ID A0A1W0A8K1_9STRA Unreviewed; 794 AA.
AC A0A1W0A8K1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA repair and recombination protein RadA {ECO:0000256|ARBA:ARBA00018144};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=THRCLA_01327 {ECO:0000313|EMBL:OQS06637.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS06637.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS06637.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS06637.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC Evidence={ECO:0000256|ARBA:ARBA00023529};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
CC {ECO:0000256|ARBA:ARBA00007095}.
CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC {ECO:0000256|ARBA:ARBA00008050}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQS06637.1}.
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DR EMBL; JNBS01000320; OQS06637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0A8K1; -.
DR STRING; 74557.A0A1W0A8K1; -.
DR OrthoDB; 5477610at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19513; Rad51; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011941; DNA_recomb/repair_Rad51.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR NCBIfam; TIGR02239; recomb_RAD51; 1.
DR NCBIfam; TIGR02236; recomb_radA; 1.
DR PANTHER; PTHR22942:SF39; DNA REPAIR PROTEIN RAD51 HOMOLOG 1; 1.
DR PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF08423; Rad51; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003422};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003422}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..794
FT /note="DNA repair and recombination protein RadA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012009072"
FT DOMAIN 554..725
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 731..794
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 397
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 794 AA; 84773 MW; 084698FF026CDC79 CRC64;
MTFHHYLVLA TVAASVLAAD TEKIQSSLAQ QLESSNNANI IIEFNGRAEN VLAESAKLES
AHIATRAERA ELVRSVLVDH ATSTQANALK LIQNKKQEES LAVEPKQLWI SNSIAIANAP
KNLVQELAKL PEVVTIRREA MGRLITSEVT VDVVAANSTE WGLNMIQAPE VWAKGYKGQG
VVVGSIDTGA RGTHEAIKDN FRKENGYFQP EGHSPVPVDN NGHGTHTVGT SVGGKGVGVA
PEAKWISCEG CLPSGKCPES VLVACAQFML CPHDSEGKNP RCDLAPHVVN NSWGDDDEIP
DVPYYKGPMA AWRKAGIIPV FANANNGPKC GTVLSPGDYD NVIGVGATTS KDGLASFSSK
GPNKYGRMKP DISAPGQGVR SSYKTSDTSY ASLSGTSMAT PHVTGAIALM ISAKPGITYD
EIYSLLTTTV ETKSLQNDPL TCGGLSGDNM SSGAMMMNSR YEAAEEEMDH GAAQIQGPCG
IAALEQSGIN ASDINKLKDS GFHTVDAIAM ATKKQLIGIK GITEAKADKM LKAARDMVNV
GFTTASDVMQ SRKDLITLTT GSTAVDELLR GGFETGSITE IFGEFRTGKT QLCHQLCVTC
QLPVDKGGGE GKALFIDTEG TFRPQRLVAI AERYGLDGDS VLDNVAFARA YNSEHQMQLL
SQASAMMAES RYALVVVDSA TALFRTDYSG RGELAARQQE LAKFLRALTR MADEFGVAVV
ITNQMTANPD SGMFAKDPLQ PIGGNIMAHA SCTRLRLKKA RGENRVMKVV DSPILPEAEA
MYSITEQGIQ DEQN
//
