ID A0A3Q3AW30_KRYMA Unreviewed; 1390 AA.
AC A0A3Q3AW30;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA-directed RNA polymerase subunit {ECO:0000256|RuleBase:RU004279};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU004279};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000020781.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000020781.1}
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|RuleBase:RU004279};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|ARBA:ARBA00006460, ECO:0000256|RuleBase:RU004279}.
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DR RefSeq; XP_017294036.1; XM_017438547.1.
DR Ensembl; ENSKMAT00000021055.1; ENSKMAP00000020781.1; ENSKMAG00000015290.1.
DR GeneID; 108249262; -.
DR CTD; 11128; -.
DR GeneTree; ENSGT00930000151028; -.
DR OrthoDB; 169836at2759; -.
DR Proteomes; UP000264800; Unplaced.
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; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_N; 1.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF32; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1; 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:UP000264800};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT DOMAIN 248..553
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
SQ SEQUENCE 1390 AA; 155626 MW; 7D68681D0A9DF52A CRC64;
MVKEQFRETD VAKKISHICF GIKSAEQMRK QAHIQVVSKN LYSQDAKHTP LAYGVLDHRM
GTSEKDRPCL TCGKNLADCL GHYGYLDLEL PCFHVGYFKA IIGILQMICK TCSSIMLTKE
EKQQFMDYLK RPNLAYLQKR GLKKKISDKC RKRTVCLQCS AFNGPVKKCG LLKIIHEKYK
TSKKVVDSFV SEFLQSFDTA IEHNKLMEPL LSRAQENLNP LVVLNLLRRI PAEDVPLLLM
NPDAGKPADL IITRLLVPPL CIRPSVVSDL KSGTNEDDLT MKLTEIIFLN DVIKKHRMTG
AKTQMIMEDW DFLQLQCALY INSELSGIPL NMAPKKWTRG FVQRLKGKQG RFRGNLSGKR
VDFSGRTVIS PDPNLRIDEV AVPVHVAKIL TYPERVNKAN LELMRKLVRN GPDVHPGANF
IQNRHTQMKR FLKYGNREKI AQELKFGDVV ERHMIDGDIV LFNRQPSLHK LSIMAHIARV
KPHRTFRFNE CVCTPYNADF DGDEMNLHLP QTEEAKAEAL ILMGTKANLV TPRNGEPLIA
AIQDFLTGAY LLTLKDTFFD RSKACQIVAS ILVGKDEKVK ISLPHPAIMK PIALWTGKQI
FSIILKPSKD CPVNANLRTK GKQYCGKGED LCFNDSYVVI HNSELMCGSM DKGTLGSGSK
NNIFYILLRD WGQLEAANAM SRLARLAPVY LSNRGFSIGI GDVTPGQGLL KAKQDLLDDG
YGKCDEYIEA LATGKLQQQP GCTAEETLEA LILRELSVIR DRAGSACLRE LDKSNSPLIM
ALCGSKGSFI NISQMIACVG QQAISGSRVP DGFENRSLPH FEKHSKLPAA KGFVADSFYS
GLTPTEFFFH TMAGREGLVD TAVKTAETGY MQRRLVKSLE DLCSQYDLTV RSSTGDIIQF
IYGGDGLDPA AMEGKDEPLE FKRVLDNIRA VYACPNEPAL SQNELVLTAD DIMKRADFVC
CRDNFLEEIR KFIKTTSERI KKTRDKYGIN DNGTTEPKVL YQLDRITPTQ LEKFLETCRD
KYMRAQMEPG SAVGALCAQS IGEPGTQMTL KTFHFAGVAS MNITLGVPRI KEIINASKNI
STPIITAHLD IEDDADFARL VKGRIEKTLL GEISEYIEEV FLPDDCFILV KLSLERIRLL
RLEVNAETVR YSICMSKLRV KPRDIAVHGE AVVCVSPKEN NKSSMYYVLQ SLKEELPKVV
VQGIPEVARA VIHIDEQTGK NKYKLLVEGD NLRAVMATHG VNGNRTTSNN TYEVEKTLGI
EAARSTIINE IQYTMVNHGM SIDRRHVMLL ADLMSYKGEI LGITRFGLAK MKESVLMLAS
FEKTADHLFD AAYFGQKDSV CGVSECIIMG IPMNIGTGLF KLLHKANRDP TPVTRPLLFD
SADFHIPLIT
//
