ID A0A0P7AIT5_9HYPO Unreviewed; 1754 AA.
AC A0A0P7AIT5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=AK830_g9188 {ECO:0000313|EMBL:KPM37376.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM37376.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM37376.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM37376.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM37376.1}.
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DR EMBL; LKCW01000168; KPM37376.1; -; Genomic_DNA.
DR STRING; 78410.A0A0P7AIT5; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
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: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; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000050424};
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 242..548
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 151..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 689..716
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1556..1571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1754 AA; 192969 MW; D4706A8A96268A7A CRC64;
MANLYFTHSS APLKTVEEIQ FGLMSPEEIK NMSVCHILYP ETMEENKIKP RDGGLNDPLL
GSIDRQFRCK TCNQAMGECP GHFGHIELAK PVYHPGFIKK VKKILEIVCH NCSKVLADKS
DPEFAAAIGT RDPKVRFHRV WEVCKKKRRC ENEERNDKNK EEFAPGVKLP PVENHGGCGN
VQPNVRQAAL QLKAAFEVQQ EDNTKRRETT PITPEMAHAI LRRISEADLV NMGLNSDYAR
PEWMVLTVLP VPPPPVRPSI SMDGTSTGMR NEDDLTYKLG DIIRANGNVK QAIREGSPQH
IARDFEELLQ YHVATYMDND IAGQPRALQK SGRPVKAIRA RLKGKEGRLR GNLMGKRVDF
SARTVITGDA NLSLHEVGVP RSIARTLTYP ETVTPYNISK LHQLVENGPN EHPGAKYVIR
SDGTRIDLRH HRRAAQISLE YGWKVERHLI DGDYIIFNRQ PSLHKESMMG HRVRVMPYST
FRLNLSVTSP YNADFDGDEM NLHVPQSEET RAEVKELCLV PLNIVSPQKN GPLMGIVQDS
LAGVYKLCRR DTFLTKDEVM NQMLWLPNWD GIIPQPAILK PQPRWTGKQI ISMVIPKEVS
LHTAPDSKED NPINDEGLLI QSGHLMYGLL TKKYVGAAAG GIIHVSYNEL GPQGAMAFLN
GVQQVVTHWL LQTGHSIGIG DTIPDKATIE KVQVHIDEEK AEVARLTAQA TANELEALPG
MNVRATFENK VSMALNQARD KAGTTTQKSL KDSNNAVTMA SSGSKGSSIN ISQMTALVGQ
QIVEGKRIPF GFKYRTLPHF TKDDYSPEAR GFVENSYLRG LTPSEFFFHA MAGREGLIDT
AVKTAETGYI QRRLVKALED LSARYDGTVR NSLGDVVQFL YGEDGLDAMC IEKQKLGILN
MSDAAFEQKY RLDLANPPDW FKKDYEYGNE LTGDKPSMAL LDSEWDALLS DRRVVRRINK
SKMNEEMMQL PLHIGRVIES AKRVFNVKAN DRSNLRPSDV IVSIQEMLAK MKIVRGKDPI
SDEADANATI LWKALVRSRL SFKEIVKEHR LNKLAFDHIL GELLNRWDRA FVSPGEMVGV
LAAQSIGEPA TQMTLNTFHF AGVSSKNVTL GVPRLKEILN LAKNIKTPSM AVYLGEELAK
QEQAKKLRSM VEYTNLRSVT SVTEIYYDPD IQATNIPEDV DMVESYFLIP DDTQDTIDQQ
SRWLLRITLD RQKMLDKEIK IDDVAQRIKE EYNNDLAIIF SDNNAEEQVI RIRTVSAGDK
DDDGDGKMED DVMLKRLEAH LLDTLTLRGV PGVERAFLTK GTRMVESPDG ALLAIKNDDR
CTQWYLDTSG SALREVLAVN GVDGTRTYTN DLWQVVEVFG IEAARSALVK ELTNVLAFDG
SYVNHRHIAL LVDVMTYRGV ISAVTRHGIN RADTGALMRC SFEETVEILL EAAATGELDD
CRGISENVML GQMAPMGTGN FDVLLDPKML ETVISDNSRM GLMPGMPVKD GQVEGAATPY
DTGSPMADSG YLSLSSPAAG NFSPIQGAGS DTPTGFGTEY NGGGFGPGSM SPYSRGGAAS
PFSTSPTSPF GAGMGGYSPS SPNAGYSPTS PLIDGGIGRY ATSPSFSPSS PSFSPTSPML
RPTSPASPNY SPTSPSYSPA SPSSPRHYSP TSPAQFNSPT SPSYSPASPN YSPASPNLHA
GGATSPSYSP ASPTWSPTSP EAYSPTSPSF QRSPGAQHSP TSPSYSPTSP SFSPRTPGPG
TSGNQYSPNS PAND
//
