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Database: UniProt
Entry: D8QRR8_SELML
LinkDB: D8QRR8_SELML
Original site: D8QRR8_SELML 
ID   D8QRR8_SELML            Unreviewed;       114 AA.
AC   D8QRR8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|PIRNR:PIRNR005586};
GN   ORFNames=SELMODRAFT_77443 {ECO:0000313|EMBL:EFJ37302.1},
GN   SELMODRAFT_95006 {ECO:0000313|EMBL:EFJ27645.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ37302.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11
CC       RNA polymerase family. {ECO:0000256|PIRNR:PIRNR005586,
CC       ECO:0000256|RuleBase:RU003474}.
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DR   EMBL; GL377581; EFJ27645.1; -; Genomic_DNA.
DR   EMBL; GL377566; EFJ37302.1; -; Genomic_DNA.
DR   RefSeq; XP_002962042.1; XM_002961996.1.
DR   RefSeq; XP_002971047.1; XM_002971001.1.
DR   AlphaFoldDB; D8QRR8; -.
DR   STRING; 88036.D8QRR8; -.
DR   EnsemblPlants; EFJ27645; EFJ27645; SELMODRAFT_95006.
DR   EnsemblPlants; EFJ37302; EFJ37302; SELMODRAFT_77443.
DR   GeneID; 9630483; -.
DR   GeneID; 9642356; -.
DR   Gramene; EFJ27645; EFJ27645; SELMODRAFT_95006.
DR   Gramene; EFJ37302; EFJ37302; SELMODRAFT_77443.
DR   KEGG; smo:SELMODRAFT_77443; -.
DR   KEGG; smo:SELMODRAFT_95006; -.
DR   eggNOG; KOG2691; Eukaryota.
DR   HOGENOM; CLU_093932_0_1_1; -.
DR   InParanoid; D8QRR8; -.
DR   OMA; EVADNSC; -.
DR   OrthoDB; 19808at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
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:0001193; P:maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IBA:GO_Central.
DR   CDD; cd10508; Zn-ribbon_RPB9; 1.
DR   Gene3D; 2.20.25.10; -; 2.
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; IPR034012; Zn_ribbon_RPB9_C.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   PANTHER; PTHR11239; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR11239:SF1; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9; 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; 2.
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};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005586};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514};
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          72..113
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   ZN_FING         7..32
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-2"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         10
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         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         79
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"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
SQ   SEQUENCE   114 AA;  13301 MW;  3A2243EB5A0EEB5A CRC64;
     MSTMKFCREC NNILYPKEDR DQKLLLYACR NCDHQEAADN NCVYRNEVHH TADERTQVLQ
     DVASDPTLPR TKDVRCSRCK HGEAVFFQAT ARGEEGMTLF FVCCNPNCGY RWRD
//
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