ID A0A452H1E7_9SAUR Unreviewed; 1487 AA.
AC A0A452H1E7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00012418};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000008437.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000008437.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460}.
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DR Ensembl; ENSGAGT00000009713.1; ENSGAGP00000008437.1; ENSGAGG00000004984.1.
DR Proteomes; UP000291020; 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; 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; 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; 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; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 111..454
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 1208..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 168588 MW; D245FD9D4354283C CRC64;
LKLSKLIAQF WKLHMTSKRC PNCKSRRSLV RKEHNSKLTV TYPTVVQQKS GKEAILEEPA
IIDETQLGKR GYLTPITAKD HVVALWKNEG FFLNYLFSGL EVGENSGFSP DMFFLDLLVV
PPSRYRPVNR LGDQMFTNGQ TVNLQAVMKD VQLIRKLLAF MAQEQSQPIK LVENEIQKPL
ESLDRSVLAM ISGQSTADKL YNIWIRLQSH VNIVFDSDMD KLMTEKYPGV RQILEKKEGL
FRKHMMGKRV DYAARSVICP DMYIATNEIG IPMVFATKLT YPQPVTPWNV KELRQAVING
PNVHPGASMV INEDGSRTVL SASSQTQREA IAKQLLTPST GAPKPGMKIV CRHLKNGDVL
LLNRQPTLHR PSIQAHRARI LPGEKVLRLH YANCKAYNAD FDGDEMNAHF PQSELGRAEA
YVLACTDEQY LVPKDGKPLA GLIQDHMISG ASMTIRGCFF TREQYMELIY RGLTDKKGRV
KILPPAIMKP QRLWTGKQVI VSTLLINVIP ENQIPLNLSG KAKIGGKAWV KGPQNRIPGS
NLDSMCESQV IIRDGELLCG VLDKAHYGSS AYGLVHCCHE VYGGETSGKV LTCLARLFTA
YLQLYRGFTM GVEDILVKPQ ADHRRHRIIE VSTHCGTRAV RSAFNLPETA SCEEIQGKWQ
DAHLHKDQRD FNMVDLKFKE EVNTYSNEVN KACMPLGLHR SFPENNLQLM VQSGAKGSTV
NTMQISCLLG QIELEGRRPP LMASGKSLPC FQPYDFSPRS GGFVTGRFLT GIKPAEFFFH
CMAGREGLVD TAVKTSRSGY LQRCIIKHLE GLVVQYDLSV RDSDGSVVQF LYGEDGLDIP
RTQFLQPKQF PFIAENYEVI QKSKHIDEVL SKMDPQQANQ HFRAIKKWQA KHQVSLPREG
AFLMYSQKKM ARVREQTLGG EIINGRDPAT LQLLKMWYEL DEKSRRKYIK RTSKCPDPSL
AVWRPDVYFA SVSEAFESEV ENYISEWNAR NNSNYVKSEL SCDRLSNLLH LKWQRSLCDP
GEAVGLLAAQ SIGEPSTQMT LNTFHFAGRG EMNVTLGIPR LREILMVASA NIKTPMMSVP
VLSTKKAHKK VKRLKKQFTR VCLAEVLRKV EVEESLCIEG KLSKHRLYQI KFYFLPYEYY
REEKCLKPRD ILYFMETRFF KILLETIKRK SAKLASFNVV NTRKATRRDL DGSGEESQEN
QHIISVQVDY ESEEENSEEN GDENAEEEEG MLHDDKRAED AEEGVQNENN CQTKKEKGPK
LEHSTQLRVS AVMSSHSSIV NYTYDTENEL WCEVSLKLPL MKAYFDLSSI LTSLMQNTIV
HETKGITRCF LNESTNKKGE KEFVLNTEGI NLPELFRYAD LLDLSRLYSN DIHAMAKTYG
IEAALRVIEK EIKDVFAVYG IVVDPRHLSL VADYMCFEGV YKPLNRFGMQ SNSSPLQQMT
FETSYKFLKE ATMMGAHDEL RSPSACLVVG KVVRGGTGLF DLKQPLT
//
