RFA1_TETTS
ID RFA1_TETTS Reviewed; 671 AA.
AC D8UYN9; Q234B5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 2.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit {ECO:0000305};
DE Short=RP-A p70 {ECO:0000305};
DE AltName: Full=Replication factor A protein 1 {ECO:0000305};
DE Short=RF-A protein 1 {ECO:0000305};
GN Name=RPA1 {ECO:0000303|PubMed:19941821};
GN ORFNames=TTHERM_00106890 {ECO:0000312|EMBL:EAR92088.3};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19941821; DOI=10.1016/j.molcel.2009.09.041;
RA Min B., Collins K.;
RT "An RPA-related sequence-specific DNA-binding subunit of telomerase
RT holoenzyme is required for elongation processivity and telomere
RT maintenance.";
RL Mol. Cell 36:609-619(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210;
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
RN [3]
RP IDENTIFICATION IN THE RPA COMPLEX.
RX PubMed=27895115; DOI=10.1074/jbc.m116.763664;
RA Upton H.E., Chan H., Feigon J., Collins K.;
RT "Shared subunits of Tetrahymena telomerase holoenzyme and replication
RT protein A have different functions in different cellular complexes.";
RL J. Biol. Chem. 292:217-228(2017).
CC -!- FUNCTION: As part of the heterotrimeric replication protein A (RPA)
CC complex, binds and stabilizes single-stranded DNA intermediates, that
CC form during DNA replication or upon DNA stress (By similarity). It
CC prevents their reannealing and in parallel, recruits and activates
CC different proteins and complexes involved in DNA metabolism (By
CC similarity). Thereby, it plays an essential role both in DNA
CC replication and the cellular response to DNA damage (By similarity). In
CC the cellular response to DNA damage, the RPA complex controls DNA
CC repair and DNA damage checkpoint activation (By similarity).
CC {ECO:0000250|UniProtKB:P27694}.
CC -!- SUBUNIT: Component of the replication protein A complex (RPA), a
CC heterotrimeric complex composed of RPA1, RPA2/TEB2 and RPA3/TEB3.
CC {ECO:0000269|PubMed:27895115}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAR92088.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GQ274003; ADB03555.2; -; mRNA.
DR EMBL; GG662767; EAR92088.3; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001012333.3; XM_001012333.3.
DR AlphaFoldDB; D8UYN9; -.
DR SMR; D8UYN9; -.
DR STRING; 5911.EAR92088; -.
DR EnsemblProtists; EAR92088; EAR92088; TTHERM_00106890.
DR GeneID; 7846583; -.
DR KEGG; tet:TTHERM_00106890; -.
DR eggNOG; KOG0851; Eukaryota.
DR HOGENOM; CLU_409686_0_0_1; -.
DR OMA; ANDLREW; -.
DR OrthoDB; 1189265at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR PANTHER; PTHR23273; PTHR23273; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..671
FT /note="Replication protein A 70 kDa DNA-binding subunit"
FT /id="PRO_0000449912"
FT DNA_BIND 240..322
FT /note="OB"
FT /evidence="ECO:0000255"
FT ZN_FING 530..549
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 143..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 76806 MW; 9036A63597A0CA74 CRC64;
MVTQLTKNAI DSLINSTNPD EQYVIQVLKA PQSVAENLFK ICISDGFCKF KKGYFVSDAA
TKCQDLKDLC IIKCKKYIDD SNHDKERIII SNYELIYSNI QEQIGKPIEY KQYKSSGFSN
PEGSTVIPSQ YLSRNAQILQ QNQVSQPKQM VTPPVSNINK PTPAVNNTFA QKPAVTNQNI
QRVNQNPQQM NKTAPVKQNN NNNNNNNGNN KNNSSLQIST DGDEQNLEYI RNLQPNGQPQ
TIKVRITKKG DLKSFKEKQG KLFSIDVIDK FGDECSISFF NEIAEQYDGL FKVGQVIVLK
QFSVKVNNNH QYNKGDHTVT VNKESKILIC QEDPSIPMIK LNRQFIQDMQ NKQKGDLIDL
IVVVKADTEV KTMILKKDNQ QQSKRDIISF DESLIETEIT LWGETAKDYD AKQGDIIVFK
DAKIGEFKDK KQINIGYGTQ IFMNPDEQLF PQIHDVKKWY LSLNSDQLST IQKAQGNDTG
PREVTSFESS LNILKEEIKN LQTDPEMKIW KEIRGQIMYI KDTPLYYNAC FSCKKKIARN
NEVWTCINCN KDFNEPDSRY ILSLNISDST DTIWVSAFDE VGQKILGVKG DVFRYADEDT
EHGTETKKKL LMAAQNKEYR FLLLTKQERD QNGNARDKTV IHAIKDFQPA YEAKKIINSL
EKFMVIEENN P
