ID W6JHD7_9MYRI Unreviewed; 1646 AA.
AC W6JHD7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
DE Flags: Fragment;
GN Name=RPB1 {ECO:0000313|EMBL:BAO48672.1};
OS Riukiaria sp. R001.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Diplopoda;
OC Helminthomorpha; Polydesmida; Xystodesmidae; Xystodesminae; Xystodesmini;
OC Riukiaria.
OX NCBI_TaxID=1366098 {ECO:0000313|EMBL:BAO48672.1};
RN [1] {ECO:0000313|EMBL:BAO48672.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R001 {ECO:0000313|EMBL:BAO48672.1};
RX PubMed=24535281; DOI=10.1038/srep04127;
RA Miyazawa H., Ueda C., Yahata K., Su Z.-H.;
RT "Molecular phylogeny of Myriapoda provides insights into evolutionary
RT patterns of the mode in post-embryonic development.";
RL Sci. Rep. 4:4127-4127(2014).
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|ARBA:ARBA00024550,
CC 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|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR EMBL; AB831755; BAO48672.1; -; mRNA.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_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; 3.30.1360.140; -; 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; 2.
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; IPR000684; RNA_pol_II_repeat_euk.
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; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF37; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1; 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 Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 3.
PE 2: Evidence at transcript level;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU004279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 238..541
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 153..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1646
FT /evidence="ECO:0000313|EMBL:BAO48672.1"
SQ SEQUENCE 1646 AA; 183475 MW; 620EC1B6FAA12F46 CRC64;
MGSDSRAPLR EVKKVQFGIL SPDEIKRFSV TEGGIRFPEI YEGGRPKQGG LMDPRQGVID
RVSRCQTCAG NMTECPGHFG HIELAKPVFH VGFLNKTIKI LRCVCFYCSK LLVNSNNPKI
KDILAKSKGQ PRKRIAHVYD LCKGKNICEG GDEMDMTSQQ EGGDQENPKH ATHGGCGRYQ
PKIRRAGLDL TAEWKHVNED SQERKIVLTA ERVWEIFKHV SDEECMILGM DPKHSRPDWM
IVTVLPVPPL QVRPAVVMYG SARNQDDLTH KLADIVKANN ELLHNEQIGA AAHVIAENIK
MLQFHVATLV DNDLPGLPKA MQKSGRPLKS LKARLKGKEG RIRGNLMGKR VDFSARTVIT
PDPNLRIDQV GVPRSIAQNL TFPEIVTPFN IDKMQELVRR GNSQYPGAKY IVRDNGERID
LRFHPKPSDL HLQCGYKVER HVRDGDVVIF NRQPTLHKMS MMGHHIRVFP WSTFRMNLSV
TTPYNADFDG DEMNLHVPQS METRAEIEEL AIVPRQIITP QSNRPVMGIV QDTLTAVRKM
TKRDVFLEKE HMMNILMFLP IWDGKMPQPA ILKPKPLWTG KQIFSLIIPG NVNVIRTHST
HPDDEDDGPY KWISPGDTKV LVEHGELICG ILCKKTLGTS AGSLLHIVML ELGWEVAGHF
YWHIQTVVNN WLLLEGHTIG IGDTIADRQT YDDIQETIRK AKQDVIEVIE KAHNDELEPT
PGNTLRQTFE NQVNRILNDA RDKTGSSAQK SLSEHNNFKA MVVSGSKGSK INISQVIACV
GQQNVEGKRI PFGFQKRTLP HFIKDDYGPE SRGFVENSYL AGLTPSEFYF HAMGGREGLI
DTAVKTAETG YIQRRLIKAM ESVMVAYDGT IRNSVGQLIQ LRYGEDGLDG CAVEFQTLPT
LKPSTKAFEK KFRFDVSNER QLRRIFSEDI VKELIGSAQV VAELEKEWDT LKRDREVLRD
VFPKGDNKVV LPGNLQRMIW NAQKIFHINL RSPTDLSPLK VLEGVKELTK KIIVVPGDDN
LSRQANENAT LLFNCLLRST LCTKRVAEEF RLSWEAFEWL LGEIETRFNQ AQAQPGEMVG
ALAAQSLGEP ATQMTLNTFH YAGVSAKNVT LGVPRLKEII NISKKPKTPS LTVFLTGAAA
RDAEKAKDVL CRLEHTTLRK VTANTAIYYD PDPQNTVIAE DQEFVNVYYE MPDFDPTRIS
PWLLRVELDR KRMTDKKLTM EQISEKINAG FGDDLNCIFN DDNAEKLVLR IRIMNSDESK
FQDEEEQVDK MEDDVFLRCI EANMLSDMTL QGIESIAKVY MHLPSTDDKK RIVIVDTGEY
KPIAEWLLET DGTSLMKVLS ERDVDPMRTH SNDICEIFSV LGIEAVRKSV EKEMNHVISF
DGSYVNYRHL ALLCDVMTAK GHLMAITRHG INRQDTGALM RCSFEETVDI LLDAAAHAEF
DPMRGVSENI MLGQLARLGT GCFDLMLDAE KCKYGMEIPV NLPGVMGMGG MFFGGATSLS
TGGLSPQMTP WNQGATPGYA SAWSPGIGSG MTPGAAGFSP SASSDASGYS PGYSPAWSPQ
PGSPSSPGPS SPYIPSPGAL SPSYSPSSPT YAPTSPSLTP QSPSYSPTSP SYSPTSPSYS
PTSPNYSPRS PTYSPTSXTN SPTSPS
//
