ID   RPA_METTH               Reviewed;         792 AA.
AC   O27438; O27437;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Replication factor A;
DE            Short=RF-A;
DE            Short=RP-A;
DE            Short=RPA;
DE   AltName: Full=Replication factor A protein 1;
DE   AltName: Full=Replication protein A;
DE   AltName: Full=Single-stranded DNA-binding protein;
GN   Name=rpa; OrderedLocusNames=MTH_1384/MTH_1385;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   SEQUENCE REVISION TO 614, FUNCTION, AND SUBUNIT.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=10497247; DOI=10.1074/jbc.274.40.28751;
RA   Kelman Z., Pietrokovski S., Hurwitz J.;
RT   "Isolation and characterization of a split B-type DNA polymerase from the
RT   archaeon Methanobacterium thermoautotrophicum deltaH.";
RL   J. Biol. Chem. 274:28751-28761(1999).
RN   [3]
RP   FUNCTION, INTERACTION WITH HEL308, SUBUNIT, AND DNA-BINDING.
RX   PubMed=21195035; DOI=10.1016/j.dnarep.2010.12.001;
RA   Woodman I.L., Brammer K., Bolt E.L.;
RT   "Physical interaction between archaeal DNA repair helicase Hel308 and
RT   replication protein A (RPA).";
RL   DNA Repair 10:306-313(2011).
RN   [4]
RP   STRUCTURE BY NMR OF 62-167.
RA   Rossi P., Xiao R., Acton T.B., Montelione G.T.;
RT   "Solution NMR Structure of the replication factor A related protein from
RT   Methanobacterium thermoautotrophicum. Northeast structural genomics target
RT   TR91A.";
RL   Submitted (JUN-2008) to the PDB data bank.
CC   -!- FUNCTION: Inhibits DNA polymerase activity of PolB, which can be
CC       overcome by RFC and PNCA. Stimulates 3'-to 5'-exonuclease activity of
CC       PolB at 30 degrees Celsius, but has no effect at 50 or 70 degrees
CC       Celsius. Bind ssDNA and replication forks; replication forks structures
CC       bind both Hel308 and this protein. Has no effect on helicase activity
CC       of Hel308; may help target the helicase to DNA substrates that require
CC       DNA re-modeling. {ECO:0000269|PubMed:10497247,
CC       ECO:0000269|PubMed:21195035}.
CC   -!- SUBUNIT: Probably binds DNA polymerase PolB. Binds helicase Hel308, in
CC       presence and absence of DNA. {ECO:0000269|PubMed:10497247,
CC       ECO:0000269|PubMed:21195035}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB85861.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAB85862.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE000666; AAB85861.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE000666; AAB85862.1; ALT_FRAME; Genomic_DNA.
DR   PIR; C69051; C69051.
DR   PDB; 2K50; NMR; -; A=62-167.
DR   PDBsum; 2K50; -.
DR   AlphaFoldDB; O27438; -.
DR   SMR; O27438; -.
DR   STRING; 187420.MTH_1385; -.
DR   DNASU; 1471102; -.
DR   EnsemblBacteria; AAB85861; AAB85861; MTH_1384.
DR   EnsemblBacteria; AAB85862; AAB85862; MTH_1385.
DR   KEGG; mth:MTH_1384; -.
DR   KEGG; mth:MTH_1385; -.
DR   PATRIC; fig|187420.15.peg.1350; -.
DR   HOGENOM; CLU_1485916_0_0_2; -.
DR   EvolutionaryTrace; O27438; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 6.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR013955; Rep_factor-A_C.
DR   Pfam; PF08646; Rep_fac-A_C; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 3.
DR   SUPFAM; SSF50249; SSF50249; 6.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA repair; DNA replication; DNA-binding;
KW   Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..792
FT                   /note="Replication factor A"
FT                   /id="PRO_0000429010"
FT   DNA_BIND        81..140
FT                   /note="OB 1"
FT   DNA_BIND        192..273
FT                   /note="OB 2"
FT   DNA_BIND        301..365
FT                   /note="OB 3"
FT   DNA_BIND        422..494
FT                   /note="OB 4"
FT   ZN_FING         678..696
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:2K50"
FT   STRAND          78..88
FT                   /evidence="ECO:0007829|PDB:2K50"
FT   STRAND          103..111
FT                   /evidence="ECO:0007829|PDB:2K50"
FT   STRAND          114..121
FT                   /evidence="ECO:0007829|PDB:2K50"
FT   HELIX           124..129
FT                   /evidence="ECO:0007829|PDB:2K50"
FT   STRAND          135..144
FT                   /evidence="ECO:0007829|PDB:2K50"
FT   STRAND          148..151
FT                   /evidence="ECO:0007829|PDB:2K50"
FT   STRAND          153..156
FT                   /evidence="ECO:0007829|PDB:2K50"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:2K50"
SQ   SEQUENCE   792 AA;  90209 MW;  E3D052AD0C80CA01 CRC64;
     MKEELKREYE RIKDRISPEE FEELIEKKKE ELGDIGFMDD LTIASTVVDD ILKEKNTMLS
     EKPEHRMDTI SKLEEGAETP VTGRVMKISS PRTFTTRKGR EGKLANVIIA DDTGELRAVF
     WTENIKLLKK FREGDVIRIK DVNIRGGFGG RKEAHLMPRS TVEVLDPEDY PEFPEYREEI
     TPIGDLVEDD EVNVIARITG VSRVRTFERD GREGRFISLD IMDATGSTTY TLWNNDVNLV
     EELGLKEGDA VKILWAQPRR RDDKVTLTHT SLTRVVPGEY DVPEFREELV KIGDLHEMRN
     VTVMGLVTKV NDPVEFERND GTTGSVKSIE IADDTGSARV TLWDEDTRIK INKGDIIRIS
     GANVEFDDFN QSYRINTNFN TRITLNPESD GALLKVLEEY REQMRPMKIS EILEMEDEGE
     EVDVVGRIFS LSDPREFERE DGTGIVRSME LADETGKIRI SLWDEKAEKP MNIGDAVRIE
     NARIRLGLYS VELSAGRTTR IVNPLPEDME DLPSFEELEE MLYQTKKIAD LEEDDRNIRI
     IARVVDLFEP REFQRGDGTP GLVRTAEFAD DTGSIRASLW DDAAEKPLSI GDPVKIENPR
     VVFRDDMGGG RLELSIGNSS RIEPASERDL EGLPSFDELQ EMLYPHRDIA DLDEDSRNVL
     IEGELIEMSG RRILSIKCPS CNERLDLSDE NICNFCGELV DEPRYLLMIP GRIMDDTGEV
     MITFFGREAE SILEMTTDEV VNIINQSADE SALEERVEDL NGVTVRVIGN ADMDVYSEEL
     RFIPRKVVKK EL