RADA_PYRHO
ID RADA_PYRHO Reviewed; 529 AA.
AC O58001;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=DNA repair and recombination protein RadA;
DE Contains:
DE RecName: Full=Pho RadA intein;
GN Name=radA; OrderedLocusNames=PH0263;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Involved in DNA repair and in homologous recombination. Binds
CC and assemble on single-stranded DNA to form a nucleoprotein filament.
CC Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand
CC exchange between homologous DNA molecules (By similarity).
CC {ECO:0000250}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
CC -!- MISCELLANEOUS: The intein interrupts the ATP-binding site.
CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC {ECO:0000305}.
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DR EMBL; BA000001; BAA29335.1; -; Genomic_DNA.
DR PIR; H71450; H71450.
DR PDB; 2LQM; NMR; -; A=153-324.
DR PDB; 4E2T; X-ray; 1.75 A; A/B=153-324.
DR PDB; 4E2U; X-ray; 1.58 A; A=151-324.
DR PDBsum; 2LQM; -.
DR PDBsum; 4E2T; -.
DR PDBsum; 4E2U; -.
DR AlphaFoldDB; O58001; -.
DR BMRB; O58001; -.
DR SMR; O58001; -.
DR STRING; 70601.3256652; -.
DR EnsemblBacteria; BAA29335; BAA29335; BAA29335.
DR KEGG; pho:PH0263; -.
DR eggNOG; arCOG00415; Archaea.
DR OMA; KRTKASY; -.
DR BRENDA; 3.6.4.B7; 5244.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00348; RadA_arch; 1.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR011938; DNA_recomb/repair_RadA.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 2.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR TIGRFAMs; TIGR02236; recomb_radA; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS50162; RECA_2; 2.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Autocatalytic cleavage; DNA damage;
KW DNA recombination; DNA-binding; Nucleotide-binding; Protein splicing.
FT CHAIN 1..152
FT /note="DNA repair and recombination protein RadA, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030161"
FT CHAIN 153..324
FT /note="Pho RadA intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030162"
FT CHAIN 325..529
FT /note="DNA repair and recombination protein RadA, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030163"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:4E2U"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:4E2U"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 219..233
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:4E2U"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:4E2U"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:4E2T"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4E2T"
FT STRAND 285..307
FT /evidence="ECO:0007829|PDB:4E2U"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:4E2U"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4E2U"
SQ SEQUENCE 529 AA; 58949 MW; 1003B397D1A51567 CRC64;
MMIMVKKGSD PEVVEIDEIE GLGLELEEES TTSKKKKKEK EIKSIEDLPG VGPATAEKLR
EAGFDTLEAI AVASPIELKE VAGISEGAAL KIIQAARKAA NLGTFMRADE YLKKRESIGR
ISTGSKSLDK LLGGGIETQA ITEVFGEFGS GKCFARDTEV YYENDTVPHM ESIEEMYSKY
ASMNGELPFD NGYAVPLDNV FVYTLDIASG EIKKTRASYI YREKVEKLIE IKLSSGYSLK
VTPSHPVLLF RDGLQWVPAA EVKPGDVVVG VREEVLRRRI ISKGELEFHE VSSVRIIDYN
NWVYDLVIPE THNFIAPNGL VLHNTQLAHT LAVMVQLPPE EGGLNGSVIW IDTENTFRPE
RIREIAKNRG LDPDEVLKHI YVARAFNSNH QMLLVQQAED KIKELLNTDK PVKLLIVDSL
TSHFRSEYIG RGALAERQQK LAKHLADLHR LANLYEIAVF VTNQVQARPD AFFGDPTRPI
GGHILAHSAT LRVYLRKGKG GKRVARLIDA PHLPEGEAVF RITEKGIED
