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Database: UniProt
Entry: Q8GSD5_ORYSJ
LinkDB: Q8GSD5_ORYSJ
Original site: Q8GSD5_ORYSJ 
ID   Q8GSD5_ORYSJ            Unreviewed;       116 AA.
AC   Q8GSD5;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|PIRNR:PIRNR005586};
GN   OrderedLocusNames=Os07g0615800 {ECO:0000313|EMBL:BAT02647.1};
GN   ORFNames=OSNPB_070615800 {ECO:0000313|EMBL:BAT02647.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:BAT02647.1, ECO:0000313|Proteomes:UP000059680};
RN   [1] {ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RA   Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA   Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA   Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA   Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA   Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA   Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA   Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA   Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA   Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA   Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA   Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA   Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA   Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA   Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA   Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA   Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA   Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA   Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA   Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA   Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA   Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA   Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA   Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA   Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA   Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA   Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA   Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA   Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA   Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA   Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA   Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA   Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA   Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA   Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA   Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA   Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA   Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA   Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA   Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA   Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2] {ECO:0000313|EMBL:BAT02647.1, ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(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}.
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DR   EMBL; AP014963; BAT02647.1; -; Genomic_DNA.
DR   RefSeq; XP_015647354.1; XM_015791868.1.
DR   AlphaFoldDB; Q8GSD5; -.
DR   SMR; Q8GSD5; -.
DR   STRING; 39947.Q8GSD5; -.
DR   PaxDb; 39947-Q8GSD5; -.
DR   EnsemblPlants; Os07t0615800-00; Os07t0615800-00; Os07g0615800.
DR   GeneID; 4343902; -.
DR   Gramene; Os07t0615800-00; Os07t0615800-00; Os07g0615800.
DR   KEGG; osa:4343902; -.
DR   eggNOG; KOG2691; Eukaryota.
DR   HOGENOM; CLU_093932_0_0_1; -.
DR   InParanoid; Q8GSD5; -.
DR   OMA; SCEHEEI; -.
DR   OrthoDB; 19808at2759; -.
DR   Proteomes; UP000059680; Chromosome 7.
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; 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:SF16; DNA-DIRECTED RNA POLYMERASE SUBUNIT; 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; PS51133; ZF_TFIIS_2; 1.
PE   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|ProteomicsDB:Q8GSD5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059680};
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          74..115
FT                   /note="TFIIS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51133"
FT   ZN_FING         9..34
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-2"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005586-1"
SQ   SEQUENCE   116 AA;  13094 MW;  33E620DA12A5ACA1 CRC64;
     MAMSALKFCG ECSNMLYPRE DKETHTLLYA CNSCEHQEPA TDTCVYKRVL RKPAGEPKDI
     LKDAATDPTL PRTRSIKCYN CGHPEAAFFQ APTKGEKGLT LYFICCNPSC GHRWRD
//
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