RPO1N_SACS2
ID RPO1N_SACS2 Reviewed; 880 AA.
AC Q980R2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1N {ECO:0000255|HAMAP-Rule:MF_00863};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00863};
DE AltName: Full=DNA-directed RNA polymerase subunit A' {ECO:0000255|HAMAP-Rule:MF_00863};
GN Name=rpo1N {ECO:0000255|HAMAP-Rule:MF_00863};
GN Synonyms=rpoA1 {ECO:0000255|HAMAP-Rule:MF_00863};
GN OrderedLocusNames=SSO0225;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP INTERACTION WITH ACIDIANUS TWO-TAILED VIRUS PROTEIN RIP.
RX PubMed=27882920; DOI=10.1038/ncomms13595;
RA Sheppard C., Blombach F., Belsom A., Schulz S., Daviter T., Smollett K.,
RA Mahieu E., Erdmann S., Tinnefeld P., Garrett R., Grohmann D.,
RA Rappsilber J., Werner F.;
RT "Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP.";
RL Nat. Commun. 7:13595-13595(2016).
RN [3] {ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ}
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN
RP COMPLEX WITH MAGNESIUM AND ZINC, FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=18235446; DOI=10.1038/nature06530;
RA Hirata A., Klein B.J., Murakami K.S.;
RT "The X-ray crystal structure of RNA polymerase from Archaea.";
RL Nature 451:851-854(2008).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. Forms the clamp head domain.
CC {ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000269|PubMed:18235446}.
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:0000255|HAMAP-Rule:MF_00863};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00863,
CC ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ,
CC ECO:0007744|PDB:3HKZ};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00863,
CC ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ,
CC ECO:0007744|PDB:3HKZ};
CC Note=Binds at least 2 Zn(2+) per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00863, ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ,
CC ECO:0007744|PDB:3HKZ};
CC -!- SUBUNIT: (Microbial infection) Interacts with acidianus two-tailed
CC virus protein RIP; this interaction results in the global inhibition of
CC transcription. {ECO:0000269|PubMed:27882920}.
CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex.
CC {ECO:0000269|PubMed:18235446}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00863}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00863}.
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DR EMBL; AE006641; AAK40566.1; -; Genomic_DNA.
DR PIR; G90163; G90163.
DR RefSeq; WP_009990476.1; NC_002754.1.
DR PDB; 2PMZ; X-ray; 3.40 A; A/Q=1-880.
DR PDB; 3HKZ; X-ray; 3.40 A; A/I=1-880.
DR PDBsum; 2PMZ; -.
DR PDBsum; 3HKZ; -.
DR AlphaFoldDB; Q980R2; -.
DR SMR; Q980R2; -.
DR DIP; DIP-60638N; -.
DR IntAct; Q980R2; 1.
DR STRING; 273057.SSO0225; -.
DR PRIDE; Q980R2; -.
DR EnsemblBacteria; AAK40566; AAK40566; SSO0225.
DR GeneID; 38424056; -.
DR GeneID; 38467847; -.
DR KEGG; sso:SSO0225; -.
DR PATRIC; fig|273057.12.peg.221; -.
DR eggNOG; arCOG04257; Archaea.
DR HOGENOM; CLU_000487_3_1_2; -.
DR InParanoid; Q980R2; -.
DR OMA; AVCPPYN; -.
DR PhylomeDB; Q980R2; -.
DR BRENDA; 2.7.7.6; 6163.
DR EvolutionaryTrace; Q980R2; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd02582; RNAP_archeal_A; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR HAMAP; MF_00863; RNApol_arch_Rpo1N; 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; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR InterPro; IPR012758; RPO1N.
DR PANTHER; PTHR19376; PTHR19376; 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 TIGRFAMs; TIGR02390; RNA_pol_rpoA1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..880
FT /note="DNA-directed RNA polymerase subunit Rpo1N"
FT /id="PRO_0000074008"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3HKZ"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:3HKZ"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00863,
FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3HKZ"
FT TURN 108..112
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:3HKZ"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 234..253
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3HKZ"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 470..479
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 489..492
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 501..509
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 518..523
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 548..552
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:3HKZ"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 585..591
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 600..603
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 611..617
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 623..630
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 632..639
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 640..642
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 657..662
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 665..680
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 692..715
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 716..718
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 724..728
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 729..734
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 737..744
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 760..763
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 786..788
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 794..811
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 813..824
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 841..843
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 845..849
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 850..852
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 857..859
FT /evidence="ECO:0007829|PDB:2PMZ"
FT STRAND 860..864
FT /evidence="ECO:0007829|PDB:2PMZ"
FT HELIX 867..874
FT /evidence="ECO:0007829|PDB:2PMZ"
FT TURN 875..877
FT /evidence="ECO:0007829|PDB:3HKZ"
SQ SEQUENCE 880 AA; 99675 MW; 5C8AE20EFC71DE25 CRC64;
MSEKNIKGIK FGILSPDEIR KMSVTAIITP DVYDEDGTPI EGSVMDPRLG VIEPGQKCPT
CGNTLGNCPG HFGHIELVRP VIHVGLVKHI YEFLKATCRR CGRVKISEDE IEKYSRIYNA
IKKRWPSAAR RLTEYVKKTA MKAQVCPHCN EKQYKIKLEK PYNFYEERKE GVAKLTPSDI
RERLEKIPDS DVEILGYDPT TSRPEWMILT VLPVPPITIR PSIMIESGIR AEDDLTHKLV
DIVRINERLK ESIDAGAPQL IIEDLWDLLQ YHVATYFDNE IPGLPPSKHR SGRPLRTLAQ
RLKGKEGRFR GNLSGKRVDF SSRTVISPDP NISIDEVGVP EIIAKTLTVP ERITPWNIEK
LRQFVINGPD KWPGANYVIR PDGRRIDLRY VKDRKELAST LAPGYIIERH LIDGDIVLFN
RQPSLHRISM MAHRVRVLKG LTFRLNLLVC PPYNADFDGD EMNLHVPQSE EAIAEAKEIM
LVHKNIITPR YGGPIIGAAQ DYISGAYLLT VKTTLLTKEE AQQILGVADV KIDLGEPAIL
APREYYTGKQ VISAFLPKDF NFHGQANVSS GPRLCKNEDC PHDSYVVIKN GILLEGVFDK
KAIGNQQPES ILHWLIKEYS DEYGKWLMDN LFRVFIRFVE LQGFTMRLED VSLGDDVKKE
IYNEIDRAKV EVDNLIQKYK NGELEPIPGR TLEESLENYI LDTLDKLRST AGDIASKYLD
PFNFAYVMAR TGARGSVLNI TQMAAMLGQQ SVRGERIKRG YMTRTLPHFK PYDISPEARG
FIYSSFRTGL KPTELFFHAA GGREGLVDTA VRTSQSGYMQ RRLINALSDL RAEYDGTVRS
LYGEVVQVAY GDDGVFPMYS AHGKTVDVNR IFERVVGWKA
