ID A0A2T9YD65_9FUNG Unreviewed; 1823 AA.
AC A0A2T9YD65;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=BB559_000101 {ECO:0000313|EMBL:PVV00108.1}, BB559_004714
GN {ECO:0000313|EMBL:PVU90271.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU90271.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU90271.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU90271.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU90271.1}.
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DR EMBL; MBFT01000491; PVU90271.1; -; Genomic_DNA.
DR EMBL; MBFT01000006; PVV00108.1; -; Genomic_DNA.
DR STRING; 61424.A0A2T9YD65; -.
DR Proteomes; UP000245699; 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; 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; 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; 14.
DR PRINTS; PR01217; PRICHEXTENSN.
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; 18.
PE 3: Inferred from homology;
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:UP000245699};
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 255..558
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 152..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1823 AA; 202383 MW; 50A7741DB120A647 CRC64;
MSNNYQFSYS SAPLKKITHV QFGTFSPEEL KKMSVAKIDK PELKDENGRP KMGGLLDPRM
GSIDRNFKCQ TCGENMTECP GHFGHIELTR PVYHPGFIIR VKKILECVCW FCSKLKTDDS
EPAFQRALKV RNSNQRLKMV WDICKSRTTC EASPESEERP PVSEFQDEEG RNRQLVDGLI
GSKRKKGHGG CGNKQPVFRK EGLNLTATFK STGGEEGVAE GKQPISVTQV LQVLKKISDE
DALAMGLNVQ FARPEWLIIS VMPVPPLAVR PSIQMDATRQ SEDDLTYKLN DIIKANVRVQ
SCEVEGAPLH IIEEFEKLLQ FHVATFMNNE ISGLPQALQK SGRPIKSIRA RLKGKEGRLR
GNLMGKRVDF SARTVITGDP NIDIDQVGVP RSIARNMTYP EVVTPYNIEK LQEMVQNGPN
EHPGAKYVIR DSGERIDLRY SKRGGDIPLR IGYRVERHML DDDVVIFNRQ PSLHKMSMMG
HRVKVMPYST FRLNLSVTSP YNADFDGDEM NLHLPQSEET RAEVTEICMV PKQIVSPQSN
MPVMGIVQDT LCAINIFTKR DTLLQYDFVM NLLMTIPDWD GIVPTPCILK PQPLWSGKQI
YSMVIPKGVN CHRYNSTHPD NEYTWCSPGD TRIIIENGEL LSGALCKRTV GAVDSGLIHV
IRNELGPDYA KKFFGGTQKL VNYWFLQTGF SVGIGDTIAD DSTMQTVGDI IRECYMRVDE
LIRDAQEDRL ERLPGMTLKE TFESKVNGEL NRARDQAGKT VQNRLKECNN VRRMVVSGSK
GSYINVSQMT ASVGQQNVEG KRIPFGFKNR TLPHFSKDDY SPQSRGFVEN SYLRGLTPQE
FYFHAMGGRE GLIDTAVKTA ETGYIQRRLV KALEDIMVHY DGTVRNSLGS IIDFVYGEDG
MDACFLETQN LQTLTISDNR FENMYRVDVM DSSKGFSSDS LDFSILKNIE ANDSVQLLLD
EEFNQLTLDR KELQSFICTT GESTHPMPAN MPRLILNAQQ IFHIDRRKPS NLHPSYVIEG
IRQLADRLVV IRGDDKLSTE AQMNATLLFK IHLRSFLSTK RVIEEFHLDT NSFDWIIGEV
EACFKRAIVS PGEMVGTLAA QSIGQPATQM TLNTFHYAGV SSKNVTLGVP RLKEIINVAT
NIKTPALSIY LVPEYAHNVE RVKDVQVAIE HTTLRNIMAS TEIWYDPNIE DTIIDEDREF
VQAYYEMPDE EISSSSVSPW LLRLELSRSA VLDKKLSMSE ITNRISEFFG REIMCICNDI
NSDKLIIRCR TVRRDGGSKD DEMDESSVEE DVFLKKIEDV MLSEISLRGI KGITRVYFVQ
ENTNTLMDTG EFGRTTEWKL ETDGINLKEA LWQDHVDFHR TYSNHPIEIL EVLGIEAARG
ALLRETRKVI ESDSSYVNYR HLGLLVELMT TRGRLSAITR HGINRADTGA LMRCTFEETV
EILTDAAASG DVDHCKGVAE NIILGQMVPL GTGSFDVVLD EDMLQHAVLD PRSQGFDLAA
APNPPLYSIS AGNMTPQMTP YDSRSPAYID YSSLSSPITA VFSPIVDSGG ASPSWSGLSP
YSPAVGISPN SPAAYVPASP AYSPTSPGYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT
SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS
PSYSPTSPSY SPASLSYSPT SPSYSPTSPS YSPTSPFYNP ASPTYADTSS YPASGSYSPA
SYSPDSDHSG KPNGNVSNKK NRS
//
