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Database: UniProt
Entry: A0A0V0XJ89_TRIPS
LinkDB: A0A0V0XJ89_TRIPS
Original site: A0A0V0XJ89_TRIPS 
ID   A0A0V0XJ89_TRIPS        Unreviewed;      1726 AA.
AC   A0A0V0XJ89;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   Name=Polr1a {ECO:0000313|EMBL:KRX88044.1};
GN   ORFNames=T4E_6681 {ECO:0000313|EMBL:KRX88044.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX88044.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX88044.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX88044.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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   -!- 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:KRX88044.1}.
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DR   EMBL; JYDU01000253; KRX88044.1; -; Genomic_DNA.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd02735; RNAP_I_Rpa1_C; 1.
DR   CDD; cd01435; RNAP_I_RPA1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.357.120; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.70.2850; -; 1.
DR   Gene3D; 6.10.250.2940; -; 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; IPR047107; DNA-dir_RNA_pol1_lsu_C.
DR   InterPro; IPR015699; DNA-dir_RNA_pol1_lsu_N.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF11; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA1; 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   SMART; SM00663; RPOLA_N; 1.
DR   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU004279};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004279}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          342..675
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1406..1441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1424..1441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1726 AA;  196070 MW;  A116FA535CE78E20 CRC64;
     MLSQKLKCQA DCNTLNSAGF DILTPEEVLE ISVKEITAPN AFDALYHPIA GGLCDPAFGP
     VDYMECCATC SFTGAQCPGH YGHIRLPLPM FNPLLFDITY QLIRGTCFVC HRLFVADNEV
     ALKTFFAQME ALDEGNLALA LEIADISTAV FSELCVSDSL NLQYLKDSEN SVKESVLKER
     LEELKKNCSV QNRIFLIQFD HNCLFSHSGK ANSKGNLEIT KNVSQVRREL ISEFCTNFLY
     RRIKQCPSCA SQVTGIRNIG KRAIILTLPS KKGALKNKNN DLLKNSNNKY VHSNQRYVSA
     AEVCSHLQMV WKNGGESILS SIFPMFKTRK NLQYADGFIP TDLLFLTHLL VMPPKFRPIV
     ELAGRKYDNP ISQIYRNIIE DCLSIKRFMQ KATADKWQTE GSESVDAVQD NEEQIQTLCL
     TMQSHVNELY DNNETSRIAS GLTVQLNAKG LRQVLEKKEG LFRKHMMGKR VNFAARSVIA
     PDPYMSVDGV GIPEVFAKRL SFPEAVFSAN ATAMCEAVLH GPDVHPGANF LIDERGVKIH
     LNAGKEIERS GMAKRLLQTS QRFGIAYPKK VCRHLKENDF VLLNRQPTLH KPSIMAHKVK
     VLKNQRTLRL NYATCKTYNA DFDGDEMNAH FPQNEIARAE CSEIADVARQ FLVPKDGKPI
     AGLIQDHVVS GFMLTMRDKF LTKEDFNYLL LSAFPSVEHP WRQVPPTIFK PVRRWTGKQV
     VTTILLNVIP SHLPPINLVT KAKTSIKNWT VAGKREPIFE LSESNVVICS GELLCGVLDK
     AQMGASPYGL VHCIFELYGP AVAAKLLSCF SRLFTTYLQM RGFTLGVEDI MLTRKADSKR
     RKLLSTVDSC GSEAVREALA LEAEIEEDEV KLILAEKHFK NEKESLLRVE QCFRQATDKF
     NDQANKICFP NGLLKAFPDN GLSLMIETGA KGTSVNFFQM SCMLGQVDLE GQRVKVGMSG
     RTLPCFQRYD TKPRAGGFVS QRFLSGVRPQ EFFFHCLAGR EGLIDTAVKT SRSGYLQRCI
     IKHMEGIIAN YDLTVRDADG SIIQFYYGED GFDVTKSQFY DRTHLPFLHA NIDVLEQTSR
     DLPNFENEDN LIAEKRFAKI KRWKEKYEKC QEVESTVHKS QLAFLPNVED SSKEQLVMAW
     FECPVEERRR WLKQCAKWRP DPVMSTLRPT TCIGALSDKF LEQLDNFIEE RQATIDKSVQ
     KFAKLMKLRG MRSLVEPGET VGLLAAQSIG EPSTQMTLNT FHFAGCGEMN VTLGIPRLRE
     ILISGSATIS TPTSRVQFRQ GVSRELAEDV QRRMNRIVLN QVLEFANQME FVTTDGYSCY
     CILHADWAKF REYEITLKLS KRRKRPYSVR HLDSRTIMAK IEQSFFRSLC FSLKKMFDSG
     NKFREVEMLH IENENEINEN EDALTFAGGN DQESSEEDDD NDVDAVQAQQ RQRHKDDNEY
     LGEDEEAIEL NLLTSGESCL FDSTGESIVR QNSNSEEIRP AKDDDEQHLP LDQYRVKVMV
     VEQDSLITDY SYDSKRNHWC KATVKVPFKY GAIDMRYLVE EECSKFVVQS VRDIKRCMLT
     EENGELFLIT EGINLKVFTE RPDIFNVNRI YCNNIHTMAS MYGIEAAARS IIRETKNVFA
     SYGIEVDHRH LSLLSDYMTH TGKYYSFSRN YMNSSTSPFQ KMSFETTVNY MKEALTRRTL
     DKMQTPSANL VVGRLPRFGT GFFEVLALLP SITTAEDRNV ETEVQQ
//
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