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Database: UniProt
Entry: A0A0V0ZTF0_9BILA
LinkDB: A0A0V0ZTF0_9BILA
Original site: A0A0V0ZTF0_9BILA 
ID   A0A0V0ZTF0_9BILA        Unreviewed;      1730 AA.
AC   A0A0V0ZTF0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:KRY15883.1};
GN   ORFNames=T12_7001 {ECO:0000313|EMBL:KRY15883.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY15883.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY15883.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY15883.1};
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:KRY15883.1}.
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DR   EMBL; JYDQ01000088; KRY15883.1; -; Genomic_DNA.
DR   Proteomes; UP000054783; 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:UP000054783};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          332..665
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1404..1448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1471..1499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1432..1448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1471..1486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1730 AA;  196683 MW;  A65F8330AAD189FA CRC64;
     MFIMVQQFYG DTMLSQKLKC QADCNTLNSA GFDILTPEEV LEISVKEITV PNAFDALYHP
     IAGGLCDPAF GPVDYMEYCA TCSFTGAQCP GHYGHIRLPL PMFNPLLFDI TYQLIRGTCF
     VCHRLFVADN EVALKIFFAQ MEALDEGNLA LALEIAEIST EVFSELCVSD SPNLQNLNNS
     ENSVKKNMLK ERLEELKKNR KTNSKGNLEI TKNVSQVRRE LISEFCTNFL YRRIKQCPSC
     ASQVTGIRNI GKRAVILTLP SKKGILKKKS NDSLKNNNKY AHGNQRYVSA AEVCSHLQMV
     WKNGGENILS SVFPMFKPRK NVQYADGFIP TDLLFLTHLL VMPPKFRPIV ELAGRKCDNP
     ISQIYRNIIE DCLSIKRFMQ KATADKWQTE DSESVDAVQD SEEQIQTLCL TMQSHVNELY
     DNSETSRIAS GLTVQLSARG LRQVLEKKEG LFRKHMMGKR VNFAARSVIA PDPYMSVDGV
     GIPEVFAKRL SFPEAVFSAN ATAMSEAVLH GPDVHPGANF IIDERGMKIY LNAGKEIERS
     GMAKRLLQTS QRFGIAYPKK VCRHLKENDF VLLNRQPTLH KPSIMAHKVK VLKNQRTLRL
     NYATCKTYNA DFDGDEMNAH FPQNEIARAE CSEIADVARQ FLVPKDGKPI AGLIQDHVVS
     GFMLTMKDKF LTKEDFNYLL LSAFPSVEHP WRQVPPTIFK PVRRWTGKQV VTTILLNVIP
     SHLPPINLVT KAKTSIKNWT VPGKRNPIFE LSESNVVICS GELLCGVLDK AQMGASPYGL
     VHCIFELYGP AVAAKLLSCF SRLFTTYLQM RGFTLGVEDI MLTRKADSKR RKLLSTVDRC
     GSEAVREALA LDVGIEDDEV KLILEKMHFK NEKESLLRVE QCFRQATDKF NDQANKVCFP
     NGLLKSFPDN GLSLMIETGA KGTSVNFFQM SCMLGQVDLE GQRVKVGMSG RTLPCFQRYD
     TKPRAGGFVS QRFLSGVRPQ EFFFHCLAGR EGLIDTAVKT SRSGYLQRCI IKHMEGIVAN
     YDLTVRDADG SIIQFYYGED GFDVTKSQFY DNTHLPFLHA NIDVLEQTSG DLPNFENEDN
     LIAAKRFSKI KRWKEKYGKC PEVESMHKSQ LALLPNVNED SSNVDKEQLV AAWFEHPVEE
     RRRWLRQSVK WRPDPVMSTL RPTTCIGALS DKFLEQLDNF IQQRQARVDE SVHKFEKLMK
     LRGMRSLVEP GETVGLLAAQ SIGEPSTQMT LNTFHFAGCG EMNVTLGIPR LREILISGSA
     TISTPTSRVQ FRHGVSRELA EDVQRRMNRI VLNQVLEFAN QMEFVTTDGY CSYCCILRTG
     WYSRLLIDAN FFHRAKYREY EITLKLSKRR KRPHSVRHLD SRTVMAKIEQ GFFRSLCFSL
     KKMFDSGNKF REVEMFHIEN ENEINENEDG LTFAGGNDQD SSEEEDDNDV DAVEAQQRQR
     HKDDNEYLGE DEEAIELNLF TSGENCLFDS TGNEGESVVQ QNNSSEEIRP GKDDDDDQHL
     PLDQYRVKMV VEQDSLITDY RYDSKRNHWC KATVKVPFKY GAIDMRYLVE EECSKFVVQS
     VRDIKRCMLT EQNGELFLIT EGINLKVFTE RPDIFNVDRI YCNNIHTMAS MYGIEAAAQS
     IIRETKNVFA SYGIEVDHRH LSLLSDYMTH TGKYYSFSRN YMNSSTSPFQ KMSFETTVNY
     MKEALTRRTL DTMQTPSANL VVGRLPRFGT GFFDVLAPLP NRNVEAEAEQ
//
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