ID A0A2K1J2Q4_PHYPA Unreviewed; 1409 AA.
AC A0A2K1J2Q4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=PHYPA_021651 {ECO:0000313|EMBL:PNR35801.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR35801.1};
RN [1] {ECO:0000313|EMBL:PNR35801.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c17_4860V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR35801.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c17_4860V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c17_4860V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|RuleBase:RU004279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000256|RuleBase:RU004279};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|RuleBase:RU004279}.
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DR EMBL; ABEU02000017; PNR35801.1; -; Genomic_DNA.
DR STRING; 3218.A0A2K1J2Q4; -.
DR PaxDb; 3218-PP1S26_192V6-1; -.
DR EnsemblPlants; Pp3c17_4860V3.1; Pp3c17_4860V3.1; Pp3c17_4860.
DR EnsemblPlants; Pp3c17_4860V3.2; Pp3c17_4860V3.2; Pp3c17_4860.
DR EnsemblPlants; Pp3c17_4860V3.3; Pp3c17_4860V3.3; Pp3c17_4860.
DR EnsemblPlants; Pp3c17_4860V3.4; Pp3c17_4860V3.4; Pp3c17_4860.
DR EnsemblPlants; Pp3c17_4860V3.5; Pp3c17_4860V3.5; Pp3c17_4860.
DR EnsemblPlants; Pp3c17_4860V3.6; Pp3c17_4860V3.6; Pp3c17_4860.
DR Gramene; Pp3c17_4860V3.1; Pp3c17_4860V3.1; Pp3c17_4860.
DR Gramene; Pp3c17_4860V3.2; Pp3c17_4860V3.2; Pp3c17_4860.
DR Gramene; Pp3c17_4860V3.3; Pp3c17_4860V3.3; Pp3c17_4860.
DR Gramene; Pp3c17_4860V3.4; Pp3c17_4860V3.4; Pp3c17_4860.
DR Gramene; Pp3c17_4860V3.5; Pp3c17_4860V3.5; Pp3c17_4860.
DR Gramene; Pp3c17_4860V3.6; Pp3c17_4860V3.6; Pp3c17_4860.
DR InParanoid; A0A2K1J2Q4; -.
DR OrthoDB; 7998at2759; -.
DR Proteomes; UP000006727; Chromosome 17.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 6.10.250.2940; -; 1.
DR Gene3D; 6.20.50.80; -; 1.
DR Gene3D; 3.30.1490.180; RNA polymerase ii; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 272..577
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 346..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 156028 MW; 1F5F856005FFA1B0 CRC64;
MGRGGGGGGA AGIGGTAMGA PIAPAHASIN FSKRPFIEDV GPRKIESIRF GTMSKQDIVK
ASELHVYESM LYTMPERNPA PYSVVDTRLG TTNKKGECST CFGKLADCPG HFGHTKLEMP
VFHIGYLKNI LQILQCICKS CARILMPEEE CKLILRKMRN PRIEVLQRRA VLKKVIDRCK
RVRVCTRCGD YNGVVKKMAQ PPVKLIHDKY GKALDLKEEM IVSLEDAMKC KPELKNCINR
VYDNLDPMRV LQLFESMIEQ DCEVLDLAER PEKLIVTHLI VPPVAIRPSV EMESAAGSNE
DDITVRLLGI LNCNNSLRTC VEQGLAAEKT METWELLQSQ VSQLINSETP VPRSEQPTSG
KQPRGFVQRL KGKQGRFRGN LSGKRVDFTG RTVISPDPNL KITEVAVPLL MAQLLTYPEK
VSRYNIDKLR GRIINGMTKH PGANFIIFPD GNKLYLKFGD RRRYAAELKY GDIVERHLED
GDIVLFNRQP SLHRMSIMSH RARIMPWRTL RFNESVCNPY NADFDGDEMN LHVPQTEEAR
TEALMLMGVA NNLCTPKNGE ILVASTQDFL TSSYLFTRKD TFYDRATFTQ ACVYMGDAAE
NIDLPTPSII KPMELWTGKQ LFSVLVRPNA KTRVFVNLVS YEKNYDKKAN KGSMCPTDGY
VYFRNSELIC GQLGKATLGN GNKDGLFTVL LRDYGNEAAA VCMNRLAKLS ARWIGNHGFS
IGIDDVAPSD RLNREKEKQI TKGYNACDQH IQLYKKGKLE LQPGCNAAQT LESAVTGELN
KIREAAGNVC KDELHWRNSP LIMSECGSKG SFINISQMVA CVGQQSVGGK RAPNGFIDRT
LPHFPRHDRT PQGKGFVANS FYSGLSATEF FFHTMGGREG LVDTAVKTAE TGYMSRRLMK
ALEDLSAQYD GTVRNSSGGI VQLLYGDDGM DPVYMEGKDG APFNLDRMLM KTKATCPSYG
QLGLPPTEIE KLFNERLTKP DMTSETVGAF KTSLKKFMDS CIKDNISTRT KLGLPLDCNG
GPDQTLLEST ATYISGLTSR QLEVFLDTCI KRYHMKRVEP GAAVGAVGAQ SIGEPGTQMT
LKTFHFAGVA SMNITLGVPR IKEIINASKN ISTPIITAVL VSGNDEKAAR IVKGRIEKTT
LGEVAKSIKT VLRASQAIIS VKLDMKRIDA LQLDINSDTV ALAIVQTPKI KLKHVNIRIV
DRDKLIVIPP DQDKGKLYFY LHSLCNMLPK VIVKGIPSVE RAVINKEKGV YNLLVEGTNL
KAVMGISGVN GKLTKSNHVI EAEQTLGIEA ARNVIIDEIQ YTMGSHGMTI DARHMMLLAD
VMTYKGEVLG ITRFGIAKMK DSVLMLASFE KTTDHLFDAA IHGRVDKIEG VSECIIMGIP
MPIGTGLFKI RQKVEKLPKL SYGPTPLLS
//
