   AlphaFoldDB; A0A182XYR7; -.
DR   STRING; 30069.A0A182XYR7; -.
DR   EnsemblMetazoa; ASTEI01353-RA; ASTEI01353-PA; ASTEI01353.
DR   VEuPathDB; VectorBase:ASTE005888; -.
DR   VEuPathDB; VectorBase:ASTEI01353; -.
DR   VEuPathDB; VectorBase:ASTEI20_036906; -.
DR   OMA; CLSSECA; -.
DR   Proteomes; UP000076408; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd10509; Zn-ribbon_RPC11; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 3.90.870.10; DHBP synthase; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR   InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR   InterPro; IPR006070; Sua5-like_dom.
DR   InterPro; IPR034014; Zn_ribbon_RPC11_C.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   NCBIfam; TIGR00057; L-threonylcarbamoyladenylate synthase; 1.
DR   PANTHER; PTHR17490; SUA5; 1.
DR   PANTHER; PTHR17490:SF10; THREONYLCARBAMOYL-AMP SYNTHASE; 1.
DR   Pfam; PF02150; RNA_POL_M_15KD; 1.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   SMART; SM00661; RPOL9; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR   PROSITE; PS51163; YRDC; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA-directed RNA polymerase {ECO:0000256|RuleBase:RU003474};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003474};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076408};
KW   Transcription {ECO:0000256|RuleBase:RU003474};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ   SEQUENCE   356 AA;  39326 MW;  0DB132AF786AB1E4 CRC64;
     MLMFCPTCGN LLLVEEGTDA LRFSCNTCPY ICKIRQRISS RIYPKLKEVD HVMGGSAAWE
     NVDSTDAVCP SCSHNRAYFM QMQTRSADEP MTTFYKCLSS ECARASPLYM MKRALKYDVN
     ETSSNKQLKL SRLKLDVAKQ SKVIDTTRAD AKVIAVEKLR RGEVIAIPTD TVYGLTCSAN
     NPKAIGRLYN IKGRHELKPV AICVATVEDL RQWGEADHLS AELLNELLPG AVTVVVKRSA
     KLNNPKLNPG VSNIGIRITE NNFIQDVCAA FNEPIALTSA NKSSSQSTLE VGEFKELWPK
     LGAVFDGGQL GLSEEQRAAS TVIDLSVPGC YRIIRRGVAV EKIIKTVERH NIRLAP
//
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