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Database: UniProt
Entry: A0A3Q4M1U7_NEOBR
LinkDB: A0A3Q4M1U7_NEOBR
Original site: A0A3Q4M1U7_NEOBR 
ID   A0A3Q4M1U7_NEOBR        Unreviewed;      1685 AA.
AC   A0A3Q4M1U7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-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};
GN   Name=POLR1A {ECO:0000313|Ensembl:ENSNBRP00000000544.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000000544.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000000544.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   RefSeq; XP_006781957.1; XM_006781894.1.
DR   STRING; 32507.ENSNBRP00000000544; -.
DR   Ensembl; ENSNBRT00000000583.1; ENSNBRP00000000544.1; ENSNBRG00000000519.1.
DR   GeneID; 102783638; -.
DR   CTD; 25885; -.
DR   GeneTree; ENSGT00920000149138; -.
DR   OMA; NREDYQQ; -.
DR   OrthoDB; 169836at2759; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000000519; Expressed in blood 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:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR   GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR   GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
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:UP000261580};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU004279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004279}.
FT   DOMAIN          293..629
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   REGION          1348..1467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1370..1389
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1390..1404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1405..1435
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1437..1461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1685 AA;  189382 MW;  506B0B1DA27C8197 CRC64;
     MLFGKEVPWR RLEGMSFGIY SAEEIRKLSV KAITNFRFLD GVGNVAPNGL YDLALGPADI
     KEVCSTCCQD FNNCPGHLGH IELPLPVYNP LFFDKLYLLI RGSCLACHML TCPRAAMHLL
     LNQLKLLDHG AMQEVYQIEQ VLGQYMEENV KATVDEVVQV LQVFTDATVG MNAATSENTK
     PIKHLVEKKG SLINDFWKIH MKTRKCPHCG CGRSTVRHEH NSKLIVTMPS GAQTSDKTEE
     DLLRGKRVYM TASTAREHVN KVWEKEGFFL KCLFSGLEEC MWSKEGGSSF YPDLFFLELL
     VVPPCRYRPI NRLGDQMFTN GQTVNMQAVM KDCDVIRKLL ALIAGEKIVP ETEAVEQTDQ
     SFLSGILGAT LTDKLYNVWV RLQSHVNIVF DSDMDKLMTE KYPGIRQILE KKDGLFRKHM
     MGKRVDYAAR SVICPDMYIG TNEIGIPMVF ATKLTYPQPV TPWNVKELRQ AVLNGPNVHP
     GASMVINEDG RKTILSPTCL AQREAVAKEL LTPSPGPRKM PMKIVNRHIK NGDVLLLNRQ
     PTLHRPSIQA HCARILPGEK VLRLHYANCK AYNADFDGDE MNAHFPQSEL GRAEAYTLVS
     TDQQYLVPKD GKPLAGLIQD HMVSGTRMTI RGCFFTKDQY TELVYRGLTD KPGRVKLLPP
     AILKPQQLWT GKQVVSTLLL NVIPEKAVPL NLAGKSKIPS KAWIQVPPRA NPGYQPESMC
     DSQVVIRQGE LLVGVLDKAH YGSSAYGLVH CCYELYGGET SGKLLSCLAR LFTAYLQLYR
     GFTLGVEDIL VKLGANKRRK KIIKESLKIG TKALQAAFNL PSNVDQAEAQ SRWQDAHLNP
     DQRDFITADH KFKEVANQVN NDINKVCMPV GLHTSFPDNN LQLMVQSGAK GSTVNTMQIS
     CLLGQIELEG RRPPLMPSGK FLPCFQPYDP APGAGGFVSG RFLTGIKPQE FFFHCMAGRE
     GLVDTAVKTS RSGYLQRCVI KHLEGLVVQY DLTVRDSDGS VVQFLYGEDG LDIPKTQFLQ
     PRQFPFIEDN YEVIRRSQGL DEVLARLDPQ SATKHFAAIQ RWKAKRELAC SRSGAFLLFS
     QKKLGKLKQT DEVEADCGRN PAVLQLVQQW HTLDEASRSK YCRKSSRCPE PSLGLFRPDV
     CFGSISENFH GITEKYLQSR DTVNQDRLDT HSLRQLLHYK WQRSLCDPGE AVGLLAAQSI
     GEPSTQMTLN TFHFAGRGEM NVTLGIPRLR EILMVASANI KTPMMSVPVL NNKRALKRVK
     VLRKKLARVC LAEVLQKVGV VETLRIENHH KLRVFKITFH FLPPERYSDD RLLSPQQILH
     YMETRFFRLL LEAIKKRSAK LASIAVETRR ATARDRDDDG NGAAASGGLD EGEEEQEREI
     VDDQENEGDT DASDAKRKGK QEEEVDYESE EEDNGDDPED KEDQGVEEVE EETTAVEEPQ
     ANGRRTEKRK KGEKRVEGAE SQSEMRVNSV LESNAAIERY SYDHKHELWC EVDLALPVSK
     VHFDLTSVLT SLAQNAVIME TKGLTRCLLS ETTTKTGEKE TVLNTEGINM HEIFKYSDIL
     DINRLYSNEV HAMAKTYGIE VALKVIEKEI KNVFAVYGIE VDPRHLSLVA DYMCYEGVYK
     PLNRHAIRSN SSPLQQMTFE TSYKFLKQAT MLGSHDQLVS PSACLVVGKV VRGGTGLFEL
     KQPLQ
//
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