ID J8Q6L4_SACAR Unreviewed; 110 AA.
AC J8Q6L4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|PIRNR:PIRNR005586};
GN ORFNames=SU7_0603 {ECO:0000313|EMBL:EJS44261.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS44261.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS44261.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
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:EJS44261.1}.
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DR EMBL; ALIE01000041; EJS44261.1; -; Genomic_DNA.
DR AlphaFoldDB; J8Q6L4; -.
DR SMR; J8Q6L4; -.
DR HOGENOM; CLU_093932_3_0_1; -.
DR OrthoDB; 19847at2759; -.
DR Proteomes; UP000006968; Chromosome IV.
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; -; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
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; PF02150; RNA_POL_M_15KD; 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; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 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:UP000006968};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW 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 65..108
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
FT ZN_FING 5..29
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 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT BINDING 29
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 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
SQ SEQUENCE 110 AA; 12513 MW; E4AA802EC9F92230 CRC64;
MLSFCPSCNN MLLITSGDSG VYTLACRSCP YEFPIEGIEI YDRKKLPRKE VDDVLGGGWD
NVDQTKTQCP NYDTCGGESA YFFQLQIRSA DEPMTTFYKC VNCGHRWKEN
//
