ID A0A1X2INX8_9FUNG Unreviewed; 1585 AA.
AC A0A1X2INX8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=BCR42DRAFT_481692 {ECO:0000313|EMBL:ORZ19705.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ19705.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ19705.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ19705.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORZ19705.1}.
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DR EMBL; MCGE01000007; ORZ19705.1; -; Genomic_DNA.
DR STRING; 90262.A0A1X2INX8; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000193560; 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; 3.
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:UP000193560};
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 239..531
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 154..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1585 AA; 177111 MW; D1DBB507E3DF751B CRC64;
MNGHPFAFSS APLRRVDAVQ FGILSPDEIK AMSVAKIEFP ELYDEGSQKP RACGLLDPRM
GTIDRNYKCQ TCGEGMAECP GHFGHIDLAK PVYHIGFLTK VKKILECVCF HCSKLKVDDT
NPRFVRARKI RDKKTRMKAV WELAKGKMVC EGGDNDDNGL EDDLDESRKN PHGGCGNKQP
LIRKDGLKLY ALFKASGSDD SGNDGKTLLT AGKVLQILKN ITDQDIRDMG LSEEYARPEW
MITTILPVPL HNRGEDDLTH KLSDVLKANA NVRRCESEGA PVHVVQEFEQ LLQFHIATYM
DNDIAGQPQA LQKSGRPLKS IRARLKGKEG RLRGNLMGKR VDFSARTVIT GDPNLSLDEV
GVPRSIARNL TYPEIVTSYN IDKLQALVRN GPLEHPGAKY VIRDNGERID LRYRKRAGEI
PLQLGYRVER HIVDGDVVIF NRQPSLHKMS MMGHRIRVMP YSTFRLNLSV TSPYNADFDG
DEMNLHVPQS LETRAEITEI CMVPKQIVSP QSNKPVMGIV QDTLAGIRKF TMRDLFLEKD
LVMNIVMWVP DWDGFIPPPA ILKPKPMWTG KQILSMVIPK GINCQTFYFS HPDDETTYIS
PGDSRVIIEN GELMCGIVCK KTVGTAGGGL IHTIVNELGS EAAKNFLTGT QQVVNYWLLQ
NGFSIGIGDT IADKPTMATI TNIIAQAKQR VQEIINTAQQ DKLEIQPGMT LRESFEAKVN
QTLNKARDDA GKLAQTNLKI DNNVKQMVMA GSKGSFINIS QMSACVGQQN VEGKRIPYGF
KLRTLPHFSK DDHSPESRGF VENSYLRGLT PTEFFFHAMG GREGLIDTAV KTAETGYIQR
RLVKALEDVM VKYDGTVRNS LGDIIEFCYG EDGMDGCSVE KQKLVPLRSS DKQFEERYRV
DLAEGGFRKG ALGYDVLKDI DGNETAQQYL DQEFLQLRED RDIMRRFIFK QGDDKWPLPV
NLQRLITNAQ QIFHIDPRKA SDVHPLQIVD GISSLAERLV VVRGTDKISA ETQRNATLLF
QMLLRSTFAV KRVVEEFHLS SQAFEWVLGE VESRFLTSVV APGEMVGTIA AQSIGEPATQ
MTLNTFHYAG VSSKNVTLGV PRLKEIINVA KNIKTPRLEV WLDAERSRNI ELAKEVQVHL
EHTTLQKVTS ASEIYYDPDP RSTIIEEDAE FVDTYYQLED DNSPVVTRVS PWLLRIELNR
GMMIDKRLNI TEVVQKISDE FKNDLHVIGS DENSEKLIIR CRVMSDESEE KDMDDEDTRT
EEDTFLRKLE SSMLSSINLR GIPRIQKVYI VERKDTILNS QGKFEQTTEW GLDTDGINLQ
QVMCQHGVDE RRTYSNNTTE IMEVLGIEAT RKALLKELRN VIEFDGSYVN YRHLALLCDV
MTNRGHLMAI TRHGINRAET GALMRCSFEE TVEILMEAAA VGELDDCRGV AENIMLGQMA
PLGTGEFDVI LDEEMLKTVP ENQRHHLMPN GVPGDVPGFA TPGPGFMTPS MATPYDTRSP
DWVDFSAPST PSEPMFSPMG NSGAVGATIG ASPWRSDLSP YASSPGYSPS SPFAASPGYS
PSSPSYSPSS PSYSPSSPSY SPSSP
//
