ID A0A1R0H0T4_9FUNG Unreviewed; 1863 AA.
AC A0A1R0H0T4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=AYI68_g3119 {ECO:0000313|EMBL:OLY82754.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY82754.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY82754.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY82754.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(2016).
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=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC diphosphate; 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:ARBA00048552,
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:OLY82754.1}.
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DR EMBL; LSSL01001268; OLY82754.1; -; Genomic_DNA.
DR STRING; 133383.A0A1R0H0T4; -.
DR OrthoDB; 270392at2759; -.
DR Proteomes; UP000187455; Unassembled WGS sequence.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:UniProtKB-ARBA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:UniProtKB-ARBA.
DR CDD; cd02584; RNAP_II_Rpb1_C; 1.
DR CDD; cd02733; RNAP_II_RPB1_N; 1.
DR FunFam; 2.40.40.20:FF:000019; DNA-directed RNA polymerase II subunit RPB1; 1.
DR FunFam; 1.10.132.30:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 1.10.150.390:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 1.10.274.100:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 3.30.1360.140:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 3.30.1490.180:FF:000001; DNA-directed RNA polymerase subunit; 1.
DR FunFam; 4.10.860.120:FF:000003; DNA-directed RNA polymerase subunit; 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 NCBIfam; NF006336; PRK08566.1; 1.
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; 15.
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; 25.
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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000187455};
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 256..559
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1582..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1820
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1839
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1852..1863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1863 AA; 207027 MW; A7D26EA90D768E24 CRC64;
MSNNFQFAFS SAPLRKVKRV QFGVFCPEEL KSLSVAKIDK PELKDENGRP KIGGLLDPRM
GTIDRNFKCQ TCGENMTECP GHFGHIELAR PVYHPGFIIR VKKILECVCW YCSKLKTDES
EPAFQLALKA SNPNRRMKLV WEICKTRTVC EASPESEDRP AAAPGMMGEE ERNRQLVDGI
VSSKRSKGHG GCGHRQPIFR KEGLKLSASF KGIPGEEGVT EGKQILSVTQ VLQVLKKVTD
EDASFLGLNP LFARPEWLVI TVMPVPPLAV RPSIMMDATR QSEDDLTYKL NDILKANARV
QSCEVEGAPL HIIEEFEALL QFHVATFMNN ELSGLPQALQ KSGRPIKSIR ARLKGKEGRV
RGNLMGKRVD FSARTVITGD PNIDIDQVGV PRSIARNMTF PEVVTPYNID KLQEMVQNGP
NEHPGAKYVI RDSGERIDLR YSKRSGDIPL RIGYRVERHM VDDDVVIFNR QPSLHKMSMM
GHRVKVMPYS TFRLNLSVTS PYNADFDGDE MNLHLPQSEE TRAEITEICM VPKQIVSPQS
NSPVMGIVQD TLCAVNIFTR RDCFVAYDFL MNLLMTVPNW DGVVPPPCII KPKPLWSGKQ
IYSLVIPKGI NCYRYNSVHP DNETTYCSPG DTRVIIENGE LLSGYLDKKT VGAVDSGLIH
VIRNELGPDA AKKFFGGTQK VINYWFLQAG FSIGIGDTIA DDSTMQTVGD IIRECYMRVD
ELIRDAQEDH LECLPGMTLK ETFESRVNSE LNRARDQAGK TVQNRLKECN NVRRMVVSGS
KGSYINVSQM TACVGQQNVE GKRIPFGFKY RTLPHFAKDD YSPQSKGFVE NSYLRGLTPQ
EFYFHAMGGR EGLIDTAVKT AETGYIQRRL VKALEDIMVH YDGTVRNSLG SIVDFVYGED
GMDASYLETQ RLETLTISNS RFERLYRVDV MDPAKSFRSD SLEFSILKNI EANDSVQQAL
DDEYQQLVAD RKLLQTFICK NGEPQRPLSV NMPRLIRNAQ QLFHIDKRKL SNLHPLKIVE
ETRKLMDRLT VVRGDDKLSV EAQANATLMF QIHLRSYLSP KRVLEEYNLD SNSFDWIVGE
IEARFKRALV APGEMVGVLS AQSIGQPATQ MTLNTFHFAG VSSKNVTLGV PRLKEIINVA
TNIKTPALSI YLEQDYAHNV ERVKDVQVAI EHTTLRKIMS STEIWYDPNI EDTVIDEDRE
FVQAYYEMPD EDIDPSCVSP WVLRLELNRN AVLDKKLTMT EITNKISETF GRDIMCICND
INSDKLIIRC RIVNSGGSPK DEDFEDGQME EDVFLKRIES HMLSSISLRG IEGVQRVYFV
EEKMNTLMDT GEFGQTTEWK LDTDGINLKQ VLWQDHVDYV RTYSNHPIEI FEVLGIEAAR
GALLRETRKV IEFDSSYVNY RHLGLLVELM TTRGHLSAIT RHGINRADTG PLMRCTFEET
AEILIDAAAA GDTDYCKGVT ENIILGQLAP LGTGSFEVVL DEDMLQNAVL DPRSQGFDLA
SAPNPPIYGV SSGNMTPQMT PYSNRSPEHF DISNTSNLSA MFSPIVESGS GSPSWSGLSP
YSPSSGISPT SPVAYMPASP AYSPNSPRYS PTSPTYSPTS PSYSPTSPSY SPTSPSYSPT
SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY
SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS
PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS
PTSPSYSPAS MSYSPTSPFY NPSPPSSYSP NSPSFLNNYA PGSHSPPSEP EDSYKPKDKK
NQR
//
