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Database: UniProt
Entry: A0A091FU54_9AVES
LinkDB: A0A091FU54_9AVES
Original site: A0A091FU54_9AVES 
ID   A0A091FU54_9AVES        Unreviewed;      1669 AA.
AC   A0A091FU54;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, 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};
DE   Flags: Fragment;
GN   ORFNames=N303_09577 {ECO:0000313|EMBL:KFO72531.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO72531.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO72531.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO72531.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KL447350; KFO72531.1; -; Genomic_DNA.
DR   STRING; 55661.A0A091FU54; -.
DR   Proteomes; UP000053760; 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; cd00084; HMG-box_SF; 1.
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:UP000053760};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          270..617
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1346..1439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1358..1378
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1379..1394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1395..1412
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1425..1439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO72531.1"
FT   NON_TER         1669
FT                   /evidence="ECO:0000313|EMBL:KFO72531.1"
SQ   SEQUENCE   1669 AA;  188804 MW;  98DCD436E2715E10 CRC64;
     RKLSVKLITN PQYLDNVGNP AANGLYDLAL GPPDSKEVCA TCMQNFTNCP GHFGHIELPL
     TVYNPLFFDK LYLLIRGSCL NCHMLTCTRA VVHLLLSQLK VLEKGLLHAV HDLEVILNRA
     KQCADATGSE IEEELNNHVQ EMLQSYQMKD QCSNVKNVCE CRNKLIAQFW KAHMSSKKCP
     NCKSRRSLVR KEHNSKLTVT YPSTVYHKLG EGVVLDEPAA IDESQLGKRG YLTPMTAKEY
     IQALWKNEGF FLRYLFPGTD PHDSSGFNPD MFFLDLLVVP PSRYRPVNRV GDRLFTNGQT
     VNLQAVMKDA KMIRKLLVFM AKEQCQPIKI TEEEIQTETG ENNEPLDHSF LTTIPGQTLA
     DKLYNAWIRL QTHVNIVFDS DMDKLMTEKY PGIRQLLEKK EGLFRKHMMG KRVDFAARSV
     ICPDMYIGTN EIGIPMVFAT KLTYPQPVTP WNVKELRQAV INGPKVHPGA SMVINEDGSR
     TVLSASSLTQ REAIAKQLLT PSSGAPQTGL KIVCRHIKNG DVLLLNRQPT LHRPSIQAHR
     ARILPGEKVL RLHYANCKAY NADFDGDEMN AHFPQSELGR AEAYTLAFTD EQYLVPKDGK
     PLPGLIQDHM ISGVSMTIRG CFFTREQYME LVYRGLTDKK GRIKILPPAI MKPQRLWTGK
     QVVSTLLINI IPENHIPLNL TGKAKIGGRA WVKGPAKRCL NLDSMCESQV IIRSGELLCG
     VLDKAHFGSS AYGLVHCCYE IYGGGTSGTV LTCLGRLFTA YLQLYRGFTM GIEDILVKHE
     ADQKRQKIIE ESSQHGIEAV RAALNLPETA SCEEVQGKWQ NAHLCKDQRD FNMVDLKFKE
     EVNNYNNEVN KVCMPLGLHR RFPENNLQLM VQSGAKGSTV NTMQISCLLG QIELEGRRPP
     LMASGKSLPC FQPYDFSPSS GGFVTGRFLT GIKPSEFFFH CMAGREGLVD TAVKTSRSGY
     LQRCIIKHLE GLVVQYDLTV RDSDGSVVQF LYGEDGLDIP KTQFLQPEQF PFIAENYEVI
     QKTSHLDEAL ARMESHQATQ HFKAIKKWRA RHQNSLQREG GFLMFARKKM ASVKARIPGG
     EMKNGRDPAT LQLLKMWYEL DEKKRRKYTK KANKCPDPSL GVWRPDTYFA SVSETFGSGV
     EDYINKWESE NRQSYTQPTL SSDRLKDLLY LKWQRSLCDP GEAVGLLAAQ SIGEPSTQMT
     LNTFHFAGRG EMNVTLGIPR LREILMVASA NIKTPTMSVP VFNTKKALKK VKQLKKLLTR
     VCLAEVLQKV EIEESLRVKC KQDKHHLYKI KFHFLPHEYY KEEKCVKPRE ILHFMETRFF
     KIFLEAIKKK NAKMTSFTEI STRKATRKDL DGDQDKNDQE APAEEEENIV DAEADEGDGD
     ATEAKRRRNQ EEEEANIDEN QEDEEAESEK EKTPDAEEDQ NGAGGDDSQP LSFVSQSKKE
     KNRLLQSMDL RINAVLDSHP SIQDYTFDTE NELWCEVSLA IPLMKVYFDL SSLLVSLARS
     TVIHEVKGIT RCLLNESTNK QGEKELILHT EGINLAEMFR YSDILDLNRL YSNDIHAMAK
     NYGIESALRA IIKEIKDVFA VYGIVVDPRH LSLVADYMCF EGFYKPLNRF GIQSNSSPLQ
     QMTFETSYKF LKEATMMGAH DELRSPSACL VVGKVVKGGT GLFDLKQPL
//
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