ID A0A182FPR1_ANOAL Unreviewed; 2090 AA.
AC A0A182FPR1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|RuleBase:RU363031};
DE EC=2.7.7.6 {ECO:0000256|RuleBase:RU363031};
OS Anopheles albimanus (New world malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB008528-PA, ECO:0000313|Proteomes:UP000069272};
RN [1] {ECO:0000313|EnsemblMetazoa:AALB008528-PA}
RP IDENTIFICATION.
RC STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB008528-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) 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:RU363031}.
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:RU363031};
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|RuleBase:RU363031}.
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DR STRING; 7167.A0A182FPR1; -.
DR EnsemblMetazoa; AALB008528-RA; AALB008528-PA; AALB008528.
DR VEuPathDB; VectorBase:AALB008528; -.
DR VEuPathDB; VectorBase:AALB20_026395; -.
DR VEuPathDB; VectorBase:AALB20_028895; -.
DR Proteomes; UP000069272; Chromosome 2R.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1070.20; -; 1.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR011678; EMC1_C.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR PANTHER; PTHR20856:SF7; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2; 1.
DR Pfam; PF07774; EMC1_C; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|RuleBase:RU363031};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU363031};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363031};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363031};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 38..441
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 201..394
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 468..532
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 567..629
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04566"
FT DOMAIN 653..701
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04567"
FT DOMAIN 708..1081
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1083..1173
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
FT DOMAIN 1884..2089
FT /note="ER membrane protein complex subunit 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07774"
SQ SEQUENCE 2090 AA; 234680 MW; 7C04EBED1B2C5553 CRC64;
MYENEDDHFE EEDPEEISHE LWQEACWIVI NAYFDEKGLV RQQLDSFDEF IQMSVQRIVE
DSPAIELTAE AQHSSGEIEN PTRYLLKFDQ IYLSKPTHWE KDGSPSPMMP NEARLRNLTY
SAPLYVDITK TKIVEGQDPV ETQHQKTFIG KIPIMLRSTY CLLSQLTDRD LTELNECPLD
PGGYFIINGS EKVLIAQEKM ATNTVYVFSM KDGKYAYKTE IRSCLEHSSR PTSTLWVNMM
ARGGQSIKKS AIGQRVIAIL PYVKQEIPIM IVFRALGFVA DRDILEHIIY DFDDPEMMEM
VKPSLDEAFV VQEQNVALNF IGARGARPGV TKDKRIKYAK EILQKEMLPH VGVSDFCETK
KAYFLGYMVH RLLLAALGRR ELDDRDHYGN KRLDLAGPLL AFLFRGLFKN LMKEVRMYAQ
KFIDRGKDFN LELAIKTKII TDGLRYSLAT GNWGDQKKAH QARAGVSQVL NRLTFASTLS
HLRRVNSPIG RDGKLAKPRQ LHNTLWGMIC PAETPEGAAV GLVKNLALMA YISVGSQPSP
ILEFLEEWSM ENLEEIAPSA IADATKIFVN GCWVGIHRDP EQLMATLRKL RRQMDIIVSE
VSMIRDIRDR EIRIYTDAGR ICRPLLIVEG GSLLLRKHHI DMLKDRDYNN YGWQVLVASG
VVEYIDTLEE ETVMIAMTPY DLKQDKEYAY CTTYTHCEIH PAMILGVCAS IIPFPDHNQS
PRNTYQSAMG KQAMGVYITN FHVRMDTLAH VLYYPMKPLV TTRSMEYLRF RELPAGINSI
VAILCYTGYN QEDSVILNAS AVERGFFRSV FYRSYKDSES KRIGDQEEQF EKPNRQTCQG
MRNALYDKLD EDGIIAPGLR VSGDDVVIGK TITLPETDDD LDGTTKRFTK RDGSTFLRNS
ETGIVDQVML TLNSEGYKFC KIRVRSVRIP QIGDKFASRH GQKGTCGIQY RQEDMPFTCE
GITPDIIINP HAIPSRMTIG HLIECIQGKL GSNKGEIGDA TPFNDAVNVQ KISTFLQEYG
YHLRGNEVMY NGHTGRKINA QVFLGPTYYQ RLKHMVDDKI HSRARGPVQI LVRQPMEGRA
RDGGLRFGEM ERDCQISHGA AQFLRERLFE VSDPYRIHVC NFCGLIAIAN LRNNTFECKG
CKNKTQISQV KLPYAAKLLF QELMAMNIAP RLMRFKMMWA GVWLLALVTT CSGLYEDQIG
KFDWRQQYVG KIVHGAFDTT SVDRIIVATE SNVLAAISAK TGDIVWRQVL ESGSRGEVKL
LHVSNPSATG ARVGSRGHPG HDVITVTGSL PALVRGWNSN TGTLEWEWSL LPSVDDQAAA
DAVWFEHDGL LYHVVPVWGS HLEVTPYQAV SGQQARPMTS RIAASWTAKD RCALTESFFA
CTSKDQLLAL DLAADSSSAI LSKPLGAEGV GRPRPVRGEA AVIQNGRYYS LRTDQKLAFA
GKDAALVDRT IQEGEPILLR GTVDRVNNRL LIVAHRLRDF VKLDPIEFTI DYSDTLGDPE
LISVRCKQSN SGNSGAGLVC RMLLSAEDGA ILLIQQGKIK WVREEALAEV ATADFLDLTL
SDAEGAIEEE LNNKNGDVYG AFQRRITSQA LHLKNLFLHI LGVGPAPSKA QRAGLVRDDF
GLHKMLVVVT NSGKVFGIDN VSGKHHWIRY LPSFVGFANN VPMKLLVQRT SRFYPLPAQC
VIVGRDRMTL NGLLYIFNPI TGQPVQGGGV VELPYSVSQI SLLHKTGPDF LKALLLLDDK
NVAHVVPETL EVYADNFYMF TANHQTGQMN GFHVQYNPSS TKASKLTTTP SWQIDLSGGS
KRQQIIACEG KNPIEHVHSQ GRVMADRSVL YKYINPNLVA VATHGADNIH KYIMNVHLVD
VVSGSIVFSM SHKRVRPPLH MVHSENWLVY SYFNDKARRT EITSIELYEG KTQTNGTVWS
SLDAPPLPMV ERQSYILPVA VSALKETITE KGITSKHILI GLSTGAVAEM SWALLDPRRP
VTSPEKAREE GIMPYMPELP MPHEILVNYN QTVANLRGIH TAPSGLESTC LVLVHGLDLF
VTRVSPSKTF DLLKEDFDYF LITIVLTALT TTSFVVKQLA SKKIVKQAWK
//
