ID A0A9P0L1D4_ACAOB Unreviewed; 1710 AA.
AC A0A9P0L1D4;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN ORFNames=ACAOBT_LOCUS14864 {ECO:0000313|EMBL:CAH1982162.1};
OS Acanthoscelides obtectus (Bean weevil) (Bruchus obtectus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Bruchinae; Bruchini; Acanthoscelides.
OX NCBI_TaxID=200917 {ECO:0000313|EMBL:CAH1982162.1, ECO:0000313|Proteomes:UP001152888};
RN [1] {ECO:0000313|EMBL:CAH1982162.1}
RP NUCLEOTIDE SEQUENCE.
RA Sayadi A.;
RL Submitted (MAR-2022) 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=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|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:CAH1982162.1}.
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DR EMBL; CAKOFQ010006917; CAH1982162.1; -; Genomic_DNA.
DR OrthoDB; 270392at2759; -.
DR Proteomes; UP001152888; Unassembled WGS sequence.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IEA:TreeGrafter.
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: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 FunFam; 2.40.40.20:FF:000019; DNA-directed RNA polymerase II subunit RPB1; 1.
DR FunFam; 1.10.150.390: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:000005; 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; 2.
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; 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; 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; 13.
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; 17.
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:UP001152888};
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 236..539
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 1384..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1695
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1710 AA; 188809 MW; 80D09534EEF6DF49 CRC64;
MATNDSKAPL RTVKRVQFGI LSPDEIRRMS VTEGGIRFPE TMEAGRPKLC GLMDPRQGVI
DRNSRCQTCA GNMTECPGHF GHIDLAKPVF HIGFITKTIK ILRCVCFFCS KLLVSPNNPK
IKEVVMKSKG QPRKRLAFVY DLCKGKNICE GGDEMDVGKE GEENPQKKQG HGGCGRYQPN
IRRTGLELTA EWKHVNEDTQ EKKISLSAER VWEILKHITD EECFILGMDP KFARPDWMIV
TVLPVPPLAV RPAVVMYGSA RNQDDLTHKL ADIIKANNEL QKNEAAGAAA HIITENIKML
QFHVATLVDN DMPGMPRAMQ KSGKPLKAIK ARLKGKEGRI RGNLMGKRVD FSARTVITPD
PNLRIDQVGV PRSIAQNMTF PEIVTPFNFD KMLELVQRGN SQYPGAKYII RDNGERIDLR
FHPKPSDLHL QCGYKVERHI RDGDLVIFNR QPTLHKMSMM GHRVKVLPWS TFRMNLSCTS
PYNADFDGDE MNLHVPQSME TRAEVENLHI TPRQIITPQA NKPVMGIVQD TLTAVRKMTK
RDVFIEKEQM MNLLMFLPIW DGKMPKKSLT EYNNLKAMVV SGSKGSNINI SQVIACVGQQ
NVEGKRIPFG FRKRTLPHFI KDDYGPESRG FVENSYLAGL TPSEFYFHAM GGREGLIDTA
VKTAETGYIQ RRLIKAMESV MVHYDGTVRN SVGQLIQLRY GEDGLCGEMV EFQTLPTVKL
SNKAFEKKFR FDPSNERYLR RVFNEEVIKQ LMGSGEVISE LEREWEQLQK DREALRQIFP
SGESKVVLPC NLQRMIWNVQ KIFHINKRAP TDLSPLRVIQ GVRDLLKKCI IVAGEDRLSK
QANENATLLF QCLVRSTLCT KSVSEEFRLS TEAFEWLIGE IETRFQQAQA NPGEMVGALA
AQSLGEPATQ MTLNTFHFAG VSSKNVTLGV PRLKEIINIS KKPKAPSLTV FLTGAAARDA
EKAKNVLCRL EHTTLRKVTA NTAIYYDPDP QNTVIPEDQE FVNVYYEMPD FDPTRISPWL
LRIELDRKRM TDKKLTMEQI AEKINAGFGD DLNCIFNDDN AEKLVLRIRI MNSDDGKFGE
GGDEDVDKMD DDMFLRCIEA NMLSDMTLQG IEAISKVYMH LPQTDSKKRI VITETGEFKA
IAEWLLETDG TSLMKVLSER DVDPVRTFSN DICEIFSVLG IEAVRKSVEK EMNAVLQFYG
LYVNYRHLAL LCDVMTAKGH LMAITRHGIN RQDTGALMRC SFEETVDVLM DAASHAEVDP
MRGVSENIIM GQLPRMGTGC FDLLLDAEKC KLGIPIAQAH GTDIMSSGMF FGSAATPSSL
SPGGAMTPWN QGATPYVGSV WSPQNLMGSG MTPGGPAFSP SAASDASGMS PAYGAWSPTP
QSPAMSPYIA SPHGQSPSYS PSSPAFQQPT SPSMTPVSPG YSPSSPGYSP TSPNYSPTSP
SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPS SPRYTPASPS
YSPTSPSYSP TSPSYSPTSP SYSPASPSYS PSSPKYSPTS PNYSPTSPSF SGGSPQYSPT
SPSYSPTSPS YSPSSPQHTP AASTRYSPSS PNYSPSSPNY SPTSPQYSPH STKYSPTSPT
YTPTSPSYSP ASPAYSPQPP RYSPSSPNDQ
//
