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Database: UniProt
Entry: A0A2I2YDZ9_GORGO
LinkDB: A0A2I2YDZ9_GORGO
Original site: A0A2I2YDZ9_GORGO 
ID   A0A2I2YDZ9_GORGO        Unreviewed;      1024 AA.
AC   A0A2I2YDZ9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000033132.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000033132.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000033132.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000033132.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; CABD030103503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2YDZ9; -.
DR   Ensembl; ENSGGOT00000051868.1; ENSGGOP00000033132.1; ENSGGOG00000014800.3.
DR   GeneTree; ENSGT00930000151033; -.
DR   Proteomes; UP000001519; Chromosome 17.
DR   Bgee; ENSGGOG00000014800; Expressed in testis and 5 other cell types or tissues.
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; cd02733; RNAP_II_RPB1_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 2.40.40.20; -; 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; 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; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          246..549
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1000..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1024 AA;  115297 MW;  A29722CE7D550C23 CRC64;
     MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP
     RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD
     SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG
     HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP
     RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
     HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD
     FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII
     RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS
     TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD
     TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
     NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM
     GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA
     HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSLV FPHTGPWGTF
     WELIPHLSVS QVIAVVGQQN VEGKRIPFGF KHRTLPHFIK DDYGPESRGF VENSYLAGLT
     PTEFFFHAMG GREGLIDTAV KTAETGYIQR RLIKSMESVM VKYDATVRNS INQVVQLRYG
     EDGLAGESVE FQNLATLKPS NKAFEKKFRF DYTNERALRR TLQEDLVKDV LSNAHIQNEL
     EREFERMRED REVLRVIFPT GDSKVRVGRS ADARDVPPWM AVPRNSPPSI PPSLRSSSPV
     TCCG
//
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