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Database: UniProt
Entry: W6JHE4_9MYRI
LinkDB: W6JHE4_9MYRI
Original site: W6JHE4_9MYRI 
ID   W6JHE4_9MYRI            Unreviewed;      1648 AA.
AC   W6JHE4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
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:BAO48663.1};
OS   Pauropodidae sp. My085.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Pauropoda;
OC   Tetramerocerata; Pauropodidae.
OX   NCBI_TaxID=1366095 {ECO:0000313|EMBL:BAO48663.1};
RN   [1] {ECO:0000313|EMBL:BAO48663.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=My085 {ECO:0000313|EMBL:BAO48663.1};
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; AB831746; BAO48663.1; -; 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   Pfam; PF05001; RNA_pol_Rpb1_R; 16.
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; 12.
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          164..467
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1466..1648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1473..1490
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1498..1648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAO48663.1"
FT   NON_TER         1648
FT                   /evidence="ECO:0000313|EMBL:BAO48663.1"
SQ   SEQUENCE   1648 AA;  182549 MW;  B915B8E56460BDF4 CRC64;
     ECPGHFGHID LAKPVLHIGF LTKTIKVLRC VCFFCSKMLI NPNNPKIKDV VLKSKGMPRR
     RLAHVYDLCK TRKICEGGDD DTKENEDGQE QDVFKKLGHG GCGRFQPTIR RSGLDLTAEW
     KHVNDDTQEK KIPVTGERVY EIFRHISDEE CTVLGMDPKY ARPESMIVTV VPVPPLAVRP
     AIVMNGSNHC QDDITHKLAD IIKCNNELIR NEQSGAAAHI IAENMKMLQF HVATLTDNDS
     PGLPKAMQKS GRPLKSIKAR LKGKEGRIRG NLMGKRVDFS ARTVITPDPN LLIHQVGVPR
     SIAQNMTFPE IVTPFNIDKM RDLVRRGNSQ YPGAKYIIRD NGERIDLRFH PKPSDLHLQM
     GYKVERHIRD GDVVIFNRQP TLHKMSMMGH KIRVLPWSTF RLNLSVTTPY NADFDGDEMN
     LHVPQSMETR AEIEELALVP RQIITPQSNQ PVMGIVQDTL CAVRKMTKRD VFLEKDQMMN
     LLMYLPTWDG KMPQPAILKP KPLWTGKQLF SLIIPGNVNV IRTHSTHPDE EDDGPYKWIS
     PGDTKVLVEH GTLICGIICK KTIGTSGGSL LHIVMLEMGW ETAGLFYSHN WLLLDGHSIG
     INDTIADQET YIEIQDTIKK AKIDVVEVIE RAHNDELEPT PGNTLRQTFE NQVNRILNDA
     RDKTGSSAQK SLSEFNNFKS MVVSGSKGSK INISQVIACV GQQNVEGKRI PFGFRKRTLP
     HFIKDDYGPE SRGFVENSYL AGLTPSEFFF HAMGGREGLI DTAVKTAETG YIQRRLIKAM
     ESVMVAYDGT IRNSAGQMVQ FRYGEDGLDA CHVEIQSLAT LKPSDRAFEQ KFKFDATNER
     HLRRVFNESI VKELLGSASA VGQLESEWDQ LRKDREILRQ VFPKGENKIV LPCNLQRMIW
     NAQKIFHINT RAPTDLSPLK VVDSVRDLSK RIIVVGGEDM LSKQANENAT LLFNCHLRST
     LCTKRVAEEF KLSSEAFEWI LGEIDARFQQ SMVQPGEMVG ALAAQSLGEP ATQMTLNTFH
     YAGVSAKNVT LGVPRLKEII NISKKPKTPS LTVFLVGAPA RDAEKAKDVL CRLEHTTLRK
     VTANTAIYYD PDPQNTVIPE DQEFVSVYYE MPDFDPSRIS PWLLRIELDR KRMTDKKLTM
     EQISEKINAG FGDDLNCIFN DDNAEKLVLR IRIMNSDDGK NDDGDDQQIV DKMTDDVFLR
     CIESNMLSDM TLQGIEAIAK VYMHLPSTDD KKRIVRMETG EFKSIAEWLL ETDGTSLMRV
     LSERDVDPIR TYSNDICEIF SVMGIEAVRK SVEKEMNHVI SFDGSYVNYR HLALLCEIMT
     AKGHLMAITR HGINRQDTGA LMRCSFEETV DVLMEAASHA ECDYMRGVSE NIMLGQLAKM
     GTGSFDLLLN NEQCKFGMEI PSNLGGGVGL FFGSTSPGSG MSPQMTPWMQ GGTPAYGSVW
     SPGVGSGMTP GGAGFSPAAS DASGFSPGYS PAWSPQPGSP VSPGPVSPYI PSPAGAGLSP
     SYSPSSPYGL ASPSGQSPSY SASGSNYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP
     SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
     TSPSYSPTSP SYSPTSPSYS PTSPSYSP
//
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