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Database: UniProt
Entry: Q8MUU2_GIAIN
LinkDB: Q8MUU2_GIAIN
Original site: Q8MUU2_GIAIN 
ID   Q8MUU2_GIAIN            Unreviewed;      2076 AA.
AC   Q8MUU2; A8BY59;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE            EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
GN   Name=rpb1 {ECO:0000313|EMBL:AAM77743.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:AAM77743.1};
RN   [1] {ECO:0000313|EMBL:AAM77743.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12734189; DOI=10.1074/jbc.M303316200;
RA   Seshadri V., McArthur A.G., Sogin M.L., Adam R.D.;
RT   "Giardia lamblia RNA polymerase II: amanitin-resistant transcription.";
RL   J. Biol. Chem. 278:27804-27810(2003).
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; AF510651; AAM77743.1; -; Genomic_DNA.
DR   RefSeq; XP_001704218.1; XM_001704166.1.
DR   GeneID; 5697088; -.
DR   KEGG; gla:GL50803_0089347; -.
DR   VEuPathDB; GiardiaDB:DHA2_89347; -.
DR   VEuPathDB; GiardiaDB:GL50581_2856; -.
DR   VEuPathDB; GiardiaDB:GL50803_0089347; -.
DR   VEuPathDB; GiardiaDB:QR46_1940; -.
DR   OrthoDB; 169836at2759; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0043229; C:intracellular organelle; 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   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 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; 1.
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; 2.
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   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          234..552
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          2033..2076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2033..2059
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2060..2076
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2076 AA;  230455 MW;  A5B7F4467379C127 CRC64;
     MDKEFALRIP YGVPKRVRFT LFSENEKNSL IPIVPRESSS DQMSMFSELN STRLGVIFQE
     ENECPTCSGK AGDQDPSVLC PGHLGVVKFG YDIFHPMIID DLATLMNCFC PNCYHLKFFR
     LFKETDRELA INALNRLRDT TPTLNFLPKL AELSATIACC ERNILYRKKA SGTSRNGVAP
     QPLILAVSKS TRGSTARQAK DQDQLMDAHT CKLLITRYNK DDIVLLGLKR DHIENFIISS
     IQVGSRAVRP SIRTDGTTAE DQLTEMYVSL FRNIRDCNNN SLNAGGGATG AKSQIGPNDI
     YNAYKTLISA KGLNADGGSV PTKGIFERLS GKYGRMRSNL MGKRVNYCSR SVITGDPTIS
     INELGVPRSV ASRLTFPEVV TARNRDFLMK LVSNGNRYPG AVSKTLPSGT VQLIDTQVIN
     STGWGSSTDA DGRLGGETTN DPLPLGTIVN RHLLDGDYVL FNRQPTLHKS SFMGHRVKVL
     PYSTYRLNLS ATSSYNADFD GDEMNLHALQ SLEAVAEISE LCMVSNQVVS VKDNRPIVYI
     VQDVLLGCYL FTGKDVTIPF ARVCEYIMWM GFSRTSDPTY AHKLQRYDKG SVNQRGHSSA
     SMSYDFSDHT SGSYNPAEYD SSSYLVGNSA TGSVVDGRGS YLSTGNYGAS SASRKAYEDN
     INNDNGAYFK RPGSNVNTND HVLLNVSQPA ICYPEARWTG KQVFSMFVPR GVFYRSGDPK
     DISAHADKYI SFLDGSVMCG RIASSVVGGT ESALIHILFR DYGIEPCRAF IDNCQRVVCR
     FMLDHGFSVG MGDMVSSEHT ERKVAEIQTK LSKDISELFK LSIHYKIKLA PGQSRNDAFE
     QEVISKVSGT SLALEKVITD AAPHRNALLV MINAGSKGKK FNMMQISSSL GQQFLQSKRM
     PHRFETHRSL PCYSPFSSLN MESRGYIFNS FIRGLNPAEF YFHAVGGREG VCDTAVKTAD
     SGYVERKLLK VMESVCYRYD NSVRNDSNEI ISFRYGDDGI DPHKSESREF KDFSISDMDF
     LRAHYIDWSQ IVDFQNTEMD ESTDFYATLV REKFAVIIAK LRDTPEQFAH LCDGVSFYEV
     CDDELRAKGF DNLVLDNNLV SFTELSSYLQ NHYALFMDAE SSPGYVPENI DDSWLDIGVK
     SSLVLERDFA ISTILVEYIV LLLERIWLQR SRITLDTDVK KFTFGMNLDR IIQSEIQAGS
     INKVSRLIRE SAWRCYLKPF EAIEKVNKLL SRIKSFRPKE STLFRVILRQ CLSSKSCCYK
     YRLTSEQLDR ILATIEEKFV RGQVSPGEPV GPLAGHSVSE PATQLTLNTF HTAGTSALGG
     LGLPRLKELI DFRNPKISVS TIYLNISNQD PANAGVDTRC TSHSPMLFNR PVAPRPNSYN
     IASAEEATGR NIRQSKAWMN LAAKIEHTTF NYYIDDYKLI FDPFDELTCV ADDREWLHLE
     SEIGHLQQQV YGERPNEAVR FYSPFVLRYE IGLKQMQQKI EAGITIQTLV SRLILMLQQI
     YTSRAGRPKS EDDDEDDEDD INIKQKAMIG REMPIINYYT GLGKTVIRVR PSLTEDEYNA
     VKGSAIGSGA PDMEKSRLLA ERYDGVDAFL RNVHISGNES IRKVFMASSN PLVHYGYDGF
     TSNVDVFSQG SSDGLSMHKM SEGDLSKIGS IGKFTQPNSD ISELYLQTDG SDLLWILTQP
     EVDFTRTWTT NVREIYEILG IEAARALFIK QIRATLDKVD LNIHHYLILA DIMSSRPQNN
     KMISINRYGM QATNTGVLAQ ATFERPGATV LKAAAFGVVD PLKSVSSCVV MGKQGDFGTG
     CFDLLLNCAE LPSINEDELF PNSYYLKVHN ATTEVRPTAG AEETPVDSMG MPFSTTFISP
     TATAMVTPTS TYTSHSSVRS VVSAGGRVDA NMNPLFSPGC NRSRQAENAS RIFSSYTANT
     LTSAKSSLPT QLTITSRSRG LSNIVDGRDS RIASITSAVN SKMSAFSMTS CNSINSFRSA
     LASKASTHSN QYDTSDLVDV KGAGRYGIFT HSTNMSYENT AASIRNSGGM FASRSGSASS
     VRSQSATNID ASAADSGQSG ELRDNHEDDN NDYAEW
//
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