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Database: UniProt
Entry: A0A0V1NQ34_9BILA
LinkDB: A0A0V1NQ34_9BILA
Original site: A0A0V1NQ34_9BILA 
ID   A0A0V1NQ34_9BILA        Unreviewed;       108 AA.
AC   A0A0V1NQ34;
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=DNA-directed RNA polymerase subunit {ECO:0000256|PIRNR:PIRNR005586};
GN   Name=Polr3k {ECO:0000313|EMBL:KRZ86130.1};
GN   ORFNames=T08_4137 {ECO:0000313|EMBL:KRZ86130.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ86130.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ86130.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ86130.1};
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   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000256|PIRNR:PIRNR005586}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005586}.
CC   -!- SIMILARITY: Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11
CC       RNA polymerase family. {ECO:0000256|PIRNR:PIRNR005586,
CC       ECO:0000256|RuleBase:RU003474}.
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:KRZ86130.1}.
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DR   EMBL; JYDM01000125; KRZ86130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1NQ34; -.
DR   STRING; 92180.A0A0V1NQ34; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; -; 2.
DR   InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR   InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR   InterPro; IPR034014; Zn_ribbon_RPC11_C.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   PANTHER; PTHR11239; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR11239:SF12; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC10; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR   SMART; SM00661; RPOL9; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 2.
DR   PROSITE; PS00466; ZF_TFIIS_1; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|PIRNR:PIRNR005586};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR005586-1}; Nucleus {ECO:0000256|PIRNR:PIRNR005586};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Transcription {ECO:0000256|PIRNR:PIRNR005586,
KW   ECO:0000256|RuleBase:RU003474};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR005586-1};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PIRSR:PIRSR005586-
KW   2}.
FT   DOMAIN          65..107
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   ZN_FING         5..28
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-2"
FT   BINDING         5
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
SQ   SEQUENCE   108 AA;  12722 MW;  776A8C18CED971D7 CRC64;
     MFFFCPFCNN FLKLFSGKKG LYYACEACSF EEQVDNQYVF RTHPKMKELS HILGGPKAWE
     NAQITEEKCP KCDGGQAYFM QIQIRSADEP MTTFYRCANN YCAHRWRD
//
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