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Database: UniProt
Entry: A0A016W0U2_9BILA
LinkDB: A0A016W0U2_9BILA
Original site: A0A016W0U2_9BILA 
ID   A0A016W0U2_9BILA        Unreviewed;       119 AA.
AC   A0A016W0U2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|PIRNR:PIRNR005586};
GN   Name=Acey_s0002.g662 {ECO:0000313|EMBL:EYC33201.1};
GN   ORFNames=Y032_0002g662 {ECO:0000313|EMBL:EYC33201.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC33201.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Component of RNA polymerase I which synthesizes ribosomal RNA
CC       precursors. {ECO:0000256|ARBA:ARBA00002472}.
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   -!- 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:EYC33201.1}.
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DR   EMBL; JARK01001338; EYC33201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016W0U2; -.
DR   STRING; 53326.A0A016W0U2; -.
DR   Proteomes; UP000024635; 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; cd10507; Zn-ribbon_RPA12; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR   InterPro; IPR034004; Zn_ribbon_RPA12_C.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   PANTHER; PTHR11239; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR11239:SF14; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA12; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 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:UP000024635};
KW   Transcription {ECO:0000256|PIRNR:PIRNR005586};
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          76..116
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   ZN_FING         13..35
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-2"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
SQ   SEQUENCE   119 AA;  13282 MW;  8185E2FD6656B72D CRC64;
     MSLNFISADP EFCGFCGAIL QMPQTAPSSV ACRVCGTQWH VKEKRDHLVC RIEKVYERTV
     ADTEGMEQDD GADAIVDHVC SKCGHSKASY STMQTRSADE GQTVFYTCLK CKRKDIEYS
//
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