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Database: UniProt
Entry: A0A182UHI7_9DIPT
LinkDB: A0A182UHI7_9DIPT
Original site: A0A182UHI7_9DIPT 
ID   A0A182UHI7_9DIPT        Unreviewed;       485 AA.
AC   A0A182UHI7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
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 melas.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC020515-PA, ECO:0000313|Proteomes:UP000075902};
RN   [1] {ECO:0000313|Proteomes:UP000075902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEC020515-PA}
RP   IDENTIFICATION.
RC   STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC020515-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; A0A182UHI7; -.
DR   STRING; 34690.A0A182UHI7; -.
DR   EnsemblMetazoa; AMEC020515-RA; AMEC020515-PA; AMEC020515.
DR   VEuPathDB; VectorBase:AMEC020515; -.
DR   Proteomes; UP000075902; 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:0004252; F:serine-type endopeptidase activity; 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   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   CDD; cd10509; Zn-ribbon_RPC11; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 3.90.870.10; DHBP synthase; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 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; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR019533; Peptidase_S26.
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; PF10502; Peptidase_S26; 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; SSF51306; LexA/Signal peptidase; 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}; Signal {ECO:0000256|SAM:SignalP};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00472}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..485
FT                   /note="DNA-directed RNA polymerase III subunit RPC10"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008138176"
FT   DOMAIN          181..239
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   DOMAIN          278..468
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   REGION          233..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  54113 MW;  DBEE5C6303319C7D CRC64;
     MRFPTFLKSL LLGVPVGVTL LDCVGYVARV EGVSMQPALN PDATVTDYVF LSRWAVRNMD
     VQRGDIISLI SPKDPTQKII KRVVALQGDV ISTLGYKLPY VTVPEGHCWV EGDHTVMLMF
     CPTCGNLLLV EESTDSLRFS CNTCPYICKI RRTISSRIYP TLKEVDHVMG GSAAWENVDS
     TDAVCPSCSH NRAYFMQMQT RSADEPMTTF YKCCNQTNII SSVLTRVVVG SMKQTHKHRH
     STRTRQNYSD ANRRPHSLRY APKDVSEQES KVISTNRKDA KAIAVAKLQA GEVIAIPTDT
     VYGLTCSANN PEAIHRLYNI KGRHELKPVA ICVASIEDVR QWGETDHLND ELLNELFPGA
     VTLVVRRSSK LNNPALNPGV ANIGIRITEN KFIQHVCEAF QQPIALTSAN KSSSKSTLNV
     EEFKQLWCEL GAVFDGGQLG LSEEQRAAST VIDLSEPERY KIIRWGVSVE KIIKTVERHN
     FRAVE
//
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